ID APOL1_HUMAN Reviewed; 398 AA. AC O14791; A5PLQ4; B4DU12; E9PF24; O60804; Q5R3P7; Q5R3P8; Q96AB8; AC Q96PM4; Q9BQ03; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 5. DT 13-FEB-2019, entry version 167. DE RecName: Full=Apolipoprotein L1; DE AltName: Full=Apolipoprotein L; DE Short=Apo-L; DE Short=ApoL; DE AltName: Full=Apolipoprotein L-I; DE Short=ApoL-I; DE Flags: Precursor; GN Name=APOL1; Synonyms=APOL; 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), PROTEIN SEQUENCE OF 28-63, AND RP VARIANTS LYS-150; ILE-228 AND LYS-255. RC TISSUE=Pancreas; RX PubMed=9325276; DOI=10.1074/jbc.272.41.25576; RA Duchateau P.N., Pullinger C.R., Orellana R.E., Kunitake S.T., RA Naya-Vigne J., O'Connor P.M., Malloy M.J., Kane J.P.; RT "Apolipoprotein L, a new human high density lipoprotein apolipoprotein RT expressed by the pancreas. Identification, cloning, characterization, RT and plasma distribution of apolipoprotein L."; RL J. Biol. Chem. 272:25576-25582(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RP 2), SEQUENCE REVISION TO 155 AND 346, AND VARIANTS LYS-150; ILE-228 RP AND LYS-255. RC TISSUE=Pancreas; RX PubMed=11290834; RA Duchateau P.N., Pullinger C.R., Cho M.H., Eng C., Kane J.P.; RT "Apolipoprotein L gene family: tissue-specific expression, splicing, RT promoter regions; discovery of a new gene."; RL J. Lipid Res. 42:620-630(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=11374903; DOI=10.1006/geno.2001.6534; RA Page N.M., Butlin D.J., Lomthaisong K., Lowry P.J.; RT "The human apolipoprotein L gene cluster: identification, RT classification, and sites of distribution."; RL Genomics 74:71-78(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-228; LYS-255; RP GLY-342 AND MET-384. RX PubMed=11944986; DOI=10.1006/geno.2002.6729; RA Monajemi H., Fontijn R.D., Pannekoek H., Horrevoets A.J.G.; RT "The apolipoprotein L gene cluster has emerged recently in evolution RT and is expressed in human vascular tissue."; RL Genomics 79:539-546(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS RP LYS-150; ILE-228 AND LYS-255. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-314, AND 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 [10] RP PHOSPHORYLATION AT SER-311 AND SER-314. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted RT phosphoproteome."; RL Cell 161:1619-1632(2015). RN [11] RP VARIANT [LARGE SCALE ANALYSIS] THR-188. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [12] RP VARIANTS FSGS4 GLY-342 AND MET-384. RX PubMed=20635188; DOI=10.1007/s00439-010-0861-0; RA Tzur S., Rosset S., Shemer R., Yudkovsky G., Selig S., Tarekegn A., RA Bekele E., Bradman N., Wasser W.G., Behar D.M., Skorecki K.; RT "Missense mutations in the APOL1 gene are highly associated with end RT stage kidney disease risk previously attributed to the MYH9 gene."; RL Hum. Genet. 128:345-350(2010). RN [13] RP VARIANTS FSGS4 GLY-342 AND MET-384. RX PubMed=20647424; DOI=10.1126/science.1193032; RA Genovese G., Friedman D.J., Ross M.D., Lecordier L., Uzureau P., RA Freedman B.I., Bowden D.W., Langefeld C.D., Oleksyk T.K., RA Uscinski Knob A.L., Bernhardy A.J., Hicks P.J., Nelson G.W., RA Vanhollebeke B., Winkler C.A., Kopp J.B., Pays E., Pollak M.R.; RT "Association of trypanolytic ApoL1 variants with kidney disease in RT African Americans."; RL Science 329:841-845(2010). CC -!- FUNCTION: May play a role in lipid exchange and transport CC throughout the body. May participate in reverse cholesterol CC transport from peripheral cells to the liver. CC -!- SUBUNIT: In plasma, interacts with APOA1 and mainly associated CC with large high density lipoprotein particles. CC -!