SO3A1_HUMAN
ID SO3A1_HUMAN Reviewed; 710 AA.
AC Q9UIG8; A8K4A7; B3KPY5; B3KUR7; C6G486; Q9BW73; Q9GZV2;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Solute carrier organic anion transporter family member 3A1;
DE Short=OATP3A1;
DE AltName: Full=Organic anion transporter polypeptide-related protein 3;
DE Short=OATP-RP3;
DE Short=OATPRP3;
DE AltName: Full=Organic anion-transporting polypeptide D;
DE Short=OATP-D;
DE AltName: Full=PGE1 transporter;
DE AltName: Full=Sodium-independent organic anion transporter D;
DE AltName: Full=Solute carrier family 21 member 11;
GN Name=SLCO3A1; Synonyms=OATP3A1, OATPD, SLC21A11;
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), FUNCTION, AND VARIANT ASP-294.
RC TISSUE=Kidney;
RX PubMed=10873595; DOI=10.1006/bbrc.2000.2922;
RA Tamai I., Nezu J., Uchino H., Sai Y., Oku A., Shimane M., Tsuji A.;
RT "Molecular identification and characterization of novel members of the
RT human organic anion transporter (OATP) family.";
RL Biochem. Biophys. Res. Commun. 273:251-260(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-294.
RA Wu Y., Hsiang B.H., Zhu Y., Yang W.-P., Kirchgessner T.G.;
RT "Identification and characterization of novel human OATP family members.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-294.
RA Adachi H., Unno M., Matsuno S., Yawo H., Abe T.;
RT "Molecular identification of human PGE1 transporter expressed in cancer.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP ASP-294.
RC TISSUE=Mesangial cell, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASP-294.
RC TISSUE=Brain;
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 ALTERNATIVE SPLICING, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=16971491; DOI=10.1152/ajpcell.00597.2005;
RA Huber R.D., Gao B., Sidler Pfaendler M.-A., Zhang-Fu W., Leuthold S.,
RA Hagenbuch B., Folkers G., Meier P.J., Stieger B.;
RT "Characterization of two splice variants of human organic anion
RT transporting polypeptide 3A1 isolated from human brain.";
RL Am. J. Physiol. 292:C795-C806(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP ACETYLATION AT MET-1.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: Mediates the Na(+)-independent transport of organic anions
CC such as estrone-3-sulfate (PubMed:10873595). Mediates transport of
CC prostaglandins (PG) E1 and E2, thyroxine (T4), deltorphin II, BQ-123
CC and vasopressin, but not DPDPE (a derivative of enkephalin lacking an
CC N-terminal tyrosine residue), estrone-3-sulfate, taurocholate, digoxin
CC nor DHEAS (PubMed:16971491). {ECO:0000269|PubMed:10873595,
CC ECO:0000269|PubMed:16971491}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=101 nM for PGE1 (isoform 1) {ECO:0000269|PubMed:16971491};
CC KM=218 nM for PGE1 (isoform 2) {ECO:0000269|PubMed:16971491};
CC KM=219 nM for PGE2 (isoform 1) {ECO:0000269|PubMed:16971491};
CC KM=371 nM for PGE2 (isoform 2) {ECO:0000269|PubMed:16971491};
CC -!- INTERACTION:
CC Q9UIG8-2; Q13520: AQP6; NbExp=3; IntAct=EBI-13041931, EBI-13059134;
CC Q9UIG8-2; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-13041931, EBI-12003442;
CC Q9UIG8-2; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-13041931, EBI-712073;
CC Q9UIG8-2; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-13041931, EBI-11988865;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=OATP3A1-v1;
CC IsoId=Q9UIG8-1; Sequence=Displayed;
CC Name=2; Synonyms=OATP3A1-v2;
CC IsoId=Q9UIG8-2; Sequence=VSP_036837, VSP_036838;
CC Name=3;
CC IsoId=Q9UIG8-3; Sequence=VSP_036834, VSP_036835, VSP_036836;
CC Name=4;
CC IsoId=Q9UIG8-4; Sequence=VSP_036833;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in spleen and
CC leukocytes. Generally the expression of isoform 1 is higher than that
CC of isoform 2. Isoform 2 is particularly abundant in testis and brain.
