ID LAMB4_HUMAN Reviewed; 1761 AA. AC A4D0S4; A5PKU6; B2RTT3; B5MEB9; Q86TP7; Q86XN2; Q8NBX5; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 13-FEB-2019, entry version 101. DE RecName: Full=Laminin subunit beta-4; DE AltName: Full=Laminin beta-1-related protein; DE Flags: Precursor; GN Name=LAMB4; 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). RC TISSUE=Placenta; RA Olson P.F., Koch M., Champliaud M.F., Rowland K., Jin W., RA Burgeson R.E.; RT "Cloning and characterization of the human laminin beta-4 chain."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] 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 (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1761 (ISOFORM 3). RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1528-1761 (ISOFORM 1). RC TISSUE=Placenta; 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 [6] RP VARIANT CYS-1028. RX PubMed=25787250; DOI=10.1073/pnas.1503696112; RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W., RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., RA Stalberg P., Akerstroem G., Westin G., Hellman P., Carling T., RA Bjoerklund P., Lifton R.P.; RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in RT insulin-producing adenomas."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin CC is thought to mediate the attachment, migration and organization CC of cells into tissues during embryonic development by interacting CC with other extracellular matrix components. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound CC to each other by disulfide bonds into a cross-shaped molecule CC comprising one long and three short arms with globules at each CC end. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=A4D0S4-1; Sequence=Displayed; CC Name=2; CC IsoId=A4D0S4-2; Sequence=VSP_029913, VSP_029914; CC Name=3; CC IsoId=A4D0S4-3; Sequence=VSP_029915, VSP_029916; CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact CC with other laminin chains to form a coiled coil structure. CC -!- DOMAIN: Domains VI and IV are globular. 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; AF028816; AAC95123.1; -; mRNA. DR EMBL; AC005048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236947; EAL24387.1; -; Genomic_DNA. DR EMBL; BC045172; AAH45172.2; -; mRNA. DR EMBL; BC140804; AAI40805.1; -; mRNA. DR EMBL; BC142619; AAI42620.1; -; mRNA. DR EMBL; AK075165; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS34732.1; -. [A4D0S4-1] DR CCDS; CCDS83218.1; -. [A4D0S4-2] DR RefSeq; NP_001304975.1; NM_001318046.1. [A4D0S4-1] DR RefSeq; NP_001304977.1; NM_001318048.1. DR RefSeq; NP_031382.2; NM_007356.2. [A4D0S4-1] DR RefSeq; XP_011514280.1; XM_011515978.1. [A4D0S4-3] DR UniGene; Hs.62022; -. DR ProteinModelPortal; A4D0S4; -. DR SMR; A4D0S4; -. DR BioGrid; 116479; 2. DR IntAct; A4D0S4; 1. DR STRING; 9606.ENSP00000205386; -. DR ChEMBL; CHEMBL2364187; -. DR iPTMnet; A4D0S4; -. DR PhosphoSitePlus; A4D0S4; -. DR BioMuta; LAMB4; -. DR EPD; A4D0S4; -. DR jPOST; A4D0S4; -. DR PaxDb; A4D0S4; -. DR PRIDE; A4D0S4; -. DR ProteomicsDB; 592; -. DR ProteomicsDB; 593; -. [A4D0S4-2] DR ProteomicsDB; 594; -. [A4D0S4-3] DR Ensembl; ENST00000205386; ENSP00000205386; ENSG00000091128. [A4D0S4-1] DR Ensembl; ENST00000388781; ENSP00000373433; ENSG00000091128. [A4D0S4-1] DR GeneID; 22798; -. DR KEGG; hsa:22798; -. DR UCSC; uc003vey.3; human. [A4D0S4-1] DR CTD; 22798; -. DR DisGeNET; 22798; -. DR EuPathDB; HostDB:ENSG00000091128.12; -. DR GeneCards; LAMB4; -. DR HGNC; HGNC:6491; LAMB4. DR HPA; HPA020242; -. DR HPA; HPA024247; -. DR MIM; 616380; gene. DR neXtProt; NX_A4D0S4; -. DR OpenTargets; ENSG00000091128; -. DR PharmGKB; PA30279; -. DR eggNOG; KOG0994; Eukaryota. DR eggNOG; ENOG410XPEG; LUCA. DR GeneTree; ENSGT00940000162514; -. DR HOVERGEN; HBG052301; -. DR InParanoid; A4D0S4; -. DR KO; K06245; -. DR OMA; LFQFSHL; -. DR OrthoDB; 65841at2759; -. DR PhylomeDB; A4D0S4; -. DR TreeFam; TF312903; -. DR ChiTaRS; LAMB4; human. DR GenomeRNAi; 22798; -. DR PRO; PR:A4D0S4; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000091128; Expressed in 83 organ(s), highest expression level in skin of abdomen. DR ExpressionAtlas; A4D0S4; baseline and differential. DR Genevisible; A4D0S4; HS. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR Gene3D; 2.60.120.1490; -; 1. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR013015; Laminin_IV_B. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR038684; Laminin_N_sf. DR Pfam; PF00053; Laminin_EGF; 12. DR Pfam; PF00055; Laminin_N; 1. DR SMART; SM00180; EGF_Lam; 13. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 10. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; EGF_LAM_1; 11. DR PROSITE; PS50027; EGF_LAM_2; 13. DR PROSITE; PS51116; LAMININ_IVB; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Basement membrane; Cell adhesion; Coiled coil; KW Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; KW Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 1761 Laminin subunit beta-4. FT /FTId=PRO_0000312857. FT DOMAIN 24 264 Laminin N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00466}. FT DOMAIN 265 331 Laminin EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 332 394 Laminin EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 395 454 Laminin EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 455 505 Laminin EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 506 552 Laminin EGF-like 5; truncated. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 545 763 Laminin IV type B. {ECO:0000255|PROSITE- FT ProRule:PRU00462}. FT DOMAIN 769 816 Laminin EGF-like 6. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 817 862 Laminin EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 863 910 Laminin EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 911 969 Laminin EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 970 1021 Laminin EGF-like 10. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1022 1079 Laminin EGF-like 11. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1080 1127 Laminin EGF-like 12. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1128 1174 Laminin EGF-like 13. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT REGION 1175 1375 Domain II. FT REGION 1376 1408 Domain alpha. FT REGION 1409 1761 Domain I. FT COILED 1243 1301 {ECO:0000255}. FT COILED 1416 1480 {ECO:0000255}. FT COILED 1525 1759 {ECO:0000255}. FT CARBOHYD 169 169 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 229 229 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 246 246 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1016 1016 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1055 1055 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1223 1223 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1301 1301 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1326 1326 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1333 1333 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1469 1469 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1517 1517 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1587 1587 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1596 1596 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1609 1609 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1725 1725 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 265 ?274 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 267 295 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 297 306 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 309 329 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 332 341 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 334 359 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 362 371 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 374 392 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 395 408 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 397 423 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 425 434 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 437 452 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 455 468 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 457 475 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 477 486 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 489 503 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 506 518 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 508 525 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 527 536 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 769 781 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 771 788 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 790 799 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 802 814 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 817 829 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 819 836 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 838 847 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 850 860 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 863 872 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 865 879 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 882 891 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 894 908 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 