ID LDLR_HUMAN Reviewed; 860 AA. AC P01130; B4DII3; B4DJZ8; B4DR00; B4DTQ3; C0JYY8; H0YLU8; H0YNT7; AC Q53ZD9; Q59FQ1; Q9UDH7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 13-FEB-2019, entry version 236. DE RecName: Full=Low-density lipoprotein receptor; DE Short=LDL receptor; DE Flags: Precursor; GN Name=LDLR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP FUNCTION. RX PubMed=6091915; DOI=10.1016/0092-8674(84)90188-0; RA Yamamoto T., Davis C.G., Brown M.S., Schneider W.J., Casey M.L., RA Goldstein J.L., Russell D.W.; RT "The human LDL receptor: a cysteine-rich protein with multiple Alu RT sequences in its mRNA."; RL Cell 39:27-38(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2988123; DOI=10.1126/science.2988123; RA Suedhof T.C., Goldstein J.L., Brown M.S., Russell D.W.; RT "The LDL receptor gene: a mosaic of exons shared with different RT proteins."; RL Science 228:815-822(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Jia S., Lv L., Sun H., Wang Q., Wang H., Zhan L., Yang Z.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6). RC TISSUE=Hippocampus, Placenta, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., RA Toth E.J., Krauss R.M., Nickerson D.A.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP PROTEIN SEQUENCE OF 186-210; 394-405; 441-449; 472-495; 521-541 AND RP 605-617. RC TISSUE=Cervix carcinoma; RX PubMed=8127891; DOI=10.1073/pnas.91.5.1839; RA Hofer F., Gruenberger M., Kowalski H., Machat H., Huettinger M., RA Kuechler E., Blaas D.; RT "Members of the low density lipoprotein receptor family mediate cell RT entry of a minor-group common cold virus."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1839-1842(1994). RN [13] RP FUNCTION, AND GLYCOSYLATION. RX PubMed=3005267; RA Davis C.G., Elhammer A., Russell D.W., Schneider W.J., Kornfeld S., RA Brown M.S., Goldstein J.L.; RT "Deletion of clustered O-linked carbohydrates does not impair function RT of low density lipoprotein receptor in transfected fibroblasts."; RL J. Biol. Chem. 261:2828-2838(1986). RN [14] RP MUTAGENESIS OF CYTOPLASMIC DOMAIN, AND SUBCELLULAR LOCATION. RX PubMed=3104336; RA Davis C.G., van Driel I.R., Russell D.W., Brown M.S., Goldstein J.L.; RT "The low density lipoprotein receptor. Identification of amino acids RT in cytoplasmic domain required for rapid endocytosis."; RL J. Biol. Chem. 262:4075-4082(1987). RN [15] RP FUNCTION (MICROBIAL INFECTION) AS RECEPTOR OF HEPATITIS C VIRUS. RX PubMed=10535997; DOI=10.1073/pnas.96.22.12766; RA Agnello V., Abel G., Elfahal M., Knight G.B., Zhang Q.X.; RT "Hepatitis C virus and other flaviviridae viruses enter cells via low RT density lipoprotein receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 96:12766-12771(1999). RN [16] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT. RX PubMed=11100124; DOI=10.1038/82199; RA Liu Y., Jones M., Hingtgen C.M., Bu G., Laribee N., Tanzi R.E., RA Moir R.D., Nath A., He J.J.; RT "Uptake of HIV-1 tat protein mediated by low-density lipoprotein RT receptor-related protein disrupts the neuronal metabolic balance of RT the receptor ligands."; RL Nat. Med. 6:1380-1387(2000). RN [17] RP INTERACTION WITH LDLRAP1. RX PubMed=12221107; DOI=10.1074/jbc.M208539200; RA He G., Gupta S., Yi M., Michaely P., Hobbs H.H., Cohen J.C.; RT "ARH is a modular adaptor protein that interacts with the LDL RT receptor, clathrin, and AP-2."; RL J. Biol. Chem. 277:44044-44049(2002). RN [18] RP INTERACTION WITH ARRB1, AND MUTAGENESIS OF TYR-828 AND SER-854. RX PubMed=12944399; DOI=10.1074/jbc.M309450200; RA Wu J.-H., Peppel K., Nelson C.D., Lin F.-T., Kohout T.A., Miller W.E., RA Exum S.T., Freedman N.J.; RT "The adaptor protein beta-arrestin2 enhances endocytosis of the low RT density lipoprotein receptor."; RL J. Biol. Chem. 278:44238-44245(2003). RN [19] RP GLYCOSYLATION AT ASN-657. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [20] RP FUNCTION (MICROBIAL INFECTION) AS RECEPTOR OF HEPATITIS C VIRUS. RX PubMed=12615904; DOI=10.1084/jem.20021756; RA Bartosch B., Dubuisson J., Cosset F.-L.; RT "Infectious hepatitis C virus pseudo-particles containing functional RT E1-E2 envelope protein complexes."; RL J. Exp. Med. 197:633-642(2003). RN [21] RP INTERACTION WITH SNX17. RX PubMed=14739284; DOI=10.1074/jbc.M313689200; RA Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.; RT "Sorting motifs in the intracellular domain of the low density RT lipoprotein receptor interact with a novel domain of sorting nexin- RT 17."; RL J. Biol. Chem. 279:16237-16245(2004). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [24] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PCSK9. RX PubMed=17461796; DOI=10.1111/j.1600-0854.2007.00562.x; RA Nassoury N., Blasiole D.A., Tebon Oler A., Benjannet S., Hamelin J., RA Poupon V., McPherson P.S., Attie A.D., Prat A., Seidah N.G.; RT "The cellular trafficking of the secretory proprotein convertase PCSK9 RT and its dependence on the LDLR."; RL Traffic 8:718-732(2007). RN [25] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [26] RP SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANT SAINT RP OMER ASP-546, MUTAGENESIS OF LYS-811; LYS-816; LYS-830 AND CYS-839, RP UBIQUITINATION, AND REGION. RX PubMed=19520913; DOI=10.1126/science.1168974; RA Zelcer N., Hong C., Boyadjian R., Tontonoz P.; RT "LXR regulates cholesterol uptake through Idol-dependent RT ubiquitination of the LDL receptor."; RL Science 325:100-104(2009). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP INTERACTION WITH PCSK9. RX PubMed=21149300; DOI=10.1074/jbc.M110.199042; RA Yamamoto T., Lu C., Ryan R.O.; RT "A two-step binding model of PCSK9 interaction with the low density RT lipoprotein receptor."; RL J. Biol. Chem. 286:5464-5470(2011). RN [29] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VESICULAR RP STOMATITIS VIRUS GLYCOPROTEIN. RX PubMed=23589850; DOI=10.1073/pnas.1214441110; RA Finkelshtein D., Werman A., Novick D., Barak S., Rubinstein M.; RT "LDL receptor and its family members serve as the cellular receptors RT for vesicular stomatitis virus."; RL Proc. Natl. Acad. Sci. U.S.A. 110:7306-7311(2013). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [32] RP STRUCTURE BY NMR OF 20-67. RX PubMed=7603991; DOI=10.1073/pnas.92.14.6334; RA Daly N.L., Scanlon M.J., Djordjevic J.T., Kroon P.A., Smith R.; RT "Three-dimensional structure of a cysteine-rich repeat from the low- RT density lipoprotein receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 92:6334-6338(1995). RN [33] RP STRUCTURE BY NMR OF 65-104. RX PubMed=7578052; DOI=10.1021/bi00044a025; RA Daly N.L., Djordjevic J.T., Kroon P.A., Smith R.; RT "Three-dimensional structure of the second cysteine-rich repeat from RT the human low-density lipoprotein receptor."; RL Biochemistry 34:14474-14481(1995). RN [34] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 196-232. RX PubMed=9262405; DOI=10.1038/41798; RA Fass D., Blacklow S.C., Kim P.S., Berger J.M.; RT "Molecular basis of familial hypercholesterolaemia from structure of RT LDL receptor module."; RL Nature 388:691-693(1997). RN [35] RP STRUCTURE BY NMR OF 20-104, AND DISULFIDE BONDS. RX PubMed=10933493; DOI=10.1110/ps.9.7.1282; RA Kurniawan N.D., Atkins A.R., Bieri S., Brown C.J., Brereton I.M., RA Kroon P.A., Smith R.; RT "NMR structure of a concatemer of the first and second ligand-binding RT modules of the human low-density lipoprotein receptor."; RL Protein Sci. 9:1282-1293(2000). RN [36] RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 22-720, AND DISULFIDE BONDS. RX PubMed=12459547; DOI=10.1126/science.1078124; RA Rudenko G., Henry L., Henderson K., Ichtchenko K., Brown M.S., RA Goldstein J.L., Deisenhofer J.; RT "Structure of the LDL receptor extracellular domain at endosomal pH."; RL Science 298:2353-2358(2002). RN [37] RP X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 819-832 IN COMPLEX WITH RP LDLRAP1, INTERACTION WITH LDLRAP1, CHARACTERIZATION OF VARIANT FH RP CYS-828, MUTAGENESIS OF ILE-821 AND GLN-829, TOPOLOGY, AND MOTIF. RX PubMed=22509010; DOI=10.1073/pnas.1114128109; RA Dvir H., Shah M., Girardi E., Guo L., Farquhar M.G., Zajonc D.M.; RT "Atomic structure of the autosomal recessive hypercholesterolemia RT phosphotyrosine-binding domain in complex with the LDL-receptor RT tail."; RL Proc. Natl. Acad. Sci. U.S.A. 109:6916-6921(2012). RN [38] RP REVIEW ON FH VARIANTS. RX PubMed=1301956; DOI=10.1002/humu.1380010602; RA Hobbs H.H., Brown M.S., Goldstein J.L.; RT "Molecular genetics of the LDL receptor gene in familial RT hypercholesterolemia."; RL Hum. Mutat. 1:445-466(1992). RN [39] RP REVIEW ON FH VARIANTS. RX PubMed=9016531; DOI=10.1093/nar/25.1.172; RA Varret M., Rabes J.-P., Collod-Beroud G., Junien J., Boileau C., RA Beroud C.; RT "Software and database for the analysis of mutations in the human LDL RT receptor gene."; RL Nucleic Acids Res. 25:172-180(1997). RN [40] RP VARIANT FH 47-ASP-GLY-48 DEL. RX PubMed=3263645; DOI=10.1073/pnas.85.21.7912; RA Leitersdorf E., Hobbs H.H., Fourie A.M., Jacobs M., RA van der Westhuyzen D.R., Coetzee G.A.; RT "Deletion in the first cysteine-rich repeat of low density lipoprotein RT receptor impairs its transport but not lipoprotein binding in RT fibroblasts from a subject with familial hypercholesterolemia."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7912-7916(1988). RN [41] RP VARIANTS FH ASN-175; GLU-227 AND MET-429. RX PubMed=2569482; DOI=10.1172/JCI114258; RA Leitersdorf E., van der Westhuyzen D.R., Coetzee G.A., Hobbs H.H.; RT "Two common low density lipoprotein receptor gene mutations cause RT familial hypercholesterolemia in Afrikaners."; RL J. Clin. Invest. 84:954-961(1989). RN [42] RP VARIANT FH CYS-828. RX PubMed=3955657; DOI=10.1016/0092-8674(86)90533-7; RA Davis C.G., Lehrman M.A., Russell D.W., Anderson R.G.W., Brown M.S., RA Goldstein J.L.; RT "The J.D. mutation in familial hypercholesterolemia: amino acid RT substitution in cytoplasmic domain impedes internalization of LDL RT receptors."; RL Cell 45:15-24(1986). RN [43] RP VARIANTS FH TYR-90 AND LYS-140. RX PubMed=8347689; DOI=10.1016/0925-4439(93)90156-U; RA Rubinsztein D.C., Jialal I., Leitersdorf E., Coetzee G.A., RA van der Westhuyzen D.R.; RT "Identification of two new LDL-receptor mutations causing homozygous RT familial hypercholesterolemia in a South African of Indian origin."; RL Biochim. Biophys. Acta 1182:75-82(1993). RN [44] RP VARIANTS FH GLY-87; LYS-228 AND TYR-667. RX PubMed=2318961; DOI=10.1172/JCI114531; RA Leitersdorf E., Tobin E.J., Davignon J., Hobbs H.H.; RT "Common low-density lipoprotein receptor mutations in the French RT Canadian population."; RL J. Clin. Invest. 