CC In testis, isoform 1 is detected in spermatogonia at different stages
CC and absent from Sertoli cells, while isoform 2 is present in both (at
CC protein level). Expressed in the choroid plexus epithelium, isoform 1
CC being localized at the basolateral membrane and isoform 2 at the apical
CC one, as well as in the subapical intracellular vesicular compartments.
CC Differential expression of both isoforms is also observed in other
CC brain region: isoform 1 is very abundant in the gray matter of the
CC frontal cortex, but is not associated with neuronal cell bodies. Not
CC detected in the white matter. In contrast, isoform 2 is associated with
CC neuronal bodies and axons in both the gray and the white matters of the
CC frontal cortex. {ECO:0000269|PubMed:16971491}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AB031050; BAA89287.1; -; mRNA.
DR EMBL; AF205074; AAG42206.1; -; mRNA.
DR EMBL; AF187816; AAG43446.1; -; mRNA.
DR EMBL; AK290872; BAF83561.1; -; mRNA.
DR EMBL; AK057031; BAG51847.1; -; mRNA.
DR EMBL; AK097797; BAG53529.1; -; mRNA.
DR EMBL; FJ515841; ACS13734.1; -; Genomic_DNA.
DR EMBL; AC104020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000585; AAH00585.1; -; mRNA.
DR CCDS; CCDS10371.1; -. [Q9UIG8-1]
DR CCDS; CCDS45354.1; -. [Q9UIG8-2]
DR RefSeq; NP_001138516.1; NM_001145044.1. [Q9UIG8-2]
DR RefSeq; NP_037404.2; NM_013272.3. [Q9UIG8-1]
DR AlphaFoldDB; Q9UIG8; -.
DR SMR; Q9UIG8; -.
DR BioGRID; 118181; 14.
DR IntAct; Q9UIG8; 5.
DR STRING; 9606.ENSP00000320634; -.
DR ChEMBL; CHEMBL2073685; -.
DR DrugBank; DB00770; Alprostadil.
DR DrugBank; DB00345; Aminohippuric acid.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB00286; Conjugated estrogens.
DR DrugBank; DB01160; Dinoprost tromethamine.
DR DrugBank; DB00917; Dinoprostone.
DR DrugBank; DB01088; Iloprost.
DR DrugBank; DB09198; Lobeglitazone.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB06654; Safinamide.
DR DrugBank; DB04348; Taurocholic acid.
DR DrugBank; DB09100; Thyroid, porcine.
DR TCDB; 2.A.60.1.18; the organo anion transporter (oat) family.
DR GlyGen; Q9UIG8; 7 sites.
DR iPTMnet; Q9UIG8; -.
DR PhosphoSitePlus; Q9UIG8; -.
DR SwissPalm; Q9UIG8; -.
DR BioMuta; SLCO3A1; -.
DR DMDM; 296452954; -.
DR jPOST; Q9UIG8; -.
DR MassIVE; Q9UIG8; -.
DR MaxQB; Q9UIG8; -.
DR PaxDb; Q9UIG8; -.
DR PeptideAtlas; Q9UIG8; -.
DR PRIDE; Q9UIG8; -.
DR ProteomicsDB; 84519; -. [Q9UIG8-1]
DR ProteomicsDB; 84520; -. [Q9UIG8-2]
DR ProteomicsDB; 84521; -. [Q9UIG8-3]
DR ProteomicsDB; 84522; -. [Q9UIG8-4]
DR Antibodypedia; 29012; 77 antibodies from 16 providers.
DR DNASU; 28232; -.
DR Ensembl; ENST00000318445.11; ENSP00000320634.6; ENSG00000176463.14. [Q9UIG8-1]
DR Ensembl; ENST00000424469.2; ENSP00000387846.2; ENSG00000176463.14. [Q9UIG8-2]
DR GeneID; 28232; -.
DR KEGG; hsa:28232; -.
DR MANE-Select; ENST00000318445.11; ENSP00000320634.6; NM_013272.4; NP_037404.2.
DR UCSC; uc002bqx.3; human. [Q9UIG8-1]
DR CTD; 28232; -.
DR DisGeNET; 28232; -.
DR GeneCards; SLCO3A1; -.
DR HGNC; HGNC:10952; SLCO3A1.