913 938 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 940 949 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 952 967 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 970 984 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 972 991 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 994 1003 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1006 1019 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1022 1043 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1024 1050 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1052 1061 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1064 1077 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1080 1092 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1082 1099 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1101 1110 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1113 1125 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1128 1140 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1130 1147 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1149 1158 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1161 1172 {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DISULFID 1175 1175 Interchain. {ECO:0000305}. FT DISULFID 1178 1178 Interchain. {ECO:0000305}. FT DISULFID 1759 1759 Interchain. {ECO:0000305}. FT VAR_SEQ 709 772 LGLIPQINSLENFCSKQDLDEYQLHNCVEIASAMGPQVLPG FT ACERLIISMSAKLHDGAVACKCH -> AAVQWHNLGSLQPP FT PPECKQFSCFSFPSSWDYRHPPPHLASFCIFSRDGVSPHWP FT GWSRTPDLR (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_029913. FT VAR_SEQ 773 1761 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_029914. FT VAR_SEQ 1716 1723 DLERKIQD -> GCFQNSAR (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_029915. FT VAR_SEQ 1724 1761 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_029916. FT VARIANT 44 44 M -> T (in dbSNP:rs35644375). FT /FTId=VAR_037588. FT VARIANT 234 234 H -> Y (in dbSNP:rs2074749). FT /FTId=VAR_037589. FT VARIANT 591 591 V -> F (in dbSNP:rs9690688). FT /FTId=VAR_037590. FT VARIANT 866 866 N -> S (in dbSNP:rs2240445). FT /FTId=VAR_037591. FT VARIANT 1028 1028 G -> C (in dbSNP:rs1299564647). FT {ECO:0000269|PubMed:25787250}. FT /FTId=VAR_074174. FT VARIANT 1350 1350 T -> N (in dbSNP:rs10260756). FT /FTId=VAR_037592. FT VARIANT 1510 1510 H -> Y (in dbSNP:rs1627354). FT /FTId=VAR_037593. FT VARIANT 1612 1612 R -> S (in dbSNP:rs2528693). FT /FTId=VAR_037594. FT CONFLICT 70 70 F -> S (in Ref. 1; AAC95123). FT {ECO:0000305}. FT CONFLICT 93 93 I -> T (in Ref. 1; AAC95123). FT {ECO:0000305}. FT CONFLICT 1542 1542 L -> S (in Ref. 1; AAC95123). FT {ECO:0000305}. SQ SEQUENCE 1761 AA; 193540 MW; 57A740F079CE1FB2 CRC64; MQFQLTLFLH LGWLSYSKAQ DDCNRGACHP TTGDLLVGRN TQLMASSTCG LSRAQKYCIL SYLEGEQKCF ICDSRFPYDP YDQPNSHTIE NVIVSFEPDR EKKWWQSENG LDHVSIRLDL EALFRFSHLI LTFKTFRPAA MLVERSTDYG HNWKVFKYFA KDCATSFPNI TSGQAQGVGD IVCDSKYSDI EPSTGGEVVL KVLDPSFEIE NPYSPYIQDL VTLTNLRINF TKLHTLGDAL LGRRQNDSLD KYYYALYEMI VRGSCFCNGH ASECRPMQKM RGDVFSPPGM VHGQCVCQHN TDGPNCERCK DFFQDAPWRP AADLQDNACR SCSCNSHSSR CHFDMTTYLA SGGLSGGVCE DCQHNTEGQH CDRCRPLFYR DPLKTISDPY ACIPCECDPD GTISGGICVS HSDPALGSVA GQCLCKENVE GAKCDQCKPN HYGLSATDPL GCQPCDCNPL GSLPFLTCDV DTGQCLCLSY VTGAHCEECT VGYWGLGNHL HGCSPCDCDI GGAYSNVCSP KNGQCECRPH VTGRSCSEPA PGYFFAPLNF YLYEAEEATT LQGLAPLGSE TFGQSPAVHV VLGEPVPGNP VTWTGPGFAR VLPGAGLRFA VNNIPFPVDF TIAIHYETQS AADWTVQIVV NPPGGSEHCI PKTLQSKPQS FALPAATRIM LLPTPICLEP DVQYSIDVYF SQPLQGESHA HSHVLVDSLG LIPQINSLEN FCSKQDLDEY QLHNCVEIAS AMGPQVLPGA CERLIISMSA KLHDGAVACK CHPQGSVGSS CSRLGGQCQC KPLVVGRCCD RCSTGSYDLG HHGCHPCHCH PQGSKDTVCD QVTGQCPCHG EVSGRRCDRC LAGYFGFPSC HPCPCNRFAE LCDPETGSCF NCGGFTTGRN CERCIDGYYG NPSSGQPCRP CLCPDDPSSN QYFAHSCYQN LWSSDVICNC LQGYTGTQCG ECSTGFYGNP RISGAPCQPC ACNNNIDVTD PESCSRVTGE CLRCLHNTQG ANCQLCKPGH YGSALNQTCR RCSCHASGVS PMECPPGGGA CLCDPVTGAC PCLPNVTGLA CDRCADGYWN LVPGRGCQSC DCDPRTSQSS HCDQLTGQCP CKLGYGGKRC SECQENYYGD PPGRCIPCDC NRAGTQKPIC DPDTGMCRCR EGVSGQRCDR CARGHSQEFP TCLQCHLCFD QWDHTISSLS KAVQGLMRLA ANMEDKRETL PVCEADFKDL RGNVSEIERI LKHPVFPSGK FLKVKDYHDS VRRQIMQLNE QLKAVYEFQD LKDTIERAKN EADLLLEDLQ EEIDLQSSVL NASIADSSEN IKKYYHISSS AEKKINETSS TINTSANTRN DLLTILDTLT SKGNLSLERL KQIKIPDIQI LNEKVCGDPG NVPCVPLPCG GALCTGRKGH RKCRGPGCHG SLTLSTNALQ KAQEAKSIIR NLDKQVRGLK NQIESISEQA EVSKNNALQL REKLGNIRNQ SDSEEENINL FIKKVKNFLL EENVPPEDIE KVANGVLDIH LPIPSQNLTD ELVKIQKHMQ LCEDYRTDEN RLNEEADGAQ KLLVKAKAAE KAANILLNLD KTLNQLQQAQ ITQGRANSTI TQLTANITKI KKNVLQAENQ TREMKSELEL AKQRSGLEDG LSLLQTKLQR HQDHAVNAKV QAESAQHQAG SLEKEFVELK KQYAILQRKT STTGLTKETL GKVKQLKDAA EKLAGDTEAK IRRITDLERK IQDLNLSRQA KADQLRILED QVVAIKNEIV EQEKKYARCY S //