85:1014-1023(1990). RN [45] RP VARIANT FH HIS-433. RX PubMed=1446662; DOI=10.1111/j.1432-1033.1992.tb17383.x; RA Miyake Y., Tajima S., Funahashi T., Yamamura T., Yamamoto A.; RT "A point mutation of low-density-lipoprotein receptor causing rapid RT degradation of the receptor."; RL Eur. J. Biochem. 210:1-7(1992). RN [46] RP VARIANT FH GLY-218 DEL. RX PubMed=1867200; RA Meiner V., Landsberger D., Berkman N., Reshef A., Segal P., RA Seftel H.C., van der Westhuyzen D.R., Jeenah M.S., Coetzee G.A., RA Leitersdorf E.; RT "A common Lithuanian mutation causing familial hypercholesterolemia in RT Ashkenazi Jews."; RL Am. J. Hum. Genet. 49:443-449(1991). RN [47] RP VARIANT FH HIS-168. RX PubMed=8462973; DOI=10.1007/BF00222714; RA Leitersdorf E., Reshef A., Meiner V., Dann E.J., Beigel Y., RA van Roggen F.G., van der Westhuyzen D.R., Coetzee G.A.; RT "A missense mutation in the low density lipoprotein receptor gene RT causes familial hypercholesterolemia in Sephardic Jews."; RL Hum. Genet. 91:141-147(1993). RN [48] RP VARIANT FH PHE-318. RX PubMed=8168830; DOI=10.1007/BF00202819; RA Lelli N., Garuti R., Pedrazzi P., Ghisellini M., Simone M.L., RA Tiozzo R., Cattin L., Valenti M., Rolleri M., Bertolini S., RA Stefanutti C., Calandra S.; RT "A new missense mutation (Cys297-->Phe) of the low density lipoprotein RT receptor in Italian patients with familial hypercholesterolemia RT (FHTrieste)."; RL Hum. Genet. 93:538-540(1994). RN [49] RP VARIANT FH LEU-685. RX PubMed=2726768; DOI=10.1073/pnas.86.11.4166; RA Soutar A.K., Knight B.L., Patel D.D.; RT "Identification of a point mutation in growth factor repeat C of the RT low density lipoprotein-receptor gene in a patient with homozygous RT familial hypercholesterolemia that affects ligand binding and RT intracellular movement of receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4166-4170(1989). RN [50] RP VARIANT FH LEU-685. RX PubMed=1464748; RA Rubinsztein D.C., Coetzee G.A., Marais A.D., Leitersdorf E., RA Seftel H.C., van der Westhuyzen D.R.; RT "Identification and properties of the proline664-leucine mutant LDL RT receptor in South Africans of Indian origin."; RL J. Lipid Res. 33:1647-1655(1992). RN [51] RP VARIANTS FH PORI HIS-401 AND TURKU ASP-844. RX PubMed=7573037; RA Koivisto U.-M., Viikari J.S., Kontula K.; RT "Molecular characterization of minor gene rearrangements in Finnish RT patients with heterozygous familial hypercholesterolemia: RT identification of two common missense mutations (Gly823-->Asp and RT Leu380-->His) and eight rare mutations of the LDL receptor gene."; RL Am. J. Hum. Genet. 57:789-797(1995). RN [52] RP VARIANTS FH LYS-140; SER-338 AND LEU-685. RX PubMed=7583548; DOI=10.1161/01.ATV.15.10.1713; RA Maruyama T., Miyake Y., Tajima S., Harada-Shiba M., Yamamura T., RA Tsushima M., Kishino B., Horiguchi Y., Funahashi T., Matsuzawa Y., RA Yamamoto A.; RT "Common mutations in the low-density-lipoprotein-receptor gene causing RT familial hypercholesterolemia in the Japanese population."; RL Arterioscler. Thromb. Vasc. Biol. 15:1713-1718(1995). RN [53] RP VARIANT FH FRENCH HIS-564. RX PubMed=7550239; DOI=10.1002/humu.1380060117; RA Tricot-Guerber F., Saint-Jore B., Valenti K., Foulon T., Bost M., RA Hadjian A.J.; RT "Identification of a mutation, N543H, in exon 11 of the low-density RT lipoprotein receptor gene in a French family with familial RT hypercholesterolemia."; RL Hum. Mutat. 6:87-88(1995). RN [54] RP VARIANTS FH LYS-277; THR-423 AND ASN-579. RX PubMed=7635461; DOI=10.1007/BF00207370; RA Ekstroem U., Abrahamson M., Sveger T., Lombardi P., Nilsson-Ehle P.; RT "An efficient screening procedure detecting six novel mutations in the RT LDL receptor gene in Swedish children with hypercholesterolemia."; RL Hum. Genet. 96:147-150(1995). RN [55] RP VARIANT FH NORWEGIAN ASN-487 DEL. RX PubMed=7635482; DOI=10.1007/BF00207391; RA Leren T.P., Solberg K., Rodningen O.K., Tonstad S., Ose L.; RT "Two novel point mutations in the EGF precursor homology domain of the RT LDL receptor gene causing familial hypercholesterolemia."; RL Hum. Genet. 96:241-242(1995). RN [56] RP VARIANTS FH COLOGNE GLY-221; TYR-221 AND VAL-224. RX PubMed=7649546; RA Geisel J., Holzem G., Oette K.; RT "Screening for mutations in exon 4 of the LDL receptor gene in a RT German population with severe hypercholesterolemia."; RL Hum. Genet. 96:301-304(1995). RN [57] RP VARIANTS FH LA HABANA LYS-277; MET-429 AND MET-797. RX PubMed=7649549; DOI=10.1007/BF00210415; RA Pereira E., Ferreira R., Hermelin B., Thomas G., Bernard C., RA Bertrand V., Nassiff H., Mendez del Castillo D., Bereziat G., RA Benlian P.; RT "Recurrent and novel LDL receptor gene mutations causing heterozygous RT familial hypercholesterolemia in La Habana."; RL Hum. Genet. 96:319-322(1995). RN [58] RP VARIANTS FH TYR-168 AND ARG-366. RX PubMed=8740918; RA Gundersen K.E., Solberg K., Rodningen O.K., Tonstad S., Ose L., RA Berg K., Leren T.P.; RT "Two novel missense mutations in the LDL receptor gene causing RT familial hypercholesterolemia."; RL Clin. Genet. 49:85-87(1996). RN [59] RP VARIANT FH GLY-231. RX PubMed=8664907; RX DOI=10.1002/(SICI)1098-1004(1996)7:1<70::AID-HUMU12>3.3.CO;2-G; RA Sundvold H., Solberg K., Tonstad S., Rodningen O.K., Ose L., Berg K., RA Leren T.P.; RT "A common missense mutation (C210G) in the LDL receptor gene among RT Norwegian familial hypercholesterolemia subjects."; RL Hum. Mutat. 7:70-71(1996). RN [60] RP VARIANTS FH ARG-197; TYR-248; ALA-301; TRP-302 AND PRO-350. RX PubMed=9026534; RA Webb J.C., Sun X.-M., McCarthy S.N., Neuwirth C., Thompson G.R., RA Knigh B., Soutar A.K.; RT "Characterization of mutations in the low density lipoprotein (LDL)- RT receptor gene in patients with homozygous familial RT hypercholesterolemia, and frequency of these mutations in FH patients RT in the United Kingdom."; RL J. Lipid Res. 37:368-381(1996). RN [61] RP VARIANT FH LEU-685. RX PubMed=9254862; DOI=10.1007/s004390050503; RA Peeters A.V., van Gaal L.F., du Plessis L., Lombardi M.P.R., RA Havekes L.M., Kotze M.J.; RT "Mutational and genetic origin of LDL receptor gene mutations detected RT in both Belgian and Dutch familial hypercholesterolemics."; RL Hum. Genet. 100:266-270(1997). RN [62] RP VARIANTS FH HIS-564 AND 799-LEU--PHE-801 DEL. RX PubMed=9143924; RX DOI=10.1002/(SICI)1098-1004(1997)9:5<437::AID-HUMU10>3.0.CO;2-3; RA Jensen H.K., Jensen T.G., Faergeman O., Jensen L.G., Andresen B.S., RA Corydon M.J., Andreasen P.H., Hansen P.S., Heath F., Bolund L., RA Gregersen N.; RT "Two mutations in the same low-density lipoprotein receptor allele act RT in synergy to reduce receptor function in heterozygous familial RT hypercholesterolemia."; RL Hum. Mutat. 9:437-444(1997). RN [63] RP VARIANTS FH TRP-27; CYS-78; GLY-87; TYR-89; ASN-90; GLY-90; LYS-101; RP TYR-160; ASN-168; LEU-177; GLY-221; GLU-227; ARG-286; TYR-313; RP TYR-327; ASN-342; PRO-350; ASP-399; TRP-416; HIS-482; ARG-483; RP SER-526; ASP-549; CYS-633; LEU-649 AND ILE-726. RX PubMed=9259195; RX DOI=10.1002/(SICI)1098-1004(1997)10:2<116::AID-HUMU4>3.3.CO;2-#; RA Day I.N.M., Whittall R.A., O'Dell S.D., Haddad L., Bolla M.K., RA Gudnason V., Humphries S.E.; RT "Spectrum of LDL receptor gene mutations in heterozygous familial RT hypercholesterolemia."; RL Hum. Mutat. 10:116-127(1997). RN [64] RP VARIANTS FH PRO-56; TYR-175; TYR-356; VAL-401 AND TRP-416. RX PubMed=9104431; DOI=10.1046/j.1365-2796.1997.78119000.x; RA Leren T.P., Tonstad S., Gundersen K.E., Bakken K.S., Rodningen O.K., RA Sundvold H., Ose L., Berg K.; RT "Molecular genetics of familial hypercholesterolaemia in Norway."; RL J. Intern. Med. 241:185-194(1997). RN [65] RP VARIANTS FH LEU-177; GLY-218 DEL; SER-564 AND GLU-592. RX PubMed=9654205; DOI=10.1007/s004390050740; RA Gorski B., Kubalska J., Naruszewicz M., Lubinski J.; RT "LDL-R and Apo-B-100 gene mutations in Polish familial RT hypercholesterolemias."; RL Hum. Genet. 102:562-565(1998). RN [66] RP VARIANTS FH TRP-173 AND ARG-368. RX PubMed=9452094; RA Couture P., Vohl M.-C., Gagne C., Gaudet D., Torres A.L., Lupien P.J., RA Despres J.-P., Labrie F., Simard J., Moorjani S.; RT "Identification of three mutations in the low-density lipoprotein RT receptor gene causing familial hypercholesterolemia among French RT Canadians."; RL Hum. Mutat. Suppl. 1:S226-S231(1998). RN [67] RP VARIANTS FH GLN-416 AND MET-429. RX PubMed=9452095; RA Thiart R., Loubser O., de Villiers J.N.P., Marx M.P., Zaire R., RA Raal F.J., Kotze M.J.; RT "Two novel and two known low-density lipoprotein receptor gene RT mutations in German patients with familial hypercholesterolemia."; RL Hum. Mutat. Suppl. 1:S232-S233(1998). RN [68] RP VARIANTS FH TYR-329; ARG-414 AND MET-429. RX PubMed=9452118; RA Mak Y.T., Zhang J., Chan Y.S., Mak T.W.L., Tomlinson B., RA Masarei J.R.L., Pang C.P.; RT "Possible common mutations in the low density lipoprotein receptor RT gene in Chinese."; RL Hum. Mutat. Suppl. 1:S310-S313(1998). RN [69] RP VARIANTS FH GLU-92; GLY-95; ARG-116; LEU-177; GLY-221; TYR-221; RP LYS-277; TYR-302; LYS-434; TYR-667 AND GLU-700. RX PubMed=10206683; RX DOI=10.1002/(SICI)1098-1004(1998)11:5<413::AID-HUMU17>3.3.CO;2-6; RA Cenarro A., Jensen H.K., Casao E., Civeira F., Gonzalez-Bonillo J., RA Rodriguez-Rey J.C., Gregersen N., Pocovi M.; RT "Identification of recurrent and novel mutations in the LDL receptor RT gene in Spanish patients with familial hypercholesterolemia."; RL Hum. Mutat. 11:413-413(1998). RN [70] RP VARIANT FH CHIETI-3 GLU-228 DELINS CYS-LYS. RX PubMed=10660340; RA Motti C., Bertolini S., Rampa P., Trovatello G., Liberatoscioli L., RA Calandra S., Federici G., Cortese C.; RT "Two novel mutations consisting in minor gene rearrangements in the RT human low density lipoprotein receptor gene in Italian patients RT affected by familial hypercholesterolemia."; RL Hum. Mutat. 12:290-290(1998). RN [71] RP VARIANT FH TYR-276. RA Vergopoulos A., Bajari T., Jouma M., Aydin A., Boehring S., Luft F.C., RA Schuster H.; RT "A novel single amino acid substitution in exon 6 of the low-density RT lipoprotein receptor gene in a Syrian family."; RL Hum. Mutat. 12:365-365(1998). RN [72] RP VARIANTS FH TYR-379 AND SER-608. RX PubMed=9852677; DOI=10.1007/s100380050083; RA Hirayama T., Yamaki E., Hata A., Tsuji M., Hashimoto K., Yamamoto M., RA Emi M.; RT "Five familial hypercholesterolemic kindreds in Japan with novel RT mutations of the LDL receptor gene."; RL J. Hum. Genet. 