- INTERACTION: CC Q9UJX2:CDC23; NbExp=3; IntAct=EBI-1221934, EBI-396137; CC Q8IXL6:FAM20C; NbExp=2; IntAct=EBI-1221934, EBI-7147442; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=A; CC IsoId=O14791-1; Sequence=Displayed; CC Note=Major isoform.; CC Name=2; Synonyms=B; CC IsoId=O14791-2; Sequence=VSP_000292; CC Name=3; CC IsoId=O14791-3; Sequence=VSP_045077; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Plasma. Found on APOA-I-containing high CC density lipoprotein (HDL3). Expressed in pancreas, lung, prostate, CC liver, placenta and spleen. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000269|PubMed:26091039}. CC -!- DISEASE: Focal segmental glomerulosclerosis 4 (FSGS4) CC [MIM:612551]: A renal pathology defined by the presence of CC segmental sclerosis in glomeruli and resulting in proteinuria, CC reduced glomerular filtration rate and progressive decline in CC renal function. Renal insufficiency often progresses to end-stage CC renal disease, a highly morbid state requiring either dialysis CC therapy or kidney transplantation. {ECO:0000269|PubMed:20635188, CC ECO:0000269|PubMed:20647424}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the apolipoprotein L family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB81218.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF019225; AAB81218.2; ALT_INIT; mRNA. DR EMBL; AF323540; AAG53690.1; -; mRNA. DR EMBL; AF323548; AAK11591.1; -; Genomic_DNA. DR EMBL; AF323543; AAK11591.1; JOINED; Genomic_DNA. DR EMBL; AF323544; AAK11591.1; JOINED; Genomic_DNA. DR EMBL; AF323545; AAK11591.1; JOINED; Genomic_DNA. DR EMBL; AF323546; AAK11591.1; JOINED; Genomic_DNA. DR EMBL; AF323547; AAK11591.1; JOINED; Genomic_DNA. DR EMBL; AF305224; AAK20210.1; -; mRNA. DR EMBL; AF305428; AAL09358.1; -; mRNA. DR EMBL; AK300454; BAG62174.1; -; mRNA. DR EMBL; Z82215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC143039; AAI43040.1; -; mRNA. DR CCDS; CCDS13925.1; -. [O14791-2] DR CCDS; CCDS13926.1; -. [O14791-1] DR CCDS; CCDS46702.1; -. [O14791-3] DR RefSeq; NP_001130012.1; NM_001136540.1. [O14791-1] DR RefSeq; NP_001130013.1; NM_001136541.1. [O14791-3] DR RefSeq; NP_003652.2; NM_003661.3. [O14791-1] DR RefSeq; XP_005261853.1; XM_005261796.3. DR UniGene; Hs.114309; -. DR ProteinModelPortal; O14791; -. DR BioGrid; 114112; 2. DR CORUM; O14791; -. DR IntAct; O14791; 3. DR STRING; 9606.ENSP00000317674; -. DR iPTMnet; O14791; -. DR PhosphoSitePlus; O14791; -. DR BioMuta; APOL1; -. DR jPOST; O14791; -. DR MaxQB; O14791; -. DR PaxDb; O14791; -. DR PeptideAtlas; O14791; -. DR PRIDE; O14791; -. DR ProteomicsDB; 48240; -. DR ProteomicsDB; 48241; -. [O14791-2] DR Ensembl; ENST00000319136; ENSP00000317674; ENSG00000100342. [O14791-2] DR Ensembl; ENST00000397278; ENSP00000380448; ENSG00000100342. [O14791-1] DR Ensembl; ENST00000397279; ENSP00000380449; ENSG00000100342. [O14791-1] DR Ensembl; ENST00000422706; ENSP00000411507; ENSG00000100342. [O14791-1] DR Ensembl; ENST00000426053; ENSP00000388477; ENSG00000100342. [O14791-3] DR GeneID; 8542; -. DR KEGG; hsa:8542; -. DR UCSC; uc003ape.4; human. [O14791-1] DR CTD; 8542; -. DR DisGeNET; 8542; -. DR EuPathDB; HostDB:ENSG00000100342.20; -. DR GeneCards; APOL1; -. DR H-InvDB; HIX0016423; -. DR HGNC; HGNC:618; APOL1. DR HPA; CAB056156; -. DR HPA; HPA018885; -. DR MalaCards; APOL1; -. DR MIM; 603743; gene. DR MIM; 612551; phenotype. DR neXtProt; NX_O14791; -. DR OpenTargets; ENSG00000100342; -. DR Orphanet; 93218; Sporadic idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis. DR PharmGKB; PA24904; -. DR eggNOG; ENOG410KC8P; Eukaryota. DR eggNOG; ENOG4110P7Y; LUCA. DR GeneTree; ENSGT00510000046700; -. DR HOGENOM; HOG000294132; -. DR HOVERGEN; HBG074468; -. DR InParanoid; O14791; -. DR KO; K14480; -. DR OMA; VQKVHKG; -. DR OrthoDB; 1060131at2759; -. DR PhylomeDB; O14791; -. DR TreeFam; TF334681; -. DR Reactome; R-HSA-2168880; Scavenging of heme from plasma. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR ChiTaRS; APOL1; human. DR GeneWiki; APOL1; -. DR GenomeRNAi; 8542; -. DR PRO; PR:O14791; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000100342; Expressed in 207 organ(s), highest expression level in epithelium of bronchus. DR ExpressionAtlas; O14791; baseline and differential. DR Genevisible; O14791; HS. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0031224; C:intrinsic component of membrane; IC:BHF-UCL. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL. DR GO; GO:0005254; F:chloride channel activity; IDA:BHF-UCL. DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:1902476; P:chloride transmembrane transport; IDA:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0019835; P:cytolysis; IDA:BHF-UCL. DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL. DR GO; GO:0031640; P:killing of cells of other organism; IDA:BHF-UCL. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR InterPro; IPR008405; ApoL. DR PANTHER; PTHR14096; PTHR14096; 1. DR Pfam; PF05461; ApoL; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cholesterol metabolism; Complete proteome; KW Direct protein sequencing; Disease mutation; Glycoprotein; HDL; KW Lipid metabolism; Lipid transport; Phosphoprotein; Polymorphism; KW Reference proteome; Secreted; Signal; Steroid metabolism; KW Sterol metabolism; Transport. FT SIGNAL 1 27 {ECO:0000269|PubMed:9325276}. FT CHAIN 28 398 Apolipoprotein L1. FT /FTId=PRO_0000002040. FT MOD_RES 311 311 Phosphoserine; by FAM20C. FT {ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:26091039}. FT MOD_RES 314 314 Phosphoserine; by FAM20C. FT {ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:26091039}. FT CARBOHYD 261 261 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT VAR_SEQ 1 1 M -> MRFKSHTVELRRPCSDM (in isoform 2). FT {ECO:0000303|PubMed:11290834}. FT /FTId=VSP_000292. FT VAR_SEQ 16 33 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045077. FT VARIANT 150 150 E -> K (in dbSNP:rs2239785). FT {ECO:0000269|PubMed:11290834, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9325276}. FT /FTId=VAR_011383. FT VARIANT 188 188 I -> T (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036568. FT VARIANT 228 228 M -> I (in dbSNP:rs136175). FT {ECO:0000269|PubMed:11290834, FT ECO:0000269|PubMed:11944986, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9325276}. FT /FTId=VAR_011384. FT VARIANT 255 255 R -> K (in dbSNP:rs136176). FT {ECO:0000269|PubMed:11290834, FT ECO:0000269|PubMed:11944986, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9325276}. FT /FTId=VAR_011385. FT VARIANT 337 337 D -> N (in dbSNP:rs16996616). FT /FTId=VAR_046641. FT VARIANT 342 342 S -> G (in FSGS4; dbSNP:rs73885319). FT {ECO:0000269|PubMed:11944986, FT ECO:0000269|PubMed:20635188, FT ECO:0000269|PubMed:20647424}. FT /FTId=VAR_063598. FT VARIANT 384 384 I -> M (in FSGS4; dbSNP:rs60910145). FT {ECO:0000269|PubMed:11944986, FT ECO:0000269|PubMed:20635188, FT ECO:0000269|PubMed:20647424}. FT /FTId=VAR_061995. FT CONFLICT 24 24 G -> R (in Ref. 1; AAG53690 and 2; FT AAK11591). {ECO:0000305}. FT CONFLICT 256 256 E -> G (in Ref. 3; AAK20210). FT {ECO:0000305}. FT CONFLICT 346 346 V -> A (in Ref. 3; AAK20210). FT {ECO:0000305}. SQ SEQUENCE 398 AA; 43974 MW; BD1A8F1D7C5A889F CRC64; MEGAALLRVS VLCIWMSALF LGVGVRAEEA GARVQQNVPS GTDTGDPQSK PLGDWAAGTM DPESSIFIED AIKYFKEKVS TQNLLLLLTD NEAWNGFVAA AELPRNEADE LRKALDNLAR QMIMKDKNWH DKGQQYRNWF LKEFPRLKSE LEDNIRRLRA LADGVQKVHK GTTIANVVSG SLSISSGILT LVGMGLAPFT EGGSLVLLEP GMELGITAAL TGITSSTMDY GKKWWTQAQA HDLVIKSLDK LKEVREFLGE NISNFLSLAG NTYQLTRGIG KDIRALRRAR ANLQSVPHAS ASRPRVTEPI SAESGEQVER VNEPSILEMS RGVKLTDVAP VSFFLVLDVV YLVYESKHLH EGAKSETAEE LKKVAQELEE KLNILNNNYK ILQADQEL //