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APOL1_HUMAN
ID   APOL1_HUMAN             Reviewed;         398 AA.
AC   O14791; A5PLQ4; B4DU12; E9PF24; O60804; Q5R3P7; Q5R3P8; Q96AB8; Q96PM4;
AC   Q9BQ03;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 5.
DT   03-AUG-2022, entry version 185.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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, and
RT   plasma distribution of apolipoprotein L.";
RL   J. Biol. Chem. 272:25576-25582(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2),
RP   SEQUENCE REVISION TO 155 AND 346, AND VARIANTS LYS-150; ILE-228 AND
RP   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, classification,
RT   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 and is
RT   expressed in human vascular tissue.";
RL   Genomics 79:539-546(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS LYS-150;
RP   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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., 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., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., 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., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   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 project:
RT   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., Moore R.J.,
RA   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., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   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 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., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal 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 stage
RT   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 African
RT   Americans.";
RL   Science 329:841-845(2010).
CC   -!- FUNCTION: May play a role in lipid exchange and transport throughout
CC       the body. May participate in reverse cholesterol transport from
CC       peripheral cells to the liver.
CC   -!- SUBUNIT: In plasma, interacts with APOA1 and mainly associated with
CC       large high density lipoprotein particles.
CC   -!- INTERACTION:
CC       O14791; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-1221934, EBI-396137;
CC       O14791; 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       Name=2; Synonyms=B;
CC         IsoId=O14791-2; Sequence=VSP_000292;
CC       Name=3;
CC         IsoId=O14791-3; Sequence=VSP_045077;
CC   -!- TISSUE SPECIFICITY: Plasma. Found on APOA-I-containing high density
CC       lipoprotein (HDL3). Expressed in pancreas, lung, prostate, liver,
CC       placenta and spleen.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000269|PubMed:26091039}.
CC   -!- DISEASE: Focal segmental glomerulosclerosis 4 (FSGS4) [MIM:612551]: A
CC       renal pathology defined by the presence of segmental sclerosis in
CC       glomeruli and resulting in proteinuria, reduced glomerular filtration
CC       rate and progressive decline in renal function. Renal insufficiency
CC       often progresses to end-stage renal disease, a highly morbid state
CC       requiring either dialysis therapy or kidney transplantation.
CC       {ECO:0000269|PubMed:20635188, ECO:0000269|PubMed:20647424}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC   -!- SIMILARITY: Belongs to the apolipoprotein L family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB81218.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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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   PDB; 7L6K; NMR; -; A=61-172.
DR   PDB; 7LF7; X-ray; 2.03 A; K/M=61-172.
DR   PDB; 7LFA; X-ray; 1.86 A; A/C=61-172.
DR   PDB; 7LFB; X-ray; 1.91 A; X=61-172.
DR   PDB; 7LFD; X-ray; 2.16 A; A=152-168.
DR   PDBsum; 7L6K; -.
DR   PDBsum; 7LF7; -.
DR   PDBsum; 7LFA; -.
DR   PDBsum; 7LFB; -.
DR   PDBsum; 7LFD; -.
DR   AlphaFoldDB; O14791; -.
DR   SMR; O14791; -.
DR   BioGRID; 114112; 3.
DR   CORUM; O14791; -.
DR   IntAct; O14791; 3.
DR   STRING; 9606.ENSP00000317674; -.
DR   BindingDB; O14791; -.
DR   ChEMBL; CHEMBL4680021; -.
DR   DrugBank; DB11886; Infigratinib.
DR   DrugBank; DB00877; Sirolimus.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   TCDB; 1.C.127.1.1; the pore-forming trypanolytic apolipoprotein a1 factor (apol1) family.
DR   GlyGen; O14791; 2 sites, 2 O-linked glycans (1 site).
DR   iPTMnet; O14791; -.
DR   PhosphoSitePlus; O14791; -.
DR   BioMuta; APOL1; -.
DR   CPTAC; non-CPTAC-2628; -.
DR   jPOST; O14791; -.
DR   MassIVE; O14791; -.
DR   MaxQB; O14791; -.
DR   PaxDb; O14791; -.
DR   PeptideAtlas; O14791; -.
DR   PRIDE; O14791; -.
DR   ProteomicsDB; 20010; -.
DR   ProteomicsDB; 48240; -. [O14791-1]
DR   ProteomicsDB; 48241; -. [O14791-2]
DR   Antibodypedia; 875; 460 antibodies from 36 providers.
DR   DNASU; 8542; -.
DR   Ensembl; ENST00000319136.8; ENSP00000317674.4; ENSG00000100342.21. [O14791-2]
DR   Ensembl; ENST00000397278.8; ENSP00000380448.4; ENSG00000100342.21. [O14791-1]
DR   Ensembl; ENST00000397279.8; ENSP00000380449.4; ENSG00000100342.21. [O14791-1]
DR   Ensembl; ENST00000422706.5; ENSP00000411507.1; ENSG00000100342.21. [O14791-1]
DR   Ensembl; ENST00000426053.5; ENSP00000388477.1; ENSG00000100342.21. [O14791-3]
DR   GeneID; 8542; -.