43:250-254(1998). RN [73] RP VARIANT FH GLASCO TYR-184. RX PubMed=9678702; DOI=10.1136/jmg.35.7.573; RA Lee W.K., Haddad L., Macleod M.J., Dorrance A.M., Wilson D.J., RA Gaffney D., Dominiczak M.H., Packard C.J., Day I.N., Humphries S.E., RA Dominiczak A.F.; RT "Identification of a common low density lipoprotein receptor mutation RT (C163Y) in the west of Scotland."; RL J. Med. Genet. 35:573-578(1998). RN [74] RP VARIANTS FH GLY-87; LYS-140; ASN-172; ARG-243; LEU-306; PRO-404; RP HIS-564; SER-577; ASN-579; ILE-726 AND LYS-825. RX PubMed=10532689; DOI=10.1016/S0021-9150(99)00158-6; RA Jensen H.K., Jensen L.G., Meinertz H., Hansen P.S., Gregersen N., RA Faergeman O.; RT "Spectrum of LDL receptor gene mutations in Denmark: implications for RT molecular diagnostic strategy in heterozygous familial RT hypercholesterolemia."; RL Atherosclerosis 146:337-344(1999). RN [75] RP VARIANT FH PHE-261. RX PubMed=10422803; DOI=10.1034/j.1399-0004.1999.550506.x; RA Ekstroem U., Abrahamson M., Floren C.-H., Tollig H., Wettrell G., RA Nilsson G., Sun X.-M., Soutar A.K., Nilsson-Ehle P.; RT "An individual with a healthy phenotype in spite of a pathogenic LDL RT receptor mutation (C240F)."; RL Clin. Genet. 55:332-339(1999). RN [76] RP VARIANTS FH SER-50; ASN-221; LYS-288; VAL-432 AND HIS-564. RX PubMed=10090484; RX DOI=10.1002/(SICI)1098-1004(1999)13:3<257::AID-HUMU14>3.3.CO;2-4; RA Ebhardt M., Schmidt H., Doerk T., Tietge U., Haas R., Manns M.-P., RA Schmidtke J., Stuhrmann M.; RT "Mutation analysis in 46 German families with familial RT hypercholesterolemia: identification of 8 new mutations."; RL Hum. Mutat. 13:257-257(1999). RN [77] RP VARIANTS FH SER-338; LEU-403; THR-431; VAL-568 AND LYS-714. RX PubMed=10447263; RX DOI=10.1002/(SICI)1098-1004(1999)14:1<87::AID-HUMU13>3.3.CO;2-H; RA Hattori H., Nagano M., Iwata F., Homma Y., Egashira T., Okada T.; RT "Identification of recurrent and novel mutations in the LDL receptor RT gene in Japanese familial hypercholesterolemia."; RL Hum. Mutat. 14:87-87(1999). RN [78] RP VARIANTS ARG-2; ILE-468 AND GLN-814. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [79] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). RN [80] RP VARIANTS FH PHE-134; TRP-134; TYR-222; PRO-254; ARG-276; ARG-318; RP THR-370; GLY-415 AND TYR-579. RX PubMed=10978268; DOI=10.1161/01.ATV.20.9.e41; RA Bertolini S., Cantafora A., Averna M., Cortese C., Motti C., RA Martini S., Pes G., Postiglione A., Stefanutti C., Blotta I., RA Pisciotta L., Rolleri M., Langheim S., Ghisellini M., Rabbone I., RA Calandra S.; RT "Clinical expression of familial hypercholesterolemia in clusters of RT mutations of the LDL receptor gene that cause a receptor-defective or RT receptor-negative phenotype."; RL Arterioscler. Thromb. Vasc. Biol. 20:E41-E52(2000). RN [81] RP VARIANT FH THR-451. RX PubMed=10980548; RX DOI=10.1002/1098-1004(200009)16:3<277::AID-HUMU24>3.0.CO;2-Y; RA Miltiadous G., Elisaf M., Xenophontos S., Manoli P., Cariolou M.A.; RT "Segregation of a novel LDLR gene mutation (I430T) with familial RT hypercholesterolaemia in a Greek pedigree."; RL Hum. Mutat. 16:277-277(2000). RN [82] RP VARIANT FH 47-ASP-GLY-48 DEL, AND VARIANTS HIS-172; TRP-253; GLN-406; RP LYS-408; LEU-699 AND GLN-814. RX PubMed=10882754; DOI=10.1136/jmg.37.7.514; RA Thiart R., Scholtz C.L., Vergotine J., Hoogendijk C.F., RA de Villiers J.N.P., Nissen H., Brusgaard K., Gaffney D., Hoffs M.S., RA Vermaak W.J.H., Kotze M.J.; RT "Predominance of a 6 bp deletion in exon 2 of the LDL receptor gene in RT Africans with familial hypercholesterolaemia."; RL J. Med. Genet. 37:514-519(2000). RN [83] RP VARIANT FH SER-46. RX PubMed=11298688; DOI=10.1034/j.1399-0004.2001.590414.x; RA Takahashi M., Ikeda U., Takahashi S., Hattori H., Iwasaki T., RA Ishihara M., Egashira T., Honma S., Asano Y., Shimada K.A.; RT "A novel mutation in exon 2 of the low-density lipoprotein-receptor RT gene in a patient with homozygous familial hypercholesterolemia."; RL Clin. Genet. 59:290-292(2001). RN [84] RP INVOLVEMENT IN FH, VARIANTS FH ARG-143; TYR-148; TRP-184; CYS-574; RP ASP-639 AND ASP-806, AND VARIANTS TRP-257 AND ILE-742. RX PubMed=11462246; DOI=10.1002/humu.1171; RA Nauck M.S., Koester W., Doerfer K., Eckes J., Scharnagl H., RA Gierens H., Nissen H., Nauck M.A., Wieland H., Maerz W.; RT "Identification of recurrent and novel mutations in the LDL receptor RT gene in German patients with familial hypercholesterolemia."; RL Hum. Mutat. 18:165-166(2001). RN [85] RP VARIANTS FH TYR-89; LYS-101; GLY-218 DEL; GLY-221; ASN-221; TYR-358; RP PRO-479; HIS-482; ARG-677 AND LEU-685, AND FUNCTION. RX PubMed=17142622; DOI=10.1136/jmg.2006.038356; RG Simon Broome familial hyperlipidemia register group and scientific steering committee; RA Humphries S.E., Whittall R.A., Hubbart C.S., Maplebeck S., RA Cooper J.A., Soutar A.K., Naoumova R., Thompson G.R., Seed M., RA Durrington P.N., Miller J.P., Betteridge D.J.B., Neil H.A.W.; RT "Genetic causes of familial hypercholesterolaemia in patients in the RT UK: relation to plasma lipid levels and coronary heart disease risk."; RL J. Med. Genet. 43:943-949(2006). RN [86] RP VARIANTS FH THR-50; LEU-211; GLY-221; GLU-266; LYS-277; ARG-286; RP ARG-314; ARG-352; LYS-408; THR-431; HIS-442; MET-523; GLY-577; THR-585 RP AND LEU-685. RX PubMed=17347910; DOI=10.1007/s10545-007-0563-5; RA Widhalm K., Dirisamer A., Lindemayr A., Kostner G.; RT "Diagnosis of families with familial hypercholesterolaemia and/or Apo RT B-100 defect by means of DNA analysis of LDL-receptor gene RT mutations."; RL J. Inherit. Metab. Dis. 30:239-247(2007). RN [87] RP VARIANTS FH TYR-155; GLY-300; GLY-301; TRP-416 AND ASN-454. RX PubMed=19318025; DOI=10.1016/j.clinbiochem.2009.01.017; RA Alonso R., Defesche J.C., Tejedor D., Castillo S., Stef M., Mata N., RA Gomez-Enterria P., Martinez-Faedo C., Forga L., Mata P.; RT "Genetic diagnosis of familial hypercholesterolemia using a DNA-array RT based platform."; RL Clin. Biochem. 42:899-903(2009). RN [88] RP VARIANTS FH PRO-254; TYR-356; TYR-358; THR-451 AND SER-826. RX PubMed=19319977; DOI=10.1002/humu.21002; RA Abifadel M., Rabes J.-P., Jambart S., Halaby G., Gannage-Yared M.-H., RA Sarkis A., Beaino G., Varret M., Salem N., Corbani S., Aydenian H., RA Junien C., Munnich A., Boileau C.; RT "The molecular basis of familial hypercholesterolemia in Lebanon: RT spectrum of LDLR mutations and role of PCSK9 as a modifier gene."; RL Hum. Mutat. 30:E682-E691(2009). RN [89] RP VARIANTS HIS-139; LYS-201; SER-255; ASN-304 AND GLY-471. RX PubMed=21418584; DOI=10.1186/1471-2350-12-40; RA Al-Khateeb A., Zahri M.K., Mohamed M.S., Sasongko T.H., Ibrahim S., RA Yusof Z., Zilfalil B.A.; RT "Analysis of sequence variations in low-density lipoprotein receptor RT gene among Malaysian patients with familial hypercholesterolemia."; RL BMC Med. Genet. 12:40-40(2011). RN [90] RP VARIANT FH PHE-329. RX PubMed=22160468; DOI=10.1007/s11033-011-1314-0; RA Walus-Miarka M., Sanak M., Idzior-Walus B., Miarka P., Witek P., RA Malecki M.T., Czarnecka D.; RT "A novel mutation (Cys308Phe) of the LDL receptor gene in families RT from the South-Eastern part of Poland."; RL Mol. Biol. Rep. 39:5181-5186(2012). RN [91] RP VARIANTS FH TYR-160; ALA-168; LEU-177; TYR-184; GLY-221; GLN-228; RP LYS-228; TRP-276; TYR-285; GLY-301; PHE-318; CYS-326; SER-343; RP TYR-368; ASP-373; TRP-406; MET-429; ASN-492; ASP-549; HIS-564; RP HIS-574; TRP-595; HIS-601; LEU-685; LEU-699; MET-797 AND GLN-814. RX PubMed=24529145; DOI=10.1016/j.atherosclerosis.2013.12.028; RA Santos P.C., Morgan A.C., Jannes C.E., Turolla L., Krieger J.E., RA Santos R.D., Pereira A.C.; RT "Presence and type of low density lipoprotein receptor (LDLR) mutation RT influences the lipid profile and response to lipid-lowering therapy in RT Brazilian patients with heterozygous familial hypercholesterolemia."; RL Atherosclerosis 233:206-210(2014). RN [92] RP CHARACTERIZATION OF VARIANTS FH ARG-116; ASN-168; ASN-172; GLY-300 AND RP GLY-301, AND CHARACTERIZATION OF VARIANT TRP-257. RX PubMed=25545329; DOI=10.1016/j.atherosclerosis.2014.12.026; RA Etxebarria A., Benito-Vicente A., Stef M., Ostolaza H., Palacios L., RA Martin C.; RT "Activity-associated effect of LDL receptor missense variants located RT in the cysteine-rich repeats."; RL Atherosclerosis 238:304-312(2015). RN [93] RP CHARACTERIZATION OF VARIANTS FH TYR-155; TRP-416; ASN-454; GLY-577 AND RP LYS-825. RX PubMed=25378237; DOI=10.1002/humu.22721; RA Etxebarria A., Benito-Vicente A., Palacios L., Stef M., Cenarro A., RA Civeira F., Ostolaza H., Martin C.; RT "Functional characterization and classification of frequent low- RT density lipoprotein receptor variants."; RL Hum. Mutat. 36:129-141(2015). CC -!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of CC plasma, and transports it into cells by endocytosis. In order to CC be internalized, the receptor-ligand complexes must first cluster CC into clathrin-coated pits. {ECO:0000269|PubMed:3005267, CC ECO:0000269|PubMed:6091915}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C CC virus in hepatocytes, but not through a direct interaction with CC viral proteins. {ECO:0000269|PubMed:10535997, CC ECO:0000269|PubMed:12615904}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Vesicular CC stomatitis virus. {ECO:0000269|PubMed:23589850}. CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, may CC function as a receptor for extracellular Tat in neurons, mediating CC its internalization in uninfected cells. CC {ECO:0000269|PubMed:11100124}. CC -!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain); CC the interaction is impaired by tyrosine phosphorylation of the CC NPXY motif (By similarity). Interacts (via NPXY motif) with CC LDLRAP1 (via PID domain) (PubMed:12221107, PubMed:22509010). CC Interacts with ARRB1 (PubMed:12944399). Interacts with SNX17 CC (PubMed:14739284). Interacts with the full-length immature form of CC PCSK9 (via C-terminus) (PubMed:17461796, PubMed:21149300). CC {ECO:0000250|UniProtKB:P35951, ECO:0000269|PubMed:12221107, CC ECO:0000269|PubMed:12944399, ECO:0000269|PubMed:14739284, CC ECO:0000269|PubMed:17461796, ECO:0000269|PubMed:21149300, CC ECO:0000269|PubMed:22509010}. CC -!- SUBUNIT: (Microbial infection) Interacts with vesicular stomatitis CC virus glycoprotein. {ECO:0000269|PubMed:23589850}. CC -!