ID STAB1_HUMAN Reviewed; 2570 AA. AC Q9NY15; A7E297; Q8IUH0; Q8IUH1; Q93072; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 24-JAN-2024, entry version 194. DE RecName: Full=Stabilin-1; DE AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1; DE Short=FEEL-1; DE AltName: Full=MS-1 antigen; DE Flags: Precursor; GN Name=STAB1; Synonyms=FEEL1, KIAA0246; 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 {ECO:0000312|EMBL:CAB61827.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP VAL-912; PRO-1833 AND VAL-2282. RX PubMed=11829752; DOI=10.1042/0264-6021:3620155; RA Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P., RA Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J., RA Longati P., Velten F.W., Johansson S., Goerdt S.; RT "Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan RT receptor homologues."; RL Biochem. J. 362:155-164(2002). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE RP SPECIFICITY, AND VARIANT VAL-912. RX PubMed=12077138; DOI=10.1074/jbc.m204277200; RA Adachi H., Tsujimoto M.; RT "FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and RT angiogenesis-modulating activities."; RL J. Biol. Chem. 277:34264-34270(2002). RN [3] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-912 RP AND PRO-1833. RC TISSUE=Brain {ECO:0000312|EMBL:BAA13377.2}; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-912 RP AND PRO-1833. 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 [7] RP FUNCTION, AND INTERACTION WITH CHID1. RX PubMed=16357325; DOI=10.1182/blood-2005-07-2843; RA Kzhyshkowska J., Mamidi S., Gratchev A., Kremmer E., Schmuttermaier C., RA Krusell L., Haus G., Utikal J., Schledzewski K., Scholtze J., Goerdt S.; RT "Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up- RT regulated in alternatively activated macrophages and secreted via lysosomal RT pathway."; RL Blood 107:3221-3228(2006). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1096; ASN-1626; ASN-1727; RP ASN-2347 AND ASN-2424. 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 multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] 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). CC -!- FUNCTION: Acts as a scavenger receptor for acetylated low density CC lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and CC may play a role in defense against bacterial infection. When inhibited CC in endothelial tube formation assays, there is a marked decrease in CC cell-cell interactions, suggesting a role in angiogenesis. Involved in CC the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic CC compartment to the endosomal/lysosomal system. CC {ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:16357325}. CC -!- SUBUNIT: Interacts with CHID1. {ECO:0000269|PubMed:16357325}. CC -!- INTERACTION: CC Q9NY15; P02751: FN1; NbExp=2; IntAct=EBI-2797815, EBI-1220319; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:12077138}; CC IsoId=Q9NY15-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:12077138}; CC IsoId=Q9NY15-2; Sequence=VSP_050764, VSP_050765; CC -!- TISSUE SPECIFICITY: High levels found in spleen, lymph node, liver and CC placenta. Also expressed in endothelial cells. CC {ECO:0000269|PubMed:11829752, ECO:0000269|PubMed:12077138}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13377.