DR   KEGG; hsa:8542; -.
DR   MANE-Select; ENST00000397278.8; ENSP00000380448.4; NM_003661.4; NP_003652.2.
DR   UCSC; uc003ape.4; human. [O14791-1]
DR   CTD; 8542; -.
DR   DisGeNET; 8542; -.
DR   GeneCards; APOL1; -.
DR   HGNC; HGNC:618; APOL1.
DR   HPA; ENSG00000100342; Tissue enhanced (liver).
DR   MalaCards; APOL1; -.
DR   MIM; 603743; gene.
DR   MIM; 612551; phenotype.
DR   neXtProt; NX_O14791; -.
DR   OpenTargets; ENSG00000100342; -.
DR   Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR   PharmGKB; PA24904; -.
DR   VEuPathDB; HostDB:ENSG00000100342; -.
DR   eggNOG; ENOG502RZGU; Eukaryota.
DR   GeneTree; ENSGT01030000234599; -.
DR   HOGENOM; CLU_046288_1_0_1; -.
DR   InParanoid; O14791; -.
DR   PhylomeDB; O14791; -.
DR   TreeFam; TF334681; -.
DR   PathwayCommons; O14791; -.
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   SignaLink; O14791; -.
DR   BioGRID-ORCS; 8542; 11 hits in 1077 CRISPR screens.
DR   ChiTaRS; APOL1; human.
DR   GeneWiki; APOL1; -.
DR   GenomeRNAi; 8542; -.
DR   Pharos; O14791; Tbio.
DR   PRO; PR:O14791; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; O14791; protein.
DR   Bgee; ENSG00000100342; Expressed in gall bladder and 177 other tissues.
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:1902476; P:chloride transmembrane transport; IDA:BHF-UCL.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:BHF-UCL.
DR   GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   InterPro; IPR008405; ApoL.
DR   PANTHER; PTHR14096; PTHR14096; 1.
DR   Pfam; PF05461; ApoL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cholesterol metabolism;
KW   Direct protein sequencing; Disease variant; Glycoprotein; HDL;
KW   Lipid metabolism; Lipid transport; Phosphoprotein; Reference proteome;
KW   Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:9325276"
FT   CHAIN           28..398
FT                   /note="Apolipoprotein L1"
FT                   /id="PRO_0000002040"
FT   REGION          35..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         311
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         314
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   VAR_SEQ         1
FT                   /note="M -> MRFKSHTVELRRPCSDM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11290834"
FT                   /id="VSP_000292"
FT   VAR_SEQ         16..33
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045077"
FT   VARIANT         150
FT                   /note="E -> K (in dbSNP:rs2239785)"
FT                   /evidence="ECO:0000269|PubMed:11290834,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:9325276"
FT                   /id="VAR_011383"
FT   VARIANT         188
FT                   /note="I -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036568"
FT   VARIANT         228
FT                   /note="M -> I (in dbSNP:rs136175)"
FT                   /evidence="ECO:0000269|PubMed:11290834,
FT                   ECO:0000269|PubMed:11944986, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:9325276"
FT                   /id="VAR_011384"
FT   VARIANT         255
FT                   /note="R -> K (in dbSNP:rs136176)"
FT                   /evidence="ECO:0000269|PubMed:11290834,
FT                   ECO:0000269|PubMed:11944986, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:9325276"
FT                   /id="VAR_011385"
FT   VARIANT         337
FT                   /note="D -> N (in dbSNP:rs16996616)"
FT                   /id="VAR_046641"
FT   VARIANT         342
FT                   /note="S -> G (in FSGS4; dbSNP:rs73885319)"
FT                   /evidence="ECO:0000269|PubMed:11944986,
FT                   ECO:0000269|PubMed:20635188, ECO:0000269|PubMed:20647424"
FT                   /id="VAR_063598"
FT   VARIANT         384
FT                   /note="I -> M (in FSGS4; dbSNP:rs60910145)"
FT                   /evidence="ECO:0000269|PubMed:11944986,
FT                   ECO:0000269|PubMed:20635188, ECO:0000269|PubMed:20647424"
FT                   /id="VAR_061995"
FT   CONFLICT        24
FT                   /note="G -> R (in Ref. 1; AAG53690 and 2; AAK11591)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="E -> G (in Ref. 3; AAK20210)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346
FT                   /note="V -> A (in Ref. 3; AAK20210)"
FT                   /evidence="ECO:0000305"
FT   HELIX           67..75
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   HELIX           91..100
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   HELIX           105..125
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   HELIX           127..129
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:7L6K"
FT   HELIX           134..158
FT                   /evidence="ECO:0007829|PDB:7LFA"
FT   HELIX           162..167
FT                   /evidence="ECO:0007829|PDB:7LFA"
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
 
 
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