- SUBUNIT: (Microbial infection) May interact with HIV-1 Tat. CC {ECO:0000269|PubMed:11100124}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-988319, EBI-988319; CC P04114:APOB; NbExp=4; IntAct=EBI-988319, EBI-3926040; CC P02649:APOE; NbExp=2; IntAct=EBI-988319, EBI-1222467; CC P02749:APOH; NbExp=3; IntAct=EBI-988319, EBI-2114682; CC D3ZAR1:Ldlrap1 (xeno); NbExp=3; IntAct=EBI-988319, EBI-9250714; CC Q8NBP7:PCSK9; NbExp=10; IntAct=EBI-988319, EBI-7539251; CC Q8NBP7-1:PCSK9; NbExp=4; IntAct=EBI-988319, EBI-15656131; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17461796, CC ECO:0000269|PubMed:19520913}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit CC {ECO:0000303|PubMed:6091915}. Golgi apparatus CC {ECO:0000269|PubMed:17461796}. Early endosome CC {ECO:0000269|PubMed:17461796}. Late endosome CC {ECO:0000269|PubMed:17461796}. Lysosome CC {ECO:0000269|PubMed:17461796}. Note=Rapidly endocytosed upon CC ligand binding. {ECO:0000269|PubMed:3104336}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=P01130-1; Sequence=Displayed; CC Name=2; CC IsoId=P01130-2; Sequence=VSP_043053, VSP_043054; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P01130-3; Sequence=VSP_055014, VSP_055015; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P01130-4; Sequence=VSP_043595; CC Note=No experimental confirmation available.; CC Name=5; CC IsoId=P01130-5; Sequence=VSP_045525; CC Note=No experimental confirmation available.; CC Name=6; CC IsoId=P01130-6; Sequence=VSP_047413; CC Note=No experimental confirmation available.; CC -!- DOMAIN: The NPXY motif mediates the interaction with the clathrin CC adapter DAB2 and with LDLRAP1 which are involved in receptor CC internalization. A few residues outside the motif also play a role CC in the interaction. {ECO:0000269|PubMed:22509010}. CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:19520913, ECO:0000269|PubMed:3005267}. CC -!- PTM: Ubiquitinated by MYLIP leading to degradation. CC {ECO:0000269|PubMed:19520913}. CC -!- DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: A common CC autosomal dominant disorder characterized by elevated serum low- CC density lipoprotein (LDL) cholesterol levels, which result in CC excess deposition of cholesterol in tissues and leads to CC xanthelasma, xanthomas, accelerated atherosclerosis and increased CC risk of premature coronary heart disease. The disorder occurs in 2 CC clinical forms: a mild form that becomes evident in the fourth or CC fifth decade in individuals carrying heterozygous LDLR mutations; CC a more severe form that usually manifests in the first two decades CC of life in individuals with homozygous LDLR mutations. CC {ECO:0000269|PubMed:10090484, ECO:0000269|PubMed:10206683, CC ECO:0000269|PubMed:10422803, ECO:0000269|PubMed:10447263, CC ECO:0000269|PubMed:10532689, ECO:0000269|PubMed:10660340, CC ECO:0000269|PubMed:10882754, ECO:0000269|PubMed:10978268, CC ECO:0000269|PubMed:10980548, ECO:0000269|PubMed:11298688, CC ECO:0000269|PubMed:11462246, ECO:0000269|PubMed:1446662, CC ECO:0000269|PubMed:1464748, ECO:0000269|PubMed:17142622, CC ECO:0000269|PubMed:17347910, ECO:0000269|PubMed:1867200, CC ECO:0000269|PubMed:19318025, ECO:0000269|PubMed:19319977, CC ECO:0000269|PubMed:22160468, ECO:0000269|PubMed:22509010, CC ECO:0000269|PubMed:2318961, ECO:0000269|PubMed:24529145, CC ECO:0000269|PubMed:25378237, ECO:0000269|PubMed:25545329, CC ECO:0000269|PubMed:2569482, ECO:0000269|PubMed:2726768, CC ECO:0000269|PubMed:3263645, ECO:0000269|PubMed:3955657, CC ECO:0000269|PubMed:7550239, ECO:0000269|PubMed:7573037, CC ECO:0000269|PubMed:7583548, ECO:0000269|PubMed:7635461, CC ECO:0000269|PubMed:7635482, ECO:0000269|PubMed:7649546, CC ECO:0000269|PubMed:7649549, ECO:0000269|PubMed:8168830, CC ECO:0000269|PubMed:8347689, ECO:0000269|PubMed:8462973, CC ECO:0000269|PubMed:8664907, ECO:0000269|PubMed:8740918, CC ECO:0000269|PubMed:9026534, ECO:0000269|PubMed:9104431, CC ECO:0000269|PubMed:9143924, ECO:0000269|PubMed:9254862, CC ECO:0000269|PubMed:9259195, ECO:0000269|PubMed:9452094, CC ECO:0000269|PubMed:9452095, ECO:0000269|PubMed:9452118, CC ECO:0000269|PubMed:9654205, ECO:0000269|PubMed:9678702, CC ECO:0000269|PubMed:9852677, ECO:0000269|Ref.71}. Note=The disease CC is caused by mutations affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92646.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=LDLR; Note=LDLR mutation database; CC URL="http://www.ucl.ac.uk/fh/"; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=LDLR"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; L00352; AAA56833.1; -; Genomic_DNA. DR EMBL; L00336; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00337; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00338; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00339; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00340; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00341; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00343; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00344; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00345; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00346; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00347; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00348; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00349; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00350; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L00351; AAA56833.1; JOINED; Genomic_DNA. DR EMBL; L29401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY114155; AAM56036.1; -; mRNA. DR EMBL; AK295612; BAG58495.1; -; mRNA. DR EMBL; AK296312; BAG59010.1; -; mRNA. DR EMBL; AK299038; BAG61112.1; -; mRNA. DR EMBL; AK300313; BAG62065.1; -; mRNA. DR EMBL; BT007361; AAP36025.1; -; mRNA. DR EMBL; AY324609; AAP72971.1; -; Genomic_DNA. DR EMBL; AB209409; BAD92646.1; ALT_INIT; mRNA. DR EMBL; FJ525879; ACN81317.1; -; Genomic_DNA. DR EMBL; AC011485; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84169.1; -; Genomic_DNA. DR EMBL; BC014514; AAH14514.1; -; mRNA. DR CCDS; CCDS12254.1; -. [P01130-1] DR CCDS; CCDS56083.1; -. [P01130-2] DR CCDS; CCDS56084.1; -. [P01130-3] DR CCDS; CCDS56085.1; -. [P01130-4] DR CCDS; CCDS58651.1; -. [P01130-5] DR PIR; A01383; QRHULD. DR RefSeq; NP_000518.1; NM_000527.4. [P01130-1] DR RefSeq; NP_001182727.1; NM_001195798.1. [P01130-5] DR RefSeq; NP_001182728.1; NM_001195799.1. [P01130-4] DR RefSeq; NP_001182729.1; NM_001195800.1. [P01130-3] DR RefSeq; NP_001182732.1; NM_001195803.1. [P01130-2] DR UniGene; Hs.213289; -. DR UniGene; Hs.713981; -. DR PDB; 1AJJ; X-ray; 1.70 A; A=196-232. DR PDB; 1D2J; NMR; -; A=233-272. DR PDB; 1F5Y; NMR; -; A=22-104. DR PDB; 1F8Z; NMR; -; A=234-272. DR PDB; 1HJ7; NMR; -; A=314-393. DR PDB; 1HZ8; NMR; -; A=314-395. DR PDB; 1I0U; NMR; -; A=314-395. DR PDB; 1IJQ; X-ray; 1.50 A; A/B=398-713. DR PDB; 1LDL; NMR; -; A=20-67. DR PDB; 1LDR; NMR; -; A=64-104. DR PDB; 1LRX; Model; -; B=396-659. DR PDB; 1N7D; X-ray; 3.70 A; A=22-720. DR PDB; 1XFE; NMR; -; A=272-353. DR PDB; 2FCW; X-ray; 1.26 A; B=107-186. DR PDB; 2KRI; NMR; -; B=147-186. DR PDB; 2LGP; NMR; -; A=144-235. DR PDB; 2M7P; NMR; -; A=82-104. DR PDB; 2MG9; NMR; -; A=314-339. DR PDB; 2W2M; X-ray; 2.40 A; E=314-393. DR PDB; 2W2N; X-ray; 2.30 A; E=314-393. DR PDB; 2W2O; X-ray; 2.62 A; E=314-393. DR PDB; 2W2P; X-ray; 2.62 A; E=314-393. DR PDB; 2W2Q; X-ray; 2.33 A; E=314-393. DR PDB; 3BPS; X-ray; 2.41 A; E=314-393. DR PDB; 3GCW; X-ray; 2.70 A; E=314-393. DR PDB; 3GCX; X-ray; 2.70 A; E=314-393. DR PDB; 3M0C; X-ray; 7.01 A; C=4-788. DR PDB; 3P5B; X-ray; 3.30 A; L=316-715. DR PDB; 3P5C; X-ray; 4.20 A; L=276-715. DR PDB; 3SO6; X-ray; 1.37 A; Q=819-832. DR PDB; 4NE9; X-ray; 2.60 A; D=314-339. DR PDB; 5OY9; X-ray; 3.60 A; D=108-144. DR PDB; 5OYL; X-ray; 2.25 A; D=65-106. DR PDBsum; 1AJJ; -. DR PDBsum; 1D2J; -. DR PDBsum; 1F5Y; -. DR PDBsum; 1F8Z; -. DR PDBsum; 1HJ7; -. DR PDBsum; 1HZ8; -. DR PDBsum; 1I0U; -. DR PDBsum; 1IJQ; -. DR PDBsum; 1LDL; -. DR PDBsum; 1LDR; -. DR PDBsum; 1LRX; -. DR PDBsum; 1N7D; -. DR PDBsum; 1XFE; -. DR PDBsum; 2FCW; -. DR PDBsum; 2KRI; -. DR PDBsum; 2LGP; -. DR PDBsum; 2M7P; -. DR PDBsum; 2MG9; -. DR PDBsum; 2W2M; -. DR PDBsum; 2W2N; -. DR PDBsum; 2W2O; -. DR PDBsum; 2W2P; -. DR PDBsum; 2W2Q; -. DR PDBsum; 3BPS; -. DR PDBsum; 3GCW; -. DR PDBsum; 3GCX; -. DR PDBsum; 3M0C; -. DR PDBsum; 3P5B; -. DR PDBsum; 3P5C; -. DR PDBsum; 3SO6; -. DR PDBsum; 4NE9; -. DR PDBsum; 5OY9; -. DR PDBsum; 5OYL; -. DR ProteinModelPortal; P01130; -. DR SMR; P01130; -. DR BioGrid; 110141; 44. DR ComplexPortal; CPX-128; LDLR-PCSK9 complex. DR DIP; DIP-29695N; -. DR ELM; P01130; -. DR IntAct; P01130; 17. DR MINT; P01130; -. DR STRING; 9606.ENSP00000454071; -. DR BindingDB; P01130; -. DR ChEMBL; CHEMBL3311; -. DR DrugBank; DB00707; Porfimer. DR GlyConnect; 343; -. DR iPTMnet; P01130; -. DR PhosphoSitePlus; P01130; -. DR UniCarbKB; P01130; -. DR BioMuta; LDLR; -. DR DMDM; 126073; -. DR EPD; P01130; -. DR jPOST; P01130; -. DR MaxQB; P01130; -. DR PaxDb; P01130; -. DR PeptideAtlas; P01130; -. DR PRIDE; P01130; -. DR ProteomicsDB; 51326; -. DR ProteomicsDB; 51327; -. [P01130-2] DR ProteomicsDB; 51328; -. [P01130-3] DR ProteomicsDB; 51329; -. [P01130-4] DR DNASU; 3949; -. DR Ensembl; ENST00000455727; ENSP00000397829; ENSG00000130164. [P01130-3] DR Ensembl; ENST00000535915; ENSP00000440520; ENSG00000130164. [P01130-4] DR Ensembl; ENST00000545707; ENSP00000437639; ENSG00000130164. [P01130-2] DR Ensembl; ENST00000558013; ENSP00000453346; ENSG00000130164. [P01130-5] DR Ensembl; ENST00000558518; ENSP00000454071; ENSG00000130164. [P01130-1] DR GeneID; 3949; -. DR KEGG; hsa:3949; -. DR UCSC; uc002mqk.5; human. [P01130-1] DR CTD; 3949; -. DR DisGeNET; 3949; -. DR EuPathDB; HostDB:ENSG00000130164.11; -. DR GeneCards; LDLR; -. DR GeneReviews; LDLR; -. DR HGNC; HGNC:6547; LDLR. DR HPA; HPA009647; -. DR HPA; HPA013159; -. DR MalaCards; LDLR; -. DR MIM; 143890; phenotype. DR MIM; 606945; gene. DR neXtProt; NX_P01130; -. DR OpenTargets; ENSG00000130164; -. DR Orphanet; 391665; Homozygous familial hypercholesterolemia. DR Orphanet; 406; NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia. DR PharmGKB; PA227; -. DR eggNOG; ENOG410IPSW; Eukaryota. DR eggNOG; ENOG410Z5FJ; LUCA. DR GeneTree; ENSGT00940000161046; -. DR HOGENOM; HOG000115656; -. DR HOVERGEN; HBG006250; -. DR InParanoid; P01130; -. DR KO; K12473; -. DR OrthoDB; 1152704at2759; -. DR PhylomeDB; P01130; -. DR TreeFam; TF351700; -. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-8964026; Chylomicron clearance. DR Reactome; R-HSA-8964038; LDL clearance. DR Reactome; R-HSA-975634; Retinoid metabolism and transport. DR SIGNOR; P01130; -. DR ChiTaRS; LDLR; human. DR EvolutionaryTrace; P01130; -. DR GeneWiki; LDL_receptor; -. DR GenomeRNAi; 3949; -. DR PRO; PR:P01130; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000130164; Expressed in 222 organ(s), highest expression level in adrenal tissue. DR ExpressionAtlas; P01130; baseline and differential. DR Genevisible; P01130; HS. DR GO; GO:0045177; C:apical part of cell; ISS:BHF-UCL. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0005622; C:intracellular; ISS:ARUK-UCL. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1990666; C:PCSK9-LDLR complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl. DR GO; GO:0097443; C:sorting endosome; IEA:Ensembl. DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0032050; F:clathrin heavy chain binding; TAS:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030169; F:low-density lipoprotein particle binding; IMP:BHF-UCL. DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:BHF-UCL. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL. DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISS:ARUK-UCL. DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl. DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IMP:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL. DR GO; GO:0070508; P:cholesterol import; IMP:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0030301; P:cholesterol transport; IMP:HGNC. DR GO; GO:0034382; P:chylomicron remnant clearance; TAS:Reactome. DR GO; GO:0006897; P:endocytosis; TAS:ProtInc. DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl. DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:HGNC. DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc. DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl. DR GO; GO:0007616; P:long-term memory; IGI:ARUK-UCL. DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISS:ARUK-UCL. DR GO; GO:0061889; P:negative regulation of astrocyte activation; ISS:ARUK-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:1903979; P:negative regulation of microglial cell activation; ISS:ARUK-UCL. DR GO; GO:0051248; P:negative regulation of protein metabolic process; ISS:ARUK-UCL. DR GO; GO:0006909; P:phagocytosis; ISS:ARUK-UCL. DR GO; GO:0015914; P:phospholipid transport; ISS:BHF-UCL. DR GO; GO:0034381; P:plasma lipoprotein particle clearance; ISS:ARUK-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl. DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISS:ARUK-UCL. DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:BHF-UCL. DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL. DR GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IMP:BHF-UCL. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl. DR GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISS:BHF-UCL. DR GO; GO:0051246; P:regulation of protein metabolic process; IGI:ARUK-UCL. DR GO; GO:0061771; P:response to caloric restriction; IGI:ARUK-UCL. DR CDD; cd00112; LDLa; 7. DR Gene3D; 2.120.10.30; -; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR036055; LDL_receptor-like_sf. DR InterPro; IPR023415; LDLR_class-A_CS. DR InterPro; IPR000033; LDLR_classB_rpt. DR InterPro; IPR002172; LDrepeatLR_classA_rpt. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF00057; Ldl_recept_a; 7. DR Pfam; PF00058; Ldl_recept_b; 5. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00181; EGF; 3. DR SMART; SM00179; EGF_CA; 2. DR SMART; SM00192; LDLa; 7. DR SMART; SM00135; LY; 5. DR SUPFAM; SSF57184; SSF57184; 1. DR SUPFAM; SSF57424; SSF57424; 7. DR PROSITE; PS00010; ASX_HYDROXYL; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS01209; LDLRA_1; 7. DR PROSITE; PS50068; LDLRA_2; 7. DR PROSITE; PS51120; LDLRB; 5. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Cholesterol metabolism; Coated pit; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus; KW Host cell receptor for virus entry; Host-virus interaction; LDL; KW Lipid metabolism; Lipid transport; Lysosome; Membrane; Phosphoprotein; KW Polymorphism; Receptor; Reference proteome; Repeat; Signal; KW Steroid metabolism; Sterol metabolism; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation. FT SIGNAL 1 21 {ECO:0000250|UniProtKB:P01131}. FT CHAIN 22 860 Low-density lipoprotein receptor. FT /FTId=PRO_0000017312. FT TOPO_DOM 22 788 Extracellular. FT {ECO:0000250|UniProtKB:P01131}. FT TRANSMEM 789 810 Helical. {ECO:0000255}. FT TOPO_DOM 811 860 Cytoplasmic. FT {ECO:0000269|PubMed:22509010}. FT DOMAIN 25 65 LDL-receptor class A 1. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 66 106 LDL-receptor class A 2. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 107 145 LDL-receptor class A 3. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 146 186 LDL-receptor class A 4. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 195 233 LDL-receptor class A 5. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 234 272 LDL-receptor class A 6. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 274 313 LDL-receptor class A 7. FT {ECO:0000255|PROSITE-ProRule:PRU00124}. FT DOMAIN 314 353 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 354 393 EGF-like 2; calcium-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00076}. FT REPEAT 397 438 LDL-receptor class B 1. FT REPEAT 439 485 LDL-receptor class B 2. FT REPEAT 486 528 LDL-receptor class B 3. FT REPEAT 529 572 LDL-receptor class B 4. FT REPEAT 573 615 LDL-receptor class B 5. FT REPEAT 616 658 LDL-receptor class B 6. FT DOMAIN 663 712 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT REGION 721 768 Clustered O-linked oligosaccharides. FT REGION 811 860 Required for MYLIP-triggered down- FT regulation of LDLR. FT {ECO:0000269|PubMed:19520913}. FT MOTIF 823 828 NPXY motif. FT {ECO:0000269|PubMed:22509010}. FT MOD_RES 724 724 Phosphothreonine. FT {ECO:0000250|UniProtKB:P35952}. FT CARBOHYD 97 97 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 156 156 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19520913}. FT CARBOHYD 272 272 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19520913}. FT CARBOHYD 515 515 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 657 657 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT DISULFID 27 39 FT DISULFID 34 52 FT DISULFID 46 63 FT DISULFID 68 82 FT DISULFID 75 95 FT DISULFID 89 104 FT DISULFID 109 121 {ECO:0000250}. FT DISULFID 116 134 FT DISULFID 128 143 FT DISULFID 148 160 FT DISULFID 155 173 FT DISULFID 167 184 FT DISULFID 197 209 FT DISULFID 204 222 FT DISULFID 216 231 FT DISULFID 236 248 FT DISULFID 243 261 FT DISULFID 255 270 FT DISULFID 276 289 FT DISULFID 284 302 FT DISULFID 296 313 FT DISULFID 318 329 FT DISULFID 325 338 FT DISULFID 340 352 FT DISULFID 358 368 FT DISULFID 364 377 FT DISULFID 379 392 FT DISULFID 667 681 FT DISULFID 677 696 FT DISULFID 698 711 FT VAR_SEQ 35 155 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_047413. FT VAR_SEQ 64 105 LSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGC FT P -> S (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043595. FT VAR_SEQ 105 272 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055014. FT VAR_SEQ 106 232 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043053. FT VAR_SEQ 273 273 V -> L (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055015. FT VAR_SEQ 663 713 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043054. FT VAR_SEQ 850 851 Missing (in isoform 5). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_045525. FT VARIANT 2 2 G -> R (in dbSNP:rs5931). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_011862. FT VARIANT 27 27 C -> W (in FH; San Francisco; FT dbSNP:rs2228671). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005304. FT VARIANT 46 46 C -> S (in FH; Japanese patient; FT dbSNP:rs121908041). FT {ECO:0000269|PubMed:11298688}. FT /FTId=VAR_013949. FT VARIANT 47 48 Missing (in FH; Cape Town-1; retards FT receptor transport from the endoplasmic FT reticulum to the cell surface). FT {ECO:0000269|PubMed:10882754, FT ECO:0000269|PubMed:3263645}. FT /FTId=VAR_005305. FT VARIANT 50 50 A -> S (in FH; German patient; FT dbSNP:rs137853960). FT {ECO:0000269|PubMed:10090484}. FT /FTId=VAR_007979. FT VARIANT 50 50 A -> T (in FH; unknown pathological FT significance; dbSNP:rs137853960). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072827. FT VARIANT 52 52 C -> Y (in Paris-4; dbSNP:rs879254418). FT /FTId=VAR_005306. FT VARIANT 56 56 S -> P (in FH; dbSNP:rs878854026). FT {ECO:0000269|PubMed:9104431}. FT /FTId=VAR_007980. FT VARIANT 78 78 R -> C (in FH; dbSNP:rs370860696). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005307. FT VARIANT 87 87 W -> G (in FH; French Canadian-4; FT dbSNP:rs121908025). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:2318961, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005308. FT VARIANT 89 89 C -> Y (in FH; dbSNP:rs875989894). FT {ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005309. FT VARIANT 90 90 D -> G (in FH; London-4; FT dbSNP:rs771019366). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005310. FT VARIANT 90 90 D -> N (in FH; dbSNP:rs749038326). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005311. FT VARIANT 90 90 D -> Y (in FH; Durban-1; FT dbSNP:rs749038326). FT {ECO:0000269|PubMed:8347689}. FT /FTId=VAR_005312. FT VARIANT 92 92 Q -> E (in FH; Spanish patient; FT dbSNP:rs774467219). FT {ECO:0000269|PubMed:10206683}. FT /FTId=VAR_005313. FT VARIANT 95 95 C -> G (in FH; Spanish patient; FT dbSNP:rs879254456). FT {ECO:0000269|PubMed:10206683}. FT /FTId=VAR_005314. FT VARIANT 101 101 E -> K (in FH; Lancashire; 6% of American FT English; dbSNP:rs144172724). FT {ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005315. FT VARIANT 105 105 P -> S (in dbSNP:rs13306510). FT /FTId=VAR_059375. FT VARIANT 109 109 C -> R (in Munster-1; dbSNP:rs140807148). FT /FTId=VAR_005316. FT VARIANT 116 116 C -> R (in FH; does not affect receptor FT expression at the cell surface; results FT in reduced LDL binding; results in FT reduced LDL uptake and internalization; FT dbSNP:rs879254482). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:25545329}. FT /FTId=VAR_005317. FT VARIANT 134 134 C -> F (in FH; dbSNP:rs879254514). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062371. FT VARIANT 134 134 C -> W (in FH; dbSNP:rs879254515). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062372. FT VARIANT 139 139 D -> H (found in a patient with FT hypercholesterolemia; dbSNP:rs879254517). FT {ECO:0000269|PubMed:21418584}. FT /FTId=VAR_065780. FT VARIANT 140 140 E -> K (in FH; Philippines/Durban-2/ FT Japan; dbSNP:rs748944640). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:7583548, FT ECO:0000269|PubMed:8347689}. FT /FTId=VAR_005318. FT VARIANT 143 143 C -> R (in FH; dbSNP:rs875989901). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072828. FT VARIANT 148 148 C -> Y (in FH; dbSNP:rs879254526). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072829. FT VARIANT 155 155 C -> G (in Germany; dbSNP:rs879254535). FT /FTId=VAR_005319. FT VARIANT 155 155 C -> Y (in FH; results in defective LDL FT binding; does not affect receptor FT expression at the cell surface; FT dbSNP:rs879254536). FT {ECO:0000269|PubMed:19318025, FT ECO:0000269|PubMed:25378237}. FT /FTId=VAR_072830. FT VARIANT 160 160 C -> Y (in FH; unknown pathological FT significance; dbSNP:rs879254541). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005320. FT VARIANT 168 168 D -> A (in FH; unknown pathological FT significance; dbSNP:rs879254549). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072831. FT VARIANT 168 168 D -> H (in FH; Sephardic/Safed; 10% of FT the Sephardic Jews; dbSNP:rs200727689). FT {ECO:0000269|PubMed:8462973}. FT /FTId=VAR_005321. FT VARIANT 168 168 D -> N (in FH; does not affect receptor FT expression at the cell surface; results FT in reduced LDL binding; results in FT reduced LDL uptake and internalization; FT dbSNP:rs200727689). FT {ECO:0000269|PubMed:25545329, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005322. FT VARIANT 168 168 D -> Y (in FH; dbSNP:rs200727689). FT {ECO:0000269|PubMed:8740918}. FT /FTId=VAR_005323. FT VARIANT 172 172 D -> H (may contribute to familial FT hypercholesterolemia; dbSNP:rs879254554). FT {ECO:0000269|PubMed:10882754}. FT /FTId=VAR_013950. FT VARIANT 172 172 D -> N (in FH; does not affect receptor FT expression at the cell surface; results FT in reduced LDL binding; results in FT reduced LDL uptake and internalization; FT dbSNP:rs879254554). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:25545329}. FT /FTId=VAR_072832. FT VARIANT 173 173 C -> R (in Greece-1; dbSNP:rs879254558). FT /FTId=VAR_005324. FT VARIANT 173 173 C -> W (in FH; dbSNP:rs769318035). FT {ECO:0000269|PubMed:9452094}. FT /FTId=VAR_005325. FT VARIANT 175 175 D -> N (in FH; Afrikaner-3; 5-10% of FT Afrikaners; dbSNP:rs121908033). FT {ECO:0000269|PubMed:2569482}. FT /FTId=VAR_005326. FT VARIANT 175 175 D -> Y (in FH; dbSNP:rs121908033). FT {ECO:0000269|PubMed:9104431}. FT /FTId=VAR_007981. FT VARIANT 177 177 S -> L (in FH; Puerto Rico; FT dbSNP:rs121908026). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:9259195, FT ECO:0000269|PubMed:9654205}. FT /FTId=VAR_005327. FT VARIANT 184 184 C -> W (in FH; dbSNP:rs879254571). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072833. FT VARIANT 184 184 C -> Y (in FH; Glasco; FT dbSNP:rs121908039). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:9678702}. FT /FTId=VAR_013951. FT VARIANT 197 197 C -> F (in Shreveport; FT dbSNP:rs376459828). FT /FTId=VAR_005328. FT VARIANT 197 197 C -> R (in FH; British patient; FT dbSNP:rs730882085). FT {ECO:0000269|PubMed:9026534}. FT /FTId=VAR_005330. FT VARIANT 197 197 C -> Y (in El Salvador-1; FT dbSNP:rs376459828). FT /FTId=VAR_005329. FT VARIANT 201 201 E -> K (found in a patient with FT hypercholesterolemia; dbSNP:rs879254589). FT {ECO:0000269|PubMed:21418584}. FT /FTId=VAR_065781. FT VARIANT 211 211 H -> L (in FH; unknown pathological FT significance; dbSNP:rs879254603). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072834. FT VARIANT 218 218 Missing (in FH; Piscataway/Lithuania). FT {ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:1867200, FT ECO:0000269|PubMed:9654205}. FT /FTId=VAR_005331. FT VARIANT 221 221 D -> G (in FH; Padova; FT dbSNP:rs373822756). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:17347910, FT ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:7649546, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005332. FT VARIANT 221 221 D -> N (in FH; German patient; FT dbSNP:rs875989906). FT {ECO:0000269|PubMed:10090484, FT ECO:0000269|PubMed:17142622}. FT /FTId=VAR_007982. FT VARIANT 221 221 D -> Y (in FH; Cologne patient; FT dbSNP:rs875989906). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:7649546}. FT /FTId=VAR_005333. FT VARIANT 222 222 C -> Y (in FH; dbSNP:rs730882086). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062373. FT VARIANT 224 224 D -> G (in Italy-2; dbSNP:rs879254630). FT /FTId=VAR_005335. FT VARIANT 224 224 D -> N (in Portugal; dbSNP:rs387906303). FT /FTId=VAR_005334. FT VARIANT 224 224 D -> V (in FH; Cologne patient; FT dbSNP:rs879254630). FT {ECO:0000269|PubMed:7649546}. FT /FTId=VAR_005336. FT VARIANT 226 226 S -> P (in Miami-1; dbSNP:rs879254635). FT /FTId=VAR_005337. FT VARIANT 227 227 D -> E (in FH; Afrikaner-1/Maine; 65-70% FT of Afrikaner Americans; FT dbSNP:rs121908028). FT {ECO:0000269|PubMed:2569482, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005338. FT VARIANT 228 228 E -> CK (in Chieti-3). FT {ECO:0000269|PubMed:10660340}. FT /FTId=VAR_005339. FT VARIANT 228 228 E -> K (in FH; French Canadian-3/Mexico; FT 2% of French Canadians; FT dbSNP:rs121908029). FT {ECO:0000269|PubMed:2318961, FT ECO:0000269|PubMed:24529145}. FT /FTId=VAR_005341. FT VARIANT 228 228 E -> Q (in FH; Tulsa-2; FT dbSNP:rs121908029). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_005340. FT VARIANT 231 231 C -> G (in FH; Norwegian patient; FT dbSNP:rs746091400). FT {ECO:0000269|PubMed:8664907}. FT /FTId=VAR_005342. FT VARIANT 240 240 E -> K (in Charlotte; dbSNP:rs768563000). FT /FTId=VAR_005343. FT VARIANT 243 243 C -> R (in FH; unknown pathological FT significance; dbSNP:rs879254659). FT {ECO:0000269|PubMed:10532689}. FT /FTId=VAR_072835. FT VARIANT 248 248 C -> F (in Bretagne-1; FT dbSNP:rs879254663). FT /FTId=VAR_005344. FT VARIANT 248 248 C -> Y (in FH; British patient; FT dbSNP:rs879254663). FT {ECO:0000269|PubMed:9026534}. FT /FTId=VAR_005345. FT VARIANT 253 253 R -> W (may contribute to familial FT hypercholesterolemia; dbSNP:rs150673992). FT {ECO:0000269|PubMed:10882754}. FT /FTId=VAR_013952. FT VARIANT 254 254 Q -> P (in FH; dbSNP:rs879254667). FT {ECO:0000269|PubMed:10978268, FT ECO:0000269|PubMed:19319977}. FT /FTId=VAR_062374. FT VARIANT 255 255 C -> S (found in a patient with FT hypercholesterolemia; dbSNP:rs879254668). FT {ECO:0000269|PubMed:21418584}. FT /FTId=VAR_065782. FT VARIANT 256 256 D -> G (in Nevers; dbSNP:rs879254670). FT /FTId=VAR_005346. FT VARIANT 257 257 R -> W (polymorphism; does not affect FT receptor expression at the cell surface; FT does not affect LDL binding; does not FT affect LDL uptake and internalization; FT dbSNP:rs200990725). FT {ECO:0000269|PubMed:11462246, FT ECO:0000269|PubMed:25545329}. FT /FTId=VAR_072836. FT VARIANT 261 261 C -> F (in FH; rare mutation; strongly FT reduced receptor activity; FT dbSNP:rs121908040). FT {ECO:0000269|PubMed:10422803}. FT /FTId=VAR_013953. FT VARIANT 266 266 D -> E (in FH; Cincinnati-1; unknown FT pathological significance; FT dbSNP:rs139043155). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_005347. FT VARIANT 270 270 C -> Y (in Miami-2; dbSNP:rs879254683). FT /FTId=VAR_005348. FT VARIANT 276 276 C -> R (in FH; dbSNP:rs879254692). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062375. FT VARIANT 276 276 C -> W (in FH; unknown pathological FT significance; dbSNP:rs146651743). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072837. FT VARIANT 276 276 C -> Y (in FH; Syrian patient; FT dbSNP:rs730882089). {ECO:0000269|Ref.71}. FT /FTId=VAR_005349. FT VARIANT 277 277 E -> K (in FH; patients from Sweden and FT La Havana; unknown pathological FT significance; dbSNP:rs148698650). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:17347910, FT ECO:0000269|PubMed:7635461, FT ECO:0000269|PubMed:7649549}. FT /FTId=VAR_005350. FT VARIANT 285 285 H -> Y (in FH; unknown pathological FT significance; dbSNP:rs730882091). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072838. FT VARIANT 286 286 S -> R (in FH; Greece-2; unknown FT pathological significance; FT dbSNP:rs140241383). FT {ECO:0000269|PubMed:17347910, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005351. FT VARIANT 288 288 E -> K (in FH; German patient; FT dbSNP:rs368657165). FT {ECO:0000269|PubMed:10090484}. FT /FTId=VAR_007983. FT VARIANT 300 300 R -> G (in FH; does not affect receptor FT expression at the cell surface; results FT in reduced LDL binding; results in FT reduced LDL uptake and internalization; FT dbSNP:rs767618089). FT {ECO:0000269|PubMed:19318025, FT ECO:0000269|PubMed:25545329}. FT /FTId=VAR_072839. FT VARIANT 301 301 D -> A (in FH; Greek patient; FT dbSNP:rs879254714). FT {ECO:0000269|PubMed:9026534}. FT /FTId=VAR_005352. FT VARIANT 301 301 D -> G (in FH; does not affect receptor FT expression at the cell surface; results FT in reduced LDL binding; results in FT reduced LDL uptake and internalization; FT dbSNP:rs879254714). FT {ECO:0000269|PubMed:19318025, FT ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:25545329}. FT /FTId=VAR_072840. FT VARIANT 302 302 C -> W (in FH; Iraki patient; FT dbSNP:rs879254716). FT {ECO:0000269|PubMed:9026534}. FT /FTId=VAR_005354. FT VARIANT 302 302 C -> Y (in FH; Spanish patient; FT dbSNP:rs879254715). FT {ECO:0000269|PubMed:10206683}. FT /FTId=VAR_005353. FT VARIANT 304 304 D -> E (in Baltimore-1; FT dbSNP:rs875989909). FT /FTId=VAR_005356. FT VARIANT 304 304 D -> N (in Denver-2; dbSNP:rs121908030). FT {ECO:0000269|PubMed:21418584}. FT /FTId=VAR_005355. FT VARIANT 306 306 S -> L (in FH; Amsterdam; unknown FT pathological significance; FT dbSNP:rs11547917). FT {ECO:0000269|PubMed:10532689}. FT /FTId=VAR_005357. FT VARIANT 313 313 C -> Y (in FH; dbSNP:rs875989911 and FT dbSNP:rs875989910). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005358. FT VARIANT 314 314 G -> R (in FH; unknown pathological FT significance; dbSNP:rs72658858). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072841. FT VARIANT 318 318 C -> F (in FH; Trieste; FT dbSNP:rs879254739). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:8168830}. FT /FTId=VAR_005360. FT VARIANT 318 318 C -> R (in FH; dbSNP:rs879254738). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062376. FT VARIANT 318 318 C -> Y (in Mexico-1; leads to a defect in FT the intracellular transport of the FT receptor; dbSNP:rs879254739). FT /FTId=VAR_005359. FT VARIANT 326 326 S -> C (in FH; unknown pathological FT significance; dbSNP:rs879254747). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072842. FT VARIANT 327 327 H -> Y (in FH; dbSNP:rs747507019). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005361. FT VARIANT 329 329 C -> F (in FH; dbSNP:rs761954844). FT {ECO:0000269|PubMed:22160468}. FT /FTId=VAR_067196. FT VARIANT 329 329 C -> Y (in FH; Chinese patient; FT dbSNP:rs761954844). FT {ECO:0000269|PubMed:9452118}. FT /FTId=VAR_005362. FT VARIANT 335 335 G -> S (in Paris-6; dbSNP:rs544453230). FT /FTId=VAR_005363. FT VARIANT 338 338 C -> S (in FH; Japanese patients; FT dbSNP:rs879254753). FT {ECO:0000269|PubMed:10447263, FT ECO:0000269|PubMed:7583548}. FT /FTId=VAR_005364. FT VARIANT 342 342 D -> E (in New York-1; FT dbSNP:rs780563386). FT /FTId=VAR_005365. FT VARIANT 342 342 D -> N (in FH; unknown pathological FT significance; dbSNP:rs139361635). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005366. FT VARIANT 343 343 G -> S (in FH; Picardie; unknown FT pathological significance; FT dbSNP:rs730882096). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_005367. FT VARIANT 350 350 R -> P (in FH; dbSNP:rs875989914). FT {ECO:0000269|PubMed:9026534, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005368. FT VARIANT 352 352 C -> R (in FH; unknown pathological FT significance; dbSNP:rs879254769). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072843. FT VARIANT 352 352 C -> Y (in Mexico-2; dbSNP:rs193922566). FT /FTId=VAR_005369. FT VARIANT 354 354 D -> G (in Munster-2; dbSNP:rs755449669). FT /FTId=VAR_005370. FT VARIANT 354 354 D -> V (in Oklahoma; dbSNP:rs755449669). FT /FTId=VAR_005371. FT VARIANT 356 356 D -> Y (in FH; dbSNP:rs767767730). FT {ECO:0000269|PubMed:19319977, FT ECO:0000269|PubMed:9104431}. FT /FTId=VAR_007984. FT VARIANT 357 357 E -> K (in Paris-7; dbSNP:rs879254781). FT /FTId=VAR_005372. FT VARIANT 358 358 C -> Y (in FH; dbSNP:rs875989915). FT {ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:19319977}. FT /FTId=VAR_062377. FT VARIANT 364 364 C -> R (in Mexico-3; dbSNP:rs879254787). FT /FTId=VAR_005373. FT VARIANT 366 366 Q -> R (in FH; dbSNP:rs746982741). FT {ECO:0000269|PubMed:8740918}. FT /FTId=VAR_007985. FT VARIANT 368 368 C -> R (in FH; French Canadian patient; FT dbSNP:rs879254791). FT {ECO:0000269|PubMed:9452094}. FT /FTId=VAR_005374. FT VARIANT 368 368 C -> Y (in FH; unknown pathological FT significance; dbSNP:rs768430352). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072844. FT VARIANT 370 370 N -> T (in FH; dbSNP:rs879254792). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062378. FT VARIANT 373 373 G -> D (in FH; unknown pathological FT significance; dbSNP:rs879254797). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072845. FT VARIANT 379 379 C -> R (in Naples-1; dbSNP:rs879254803). FT /FTId=VAR_005375. FT VARIANT 379 379 C -> Y (in FH; dbSNP:rs879254804). FT {ECO:0000269|PubMed:9852677}. FT /FTId=VAR_007986. FT VARIANT 391 391 A -> T (in dbSNP:rs11669576). FT /FTId=VAR_024519. FT VARIANT 399 399 A -> D (in FH; dbSNP:rs875989918). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005376. FT VARIANT 401 401 L -> H (in Pori; dbSNP:rs121908038). FT {ECO:0000269|PubMed:7573037}. FT /FTId=VAR_005377. FT VARIANT 401 401 L -> V (in FH; dbSNP:rs146200173). FT {ECO:0000269|PubMed:9104431}. FT /FTId=VAR_007987. FT VARIANT 403 403 F -> L (in FH; Japanese patient; FT dbSNP:rs879254831). FT {ECO:0000269|PubMed:10447263}. FT /FTId=VAR_008995. FT VARIANT 404 404 T -> P (in FH; unknown pathological FT significance; dbSNP:rs879254834). FT {ECO:0000269|PubMed:10532689}. FT /FTId=VAR_072846. FT VARIANT 406 406 R -> Q (may contribute to familial FT hypercholesterolemia; dbSNP:rs552422789). FT {ECO:0000269|PubMed:10882754}. FT /FTId=VAR_013954. FT VARIANT 406 406 R -> W (in FH; unknown pathological FT significance; dbSNP:rs121908043). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072847. FT VARIANT 408 408 E -> K (in FH; Algeria-1; unknown FT pathological significance; FT dbSNP:rs137943601). FT {ECO:0000269|PubMed:10882754, FT ECO:0000269|PubMed:17347910}. FT /FTId=VAR_005378. FT VARIANT 414 414 L -> R (in FH; Chinese patient; FT dbSNP:rs748554592). FT {ECO:0000269|PubMed:9452118}. FT /FTId=VAR_005379. FT VARIANT 415 415 D -> G (in FH; dbSNP:rs879254845). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062379. FT VARIANT 416 416 R -> Q (in FH; German patient; FT dbSNP:rs773658037). FT {ECO:0000269|PubMed:9452095}. FT /FTId=VAR_005380. FT VARIANT 416 416 R -> W (in FH; results in reduced FT receptor expression at the cell surface FT due to defective receptor recycling; FT dbSNP:rs570942190). FT {ECO:0000269|PubMed:19318025, FT ECO:0000269|PubMed:25378237, FT ECO:0000269|PubMed:9104431, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005381. FT VARIANT 423 423 I -> T (in FH; Swedish patient; FT dbSNP:rs879254849). FT {ECO:0000269|PubMed:7635461}. FT /FTId=VAR_005382. FT VARIANT 429 429 V -> M (in FH; Afrikaner-2; 20-30% of FT Afrikaners and 2% of FH Dutch; FT dbSNP:rs28942078). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:2569482, FT ECO:0000269|PubMed:7649549, FT ECO:0000269|PubMed:9452095, FT ECO:0000269|PubMed:9452118}. FT /FTId=VAR_005383. FT VARIANT 431 431 A -> T (in FH; Algeria-2; unknown FT pathological significance; FT dbSNP:rs28942079). FT {ECO:0000269|PubMed:10447263, FT ECO:0000269|PubMed:17347910}. FT /FTId=VAR_005384. FT VARIANT 432 432 L -> V (in FH; German patient; FT dbSNP:rs730882100). FT {ECO:0000269|PubMed:10090484}. FT /FTId=VAR_007988. FT VARIANT 433 433 D -> H (in FH; Osaka-3; FT dbSNP:rs121908036). FT {ECO:0000269|PubMed:1446662}. FT /FTId=VAR_005385. FT VARIANT 434 434 T -> K (in FH; Algeria-3; unknown FT pathological significance; FT dbSNP:rs745343524). FT {ECO:0000269|PubMed:10206683}. FT /FTId=VAR_005386. FT VARIANT 441 441 I -> M (in Rouen; dbSNP:rs5933). FT /FTId=VAR_005388. FT VARIANT 441 441 I -> N (in Russia-1; dbSNP:rs879254862). FT /FTId=VAR_005387. FT VARIANT 442 442 Y -> H (in FH; unknown pathological FT significance; dbSNP:rs879254863). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072848. FT VARIANT 443 443 W -> C (in North Platt; FT dbSNP:rs879254867). FT /FTId=VAR_005389. FT VARIANT 451 451 I -> T (in FH; dbSNP:rs879254874). FT {ECO:0000269|PubMed:10980548, FT ECO:0000269|PubMed:19319977}. FT /FTId=VAR_062380. FT VARIANT 454 454 T -> N (in FH; results in reduced FT receptor expression at the cell surface FT due to defective receptor recycling; FT dbSNP:rs879254879). FT {ECO:0000269|PubMed:19318025, FT ECO:0000269|PubMed:25378237}. FT /FTId=VAR_072849. FT VARIANT 468 468 V -> I (in dbSNP:rs5932). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_011863. FT VARIANT 471 471 R -> G (found in a patient with FT hypercholesterolemia; dbSNP:rs879254891). FT {ECO:0000269|PubMed:21418584}. FT /FTId=VAR_065783. FT VARIANT 478 478 G -> R (in New York-2; FT dbSNP:rs144614838). FT /FTId=VAR_005390. FT VARIANT 479 479 L -> P (in FH; dbSNP:rs879254900). FT {ECO:0000269|PubMed:17142622}. FT /FTId=VAR_062381. FT VARIANT 482 482 D -> H (in FH; dbSNP:rs139624145). FT {ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005391. FT VARIANT 483 483 W -> R (in FH; dbSNP:rs879254905). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005392. FT VARIANT 485 485 H -> R (in Milan; dbSNP:rs879254906). FT /FTId=VAR_005394. FT VARIANT 487 487 Missing (in FH; Norwegian patient). FT {ECO:0000269|PubMed:7635482}. FT /FTId=VAR_005393. FT VARIANT 492 492 D -> N (in FH; unknown pathological FT significance; dbSNP:rs373646964). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072850. FT VARIANT 523 523 V -> M (in FH; Kuwait; dbSNP:rs28942080). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_005395. FT VARIANT 526 526 P -> S (in FH; Cincinnati-3; unknown FT pathological significance; FT dbSNP:rs730882106). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005396. FT VARIANT 546 546 G -> D (in Saint Omer; retention in the FT ER; dbSNP:rs28942081). FT {ECO:0000269|PubMed:19520913}. FT /FTId=VAR_005397. FT VARIANT 549 549 G -> D (in FH; Genoa; dbSNP:rs28941776). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005398. FT VARIANT 564 564 N -> H (in FH; dbSNP:rs397509365). FT {ECO:0000269|PubMed:10090484, FT ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:7550239, FT ECO:0000269|PubMed:9143924}. FT /FTId=VAR_005399. FT VARIANT 564 564 N -> S (in FH; Sicily; FT dbSNP:rs758194385). FT {ECO:0000269|PubMed:9654205}. FT /FTId=VAR_005400. FT VARIANT 565 565 G -> V (in Naples-2; dbSNP:rs28942082). FT /FTId=VAR_005401. FT VARIANT 568 568 L -> V (in FH; Japanese patient; FT dbSNP:rs746959386). FT {ECO:0000269|PubMed:10447263}. FT /FTId=VAR_008996. FT VARIANT 574 574 R -> C (in FH; dbSNP:rs185098634). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072851. FT VARIANT 574 574 R -> H (in FH; unknown pathological FT significance; dbSNP:rs777188764). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072852. FT VARIANT 577 577 W -> G (in FH; results in loss of FT receptor expression at the cell surface; FT dbSNP:rs879255000). FT {ECO:0000269|PubMed:17347910, FT ECO:0000269|PubMed:25378237}. FT /FTId=VAR_072853. FT VARIANT 577 577 W -> S (in FH; unknown pathological FT significance; dbSNP:rs138947766). FT {ECO:0000269|PubMed:10532689}. FT /FTId=VAR_072854. FT VARIANT 579 579 D -> N (in FH; Cincinnati-4; less than 2% FT receptor activity; dbSNP:rs875989929). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:7635461}. FT /FTId=VAR_005402. FT VARIANT 579 579 D -> Y (in FH; dbSNP:rs875989929). FT {ECO:0000269|PubMed:10978268}. FT /FTId=VAR_062382. FT VARIANT 585 585 I -> T (in FH; unknown pathological FT significance; dbSNP:rs879255012). FT {ECO:0000269|PubMed:17347910}. FT /FTId=VAR_072855. FT VARIANT 592 592 G -> E (in FH; Sicily; FT dbSNP:rs137929307). FT {ECO:0000269|PubMed:9654205}. FT /FTId=VAR_005403. FT VARIANT 595 595 R -> W (in FH; unknown pathological FT significance; dbSNP:rs373371572). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072856. FT VARIANT 599 599 L -> S (in London-5; dbSNP:rs879255025). FT /FTId=VAR_005404. FT VARIANT 601 601 D -> H (in FH; unknown pathological FT significance; dbSNP:rs753707206). FT {ECO:0000269|PubMed:24529145}. FT /FTId=VAR_072857. FT VARIANT 608 608 P -> S (in FH; dbSNP:rs879255034). FT {ECO:0000269|PubMed:9852677}. FT /FTId=VAR_007989. FT VARIANT 633 633 R -> C (in FH; dbSNP:rs746118995). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005405. FT VARIANT 639 639 V -> D (in FH; dbSNP:rs794728584). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072858. FT VARIANT 649 649 P -> L (in FH; dbSNP:rs879255081). FT {ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005406. FT VARIANT 667 667 C -> Y (in FH; French Canadian-2; 5% of FT French Canadians; dbSNP:rs28942083). FT {ECO:0000269|PubMed:10206683, FT ECO:0000269|PubMed:2318961}. FT /FTId=VAR_005407. FT VARIANT 677 677 C -> R (in FH; New York-3; FT dbSNP:rs775092314). FT {ECO:0000269|PubMed:17142622}. FT /FTId=VAR_005408. FT VARIANT 682 682 L -> P (in Issoire; dbSNP:rs879255119). FT /FTId=VAR_005409. FT VARIANT 685 685 P -> L (in FH; Gujerat/Zambia/Belgian/ FT Dutch/Sweden/Japan; dbSNP:rs28942084). FT {ECO:0000269|PubMed:1464748, FT ECO:0000269|PubMed:17142622, FT ECO:0000269|PubMed:17347910, FT ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:2726768, FT ECO:0000269|PubMed:7583548, FT ECO:0000269|PubMed:9254862}. FT /FTId=VAR_005410. FT VARIANT 699 699 P -> L (in FH; unknown pathological FT significance; dbSNP:rs201573863). FT {ECO:0000269|PubMed:10882754, FT ECO:0000269|PubMed:24529145}. FT /FTId=VAR_013955. FT VARIANT 700 700 D -> E (in FH; Spanish patient; FT dbSNP:rs759858813). FT {ECO:0000269|PubMed:10206683}. FT /FTId=VAR_005412. FT VARIANT 714 714 E -> K (in FH; Japanese patient; FT dbSNP:rs869320652). FT {ECO:0000269|PubMed:10447263}. FT /FTId=VAR_008997. FT VARIANT 726 726 T -> I (in FH; Paris-9; unknown FT pathological significance; FT dbSNP:rs45508991). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:9259195}. FT /FTId=VAR_005413. FT VARIANT 742 742 T -> I (in dbSNP:rs767546791). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072859. FT VARIANT 792 792 I -> F (in Russia-2; dbSNP:rs761123215). FT /FTId=VAR_005414. FT VARIANT 797 797 V -> M (in FH; La Havana patient; FT dbSNP:rs750518671). FT {ECO:0000269|PubMed:24529145, FT ECO:0000269|PubMed:7649549}. FT /FTId=VAR_005415. FT VARIANT 799 801 Missing (in FH; Danish patient). FT {ECO:0000269|PubMed:9143924}. FT /FTId=VAR_005416. FT VARIANT 806 806 V -> D (in FH; unknown pathological FT significance; dbSNP:rs879255208). FT {ECO:0000269|PubMed:11462246}. FT /FTId=VAR_072860. FT VARIANT 814 814 R -> Q (in FH; unknown pathological FT significance; dbSNP:rs5928). FT {ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10882754, FT ECO:0000269|PubMed:24529145}. FT /FTId=VAR_011864. FT VARIANT 820 822 Missing (in FH). FT /FTId=VAR_005417. FT VARIANT 825 825 N -> K (in FH; does not affect receptor FT expression at the cell surface; does not FT affect LDL binding; results in impaired FT LDL uptake and internalization; FT dbSNP:rs374045590). FT {ECO:0000269|PubMed:10532689, FT ECO:0000269|PubMed:25378237}. FT /FTId=VAR_072861. FT VARIANT 826 826 P -> S (in FH). FT {ECO:0000269|PubMed:19319977}. FT /FTId=VAR_062383. FT VARIANT 827 827 V -> I (in New York-5; FT dbSNP:rs137853964). FT /FTId=VAR_005418. FT VARIANT 828 828 Y -> C (in FH; J.D.Bari/Syria; 2-fold FT decreased affinity for LDLRAP1; FT dbSNP:rs28942085). FT {ECO:0000269|PubMed:22509010, FT ECO:0000269|PubMed:3955657}. FT /FTId=VAR_005419. FT VARIANT 844 844 G -> D (in Turku; dbSNP:rs121908037). FT {ECO:0000269|PubMed:7573037}. FT /FTId=VAR_005420. FT MUTAGEN 811 811 K->R: No change. No change; when FT associated with R-816 and R-830. FT Insensitive to MYLIP-triggered FT degradation; when associated with R-816; FT R-830 and A-839. FT {ECO:0000269|PubMed:19520913}. FT MUTAGEN 816 816 K->R: No change. No change; when FT associated with R-830. No change; when FT associated with R-811 and R-830. FT Insensitive to MYLIP-triggered FT degradation; when associated with R-830 FT and A-839. Insensitive to MYLIP-triggered FT degradation; when associated with R-811; FT R-830 and A-839. FT {ECO:0000269|PubMed:19520913}. FT MUTAGEN 821 821 I->A: 3-fold decreased affinity for FT LDLRAP1. {ECO:0000269|PubMed:22509010}. FT MUTAGEN 821 821 I->R: 10-fold decreased affinity for FT LDLRAP1. {ECO:0000269|PubMed:22509010}. FT MUTAGEN 828 828 Y->A: Abolishes interaction with ARRB2. FT {ECO:0000269|PubMed:12944399}. FT MUTAGEN 829 829 Q->A: Decreased affinity for LDLRAP1. FT {ECO:0000269|PubMed:22509010}. FT MUTAGEN 830 830 K->R: No change. No change; when FT associated with R-816. No change; when FT associated with R-811 and R-816. FT Insensitive to MYLIP-triggered FT degradation; when associated with A-839. FT Insensitive to MYLIP-triggered FT degradation; when associated with R-816 FT and A-839. Insensitive to MYLIP-triggered FT degradation; when associated with R-811; FT R-816 and A-839. FT {ECO:0000269|PubMed:19520913}. FT MUTAGEN 839 839 C->A: No change. Insensitive to MYLIP- FT triggered degradation; when associated FT with R-830. Insensitive to MYLIP- FT triggered degradation; when associated FT with R-816 and R-830. Insensitive to FT MYLIP-triggered degradation; when FT associated with R-811; R-816 and R-830. FT {ECO:0000269|PubMed:19520913}. FT MUTAGEN 854 854 S->A: No effect on receptor FT internalization. FT {ECO:0000269|PubMed:12944399}. FT MUTAGEN 854 854 S->D: Enhances interaction with ARRB2 and FT receptor internalization. FT {ECO:0000269|PubMed:12944399}. FT CONFLICT 31 31 E -> D (in Ref. 4; BAG58495). FT {ECO:0000305}. FT STRAND 29 33 {ECO:0000244|PDB:1F5Y}. FT STRAND 35 37 {ECO:0000244|PDB:1F5Y}. FT STRAND 39 41 {ECO:0000244|PDB:1LDL}. FT TURN 42 46 {ECO:0000244|PDB:1F5Y}. FT STRAND 47 49 {ECO:0000244|PDB:1F5Y}. FT STRAND 51 55 {ECO:0000244|PDB:1F5Y}. FT HELIX 56 58 {ECO:0000244|PDB:1F5Y}. FT TURN 60 62 {ECO:0000244|PDB:1LDL}. FT STRAND 65 67 {ECO:0000244|PDB:5OYL}. FT STRAND 70 72 {ECO:0000244|PDB:1LDR}. FT STRAND 77 79 {ECO:0000244|PDB:5OYL}. FT HELIX 85 87 {ECO:0000244|PDB:5OYL}. FT STRAND 90 93 {ECO:0000244|PDB:5OYL}. FT STRAND 95 97 {ECO:0000244|PDB:1F5Y}. FT HELIX 99 101 {ECO:0000244|PDB:5OYL}. FT STRAND 102 104 {ECO:0000244|PDB:5OYL}. FT STRAND 113 115 {ECO:0000244|PDB:2FCW}. FT STRAND 121 123 {ECO:0000244|PDB:2FCW}. FT HELIX 124 126 {ECO:0000244|PDB:2FCW}. FT STRAND 129 131 {ECO:0000244|PDB:2FCW}. FT TURN 138 142 {ECO:0000244|PDB:2FCW}. FT HELIX 143 147 {ECO:0000244|PDB:2FCW}. FT STRAND 148 151 {ECO:0000244|PDB:2LGP}. FT STRAND 152 154 {ECO:0000244|PDB:2FCW}. FT TURN 156 158 {ECO:0000244|PDB:2LGP}. FT STRAND 160 162 {ECO:0000244|PDB:2FCW}. FT HELIX 163 165 {ECO:0000244|PDB:2FCW}. FT STRAND 168 170 {ECO:0000244|PDB:2FCW}. FT STRAND 173 176 {ECO:0000244|PDB:2LGP}. FT HELIX 177 179 {ECO:0000244|PDB:2FCW}. FT HELIX 181 183 {ECO:0000244|PDB:2FCW}. FT TURN 189 191 {ECO:0000244|PDB:2LGP}. FT STRAND 201 204 {ECO:0000244|PDB:2LGP}. FT TURN 205 207 {ECO:0000244|PDB:2LGP}. FT STRAND 208 211 {ECO:0000244|PDB:2LGP}. FT HELIX 212 214 {ECO:0000244|PDB:1AJJ}. FT STRAND 217 219 {ECO:0000244|PDB:1AJJ}. FT STRAND 222 224 {ECO:0000244|PDB:2LGP}. FT HELIX 226 228 {ECO:0000244|PDB:1AJJ}. FT STRAND 241 243 {ECO:0000244|PDB:1D2J}. FT TURN 244 246 {ECO:0000244|PDB:1D2J}. FT STRAND 247 249 {ECO:0000244|PDB:1D2J}. FT HELIX 251 253 {ECO:0000244|PDB:1D2J}. FT STRAND 254 258 {ECO:0000244|PDB:1D2J}. FT STRAND 260 264 {ECO:0000244|PDB:1D2J}. FT HELIX 265 267 {ECO:0000244|PDB:1F8Z}. FT STRAND 268 270 {ECO:0000244|PDB:1F8Z}. FT STRAND 281 283 {ECO:0000244|PDB:1XFE}. FT STRAND 289 292 {ECO:0000244|PDB:1XFE}. FT TURN 293 296 {ECO:0000244|PDB:1XFE}. FT STRAND 306 308 {ECO:0000244|PDB:1XFE}. FT TURN 310 312 {ECO:0000244|PDB:1XFE}. FT HELIX 317 319 {ECO:0000244|PDB:2W2N}. FT HELIX 321 324 {ECO:0000244|PDB:2W2N}. FT STRAND 326 330 {ECO:0000244|PDB:2W2N}. FT STRAND 333 335 {ECO:0000244|PDB:2W2N}. FT STRAND 337 339 {ECO:0000244|PDB:2W2N}. FT STRAND 341 343 {ECO:0000244|PDB:1HZ8}. FT STRAND 345 347 {ECO:0000244|PDB:2W2N}. FT TURN 348 350 {ECO:0000244|PDB:2W2N}. FT STRAND 351 353 {ECO:0000244|PDB:2W2N}. FT HELIX 357 359 {ECO:0000244|PDB:1HJ7}. FT STRAND 363 369 {ECO:0000244|PDB:1HJ7}. FT STRAND 372 374 {ECO:0000244|PDB:3P5B}. FT STRAND 376 378 {ECO:0000244|PDB:1HJ7}. FT STRAND 381 385 {ECO:0000244|PDB:1HZ8}. FT TURN 387 389 {ECO:0000244|PDB:3P5B}. FT STRAND 392 394 {ECO:0000244|PDB:1HZ8}. FT STRAND 400 404 {ECO:0000244|PDB:1IJQ}. FT STRAND 406 413 {ECO:0000244|PDB:1IJQ}. FT STRAND 420 423 {ECO:0000244|PDB:1IJQ}. FT STRAND 427 435 {ECO:0000244|PDB:1IJQ}. FT TURN 436 439 {ECO:0000244|PDB:1IJQ}. FT STRAND 440 445 {ECO:0000244|PDB:1IJQ}. FT TURN 446 449 {ECO:0000244|PDB:1IJQ}. FT STRAND 450 455 {ECO:0000244|PDB:1IJQ}. FT STRAND 466 469 {ECO:0000244|PDB:1IJQ}. FT STRAND 478 482 {ECO:0000244|PDB:1IJQ}. FT TURN 483 486 {ECO:0000244|PDB:1IJQ}. FT STRAND 487 492 {ECO:0000244|PDB:1IJQ}. FT TURN 493 496 {ECO:0000244|PDB:1IJQ}. FT STRAND 497 502 {ECO:0000244|PDB:1IJQ}. FT STRAND 505 513 {ECO:0000244|PDB:1IJQ}. FT STRAND 519 525 {ECO:0000244|PDB:1IJQ}. FT TURN 526 529 {ECO:0000244|PDB:1IJQ}. FT STRAND 530 535 {ECO:0000244|PDB:1IJQ}. FT STRAND 537 539 {ECO:0000244|PDB:1IJQ}. FT STRAND 541 546 {ECO:0000244|PDB:1IJQ}. FT STRAND 552 556 {ECO:0000244|PDB:1IJQ}. FT STRAND 563 569 {ECO:0000244|PDB:1IJQ}. FT TURN 570 573 {ECO:0000244|PDB:1IJQ}. FT STRAND 574 579 {ECO:0000244|PDB:1IJQ}. FT TURN 580 583 {ECO:0000244|PDB:1IJQ}. FT STRAND 584 589 {ECO:0000244|PDB:1IJQ}. FT STRAND 596 600 {ECO:0000244|PDB:1IJQ}. FT TURN 602 605 {ECO:0000244|PDB:1IJQ}. FT STRAND 606 614 {ECO:0000244|PDB:1IJQ}. FT STRAND 617 622 {ECO:0000244|PDB:1IJQ}. FT TURN 623 626 {ECO:0000244|PDB:1IJQ}. FT STRAND 627 632 {ECO:0000244|PDB:1IJQ}. FT TURN 633 635 {ECO:0000244|PDB:1IJQ}. FT STRAND 640 643 {ECO:0000244|PDB:1IJQ}. FT STRAND 652 656 {ECO:0000244|PDB:1IJQ}. FT HELIX 657 659 {ECO:0000244|PDB:1IJQ}. FT STRAND 668 672 {ECO:0000244|PDB:1IJQ}. FT HELIX 673 676 {ECO:0000244|PDB:1IJQ}. FT STRAND 678 683 {ECO:0000244|PDB:1IJQ}. FT STRAND 693 697 {ECO:0000244|PDB:1IJQ}. FT STRAND 708 713 {ECO:0000244|PDB:3P5B}. FT STRAND 821 824 {ECO:0000244|PDB:3SO6}. FT TURN 826 829 {ECO:0000244|PDB:3SO6}. SQ SEQUENCE 860 AA; 95376 MW; A4C28E9B8BADAD5E CRC64; MGPWGWKLRW TVALLLAAAG TAVGDRCERN EFQCQDGKCI SYKWVCDGSA ECQDGSDESQ ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GQVDCDNGSD EQGCPPKTCS QDEFRCHDGK CISRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW PQRCRGLYVF QGDSSPCSAF EFHCLSGECI HSSWRCDGGP DCKDKSDEEN CAVATCRPDE FQCSDGNCIH GSRQCDREYD CKDMSDEVGC VNVTLCEGPN KFKCHSGECI TLDKVCNMAR DCRDWSDEPI KECGTNECLD NNGGCSHVCN DLKIGYECLC PDGFQLVAQR RCEDIDECQD PDTCSQLCVN LEGGYKCQCE EGFQLDPHTK ACKAVGSIAY LFFTNRHEVR KMTLDRSEYT SLIPNLRNVV ALDTEVASNR IYWSDLSQRM ICSTQLDRAH GVSSYDTVIS RDIQAPDGLA VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA KIKKGGLNGV DIYSLVTENI QWPNGITLDL LSGRLYWVDS KLHSISSIDV NGGNRKTILE DEKRLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDVN LLAENLLSPE DMVLFHNLTQ PRGVNWCERT TLSNGGCQYL CLPAPQINPH SPKFTCACPD GMLLARDMRS CLTEAEAAVA TQETSTVRLK VSSTAVRTQH TTTRPVPDTS RLPGATPGLT TVEIVTMSHQ ALGDVAGRGN EKKPSSVRAL SIVLPIVLLV FLCLGVFLLW KNWRLKNINS INFDNPVYQK TTEDEVHICH NQDGYSYPSR QMVSLEDDVA //