DR HPA; ENSG00000176463; Tissue enhanced (brain).
DR MIM; 612435; gene.
DR neXtProt; NX_Q9UIG8; -.
DR OpenTargets; ENSG00000176463; -.
DR PharmGKB; PA35837; -.
DR VEuPathDB; HostDB:ENSG00000176463; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_3_0_1; -.
DR InParanoid; Q9UIG8; -.
DR OMA; CNINCEC; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9UIG8; -.
DR TreeFam; TF317540; -.
DR PathwayCommons; Q9UIG8; -.
DR Reactome; R-HSA-879518; Transport of organic anions. [Q9UIG8-1]
DR SignaLink; Q9UIG8; -.
DR BioGRID-ORCS; 28232; 4 hits in 1061 CRISPR screens.
DR ChiTaRS; SLCO3A1; human.
DR GeneWiki; SLCO3A1; -.
DR GenomeRNAi; 28232; -.
DR Pharos; Q9UIG8; Tbio.
DR PRO; PR:Q9UIG8; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UIG8; protein.
DR Bgee; ENSG00000176463; Expressed in buccal mucosa cell and 188 other tissues.
DR ExpressionAtlas; Q9UIG8; baseline and differential.
DR Genevisible; Q9UIG8; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:ARUK-UCL.
DR GO; GO:0015732; P:prostaglandin transport; IDA:ARUK-UCL.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..710
FT /note="Solute carrier organic anion transporter family
FT member 3A1"
FT /id="PRO_0000191064"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..410
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..438
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..562
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..597
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..648
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 465..513
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:25732826"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 471..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 477..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 486..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036833"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036834"
FT VAR_SEQ 59..60
FT /note="YL -> MN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036835"
FT VAR_SEQ 641..710
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036836"
FT VAR_SEQ 667..692
FT /note="EFFASTLTLDNLGRDPVPANQTHRTK -> TEYQDIETEKTCPESHSPSEDS
FT FVRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036837"
FT VAR_SEQ 693..710
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036838"
FT VARIANT 294
FT /note="E -> D (in dbSNP:rs1517618)"
FT /evidence="ECO:0000269|PubMed:10873595,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT /id="VAR_054853"
FT CONFLICT 40
FT /note="K -> R (in Ref. 4; BAF83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="R -> L (in Ref. 7; AAH00585)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="G -> D (in Ref. 4; BAF83561)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> Y (in Ref. 1; BAA89287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 76553 MW; ED56724BA0998553 CRC64;
MQGKKPGGSS GGGRSGELQG DEAQRNKKKK KKVSCFSNIK IFLVSECALM LAQGTVGAYL
VSVLTTLERR FNLQSADVGV IASSFEIGNL ALILFVSYFG ARGHRPRLIG CGGIVMALGA
LLSALPEFLT HQYKYEAGEI RWGAEGRDVC AANGSGGDEG PDPDLICRNR TATNMMYLLL
IGAQVLLGIG ATPVQPLGVS YIDDHVRRKD SSLYIGILFT MLVFGPACGF ILGSFCTKIY
VDAVFIDTSN LDITPDDPRW IGAWWGGFLL CGALLFFSSL LMFGFPQSLP PHSEPAMESE
QAMLSEREYE RPKPSNGVLR HPLEPDSSAS CFQQLRVIPK VTKHLLSNPV FTCIILAACM
EIAVVAGFAA FLGKYLEQQF NLTTSSANQL LGMTAIPCAC LGIFLGGLLV KKLSLSALGA
IRMAMLVNLV STACYVSFLF LGCDTGPVAG VTVPYGNSTA PGSALDPYSP CNNNCECQTD
SFTPVCGADG ITYLSACFAG CNSTNLTGCA CLTTVPAENA TVVPGKCPSP GCQEAFLTFL
CVMCICSLIG AMAQTPSVII LIRTVSPELK SYALGVLFLL LRLLGFIPPP LIFGAGIDST
CLFWSTFCGE QGACVLYDNV VYRYLYVSIA IALKSFAFIL YTTTWQCLRK NYKRYIKNHE
GGLSTSEFFA STLTLDNLGR DPVPANQTHR TKFIYNLEDH EWCENMESVL