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AJ275213; CAB61827.1; -; mRNA. DR EMBL; AB052956; BAC15606.1; -; mRNA. DR EMBL; AB052957; BAC15607.1; -; mRNA. DR EMBL; D87433; BAA13377.2; ALT_INIT; mRNA. DR EMBL; AC006208; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC150250; AAI50251.1; -; mRNA. DR CCDS; CCDS33768.1; -. [Q9NY15-1] DR RefSeq; NP_055951.2; NM_015136.2. [Q9NY15-1] DR AlphaFoldDB; Q9NY15; -. DR SMR; Q9NY15; -. DR BioGRID; 116778; 11. DR ELM; Q9NY15; -. DR IntAct; Q9NY15; 76. DR MINT; Q9NY15; -. DR STRING; 9606.ENSP00000312946; -. DR TCDB; 9.B.87.1.22; the selenoprotein p receptor (selp-receptor) family. DR GlyConnect; 681; 7 N-Linked glycans (7 sites). DR GlyCosmos; Q9NY15; 29 sites, 12 glycans. DR GlyGen; Q9NY15; 29 sites, 12 N-linked glycans (7 sites). DR iPTMnet; Q9NY15; -. DR PhosphoSitePlus; Q9NY15; -. DR BioMuta; STAB1; -. DR DMDM; 296452949; -. DR EPD; Q9NY15; -. DR jPOST; Q9NY15; -. DR MassIVE; Q9NY15; -. DR PaxDb; 9606-ENSP00000312946; -. DR PeptideAtlas; Q9NY15; -. DR ProteomicsDB; 83149; -. [Q9NY15-1] DR ProteomicsDB; 83150; -. [Q9NY15-2] DR Antibodypedia; 1505; 172 antibodies from 33 providers. DR DNASU; 23166; -. DR Ensembl; ENST00000321725.10; ENSP00000312946.6; ENSG00000010327.10. [Q9NY15-1] DR GeneID; 23166; -. DR KEGG; hsa:23166; -. DR MANE-Select; ENST00000321725.10; ENSP00000312946.6; NM_015136.3; NP_055951.2. DR UCSC; uc003dej.4; human. [Q9NY15-1] DR AGR; HGNC:18628; -. DR CTD; 23166; -. DR DisGeNET; 23166; -. DR GeneCards; STAB1; -. DR HGNC; HGNC:18628; STAB1. DR HPA; ENSG00000010327; Tissue enhanced (lymphoid). DR MIM; 608560; gene. DR neXtProt; NX_Q9NY15; -. DR OpenTargets; ENSG00000010327; -. DR PharmGKB; PA38610; -. DR VEuPathDB; HostDB:ENSG00000010327; -. DR eggNOG; KOG1218; Eukaryota. DR GeneTree; ENSGT00940000157928; -. DR HOGENOM; CLU_001035_0_0_1; -. DR InParanoid; Q9NY15; -. DR OMA; VHAECIP; -. DR OrthoDB; 2970631at2759; -. DR PhylomeDB; Q9NY15; -. DR TreeFam; TF331489; -. DR PathwayCommons; Q9NY15; -. DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors. DR SignaLink; Q9NY15; -. DR BioGRID-ORCS; 23166; 25 hits in 1151 CRISPR screens. DR ChiTaRS; STAB1; human. DR GeneWiki; STAB1; -. DR GenomeRNAi; 23166; -. DR Pharos; Q9NY15; Tbio. DR PRO; PR:Q9NY15; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9NY15; Protein. DR Bgee; ENSG00000010327; Expressed in spleen and 153 other cell types or tissues. DR ExpressionAtlas; Q9NY15; baseline and differential. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro. DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB. DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:UniProtKB. DR GO; GO:0015035; F:protein-disulfide reductase activity; NAS:UniProtKB. DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB. DR CDD; cd00055; EGF_Lam; 1. DR Gene3D; 2.30.180.10; FAS1 domain; 7. DR Gene3D; 2.10.25.10; Laminin; 13. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024731; EGF_dom. DR InterPro; IPR036378; FAS1_dom_sf. DR InterPro; IPR000782; FAS1_domain. DR InterPro; IPR002049; LE_dom. DR InterPro; IPR000538; Link_dom. DR PANTHER; PTHR24038; STABILIN; 1. DR PANTHER; PTHR24038:SF8; STABILIN-1; 1. DR Pfam; PF12947; EGF_3; 7. DR Pfam; PF02469; Fasciclin; 6. DR Pfam; PF00193; Xlink; 1. DR SMART; SM00181; EGF; 23. DR SMART; SM00179; EGF_CA; 6. DR SMART; SM00180; EGF_Lam; 4. DR SMART; SM00554; FAS1; 7. DR SMART; SM00445; LINK; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF82153; FAS1 domain; 7. DR PROSITE; PS00022; EGF_1; 7. DR PROSITE; PS01186; EGF_2; 16. DR PROSITE; PS50026; EGF_3; 20. DR PROSITE; PS01248; EGF_LAM_1; 2. DR PROSITE; PS50213; FAS1; 7. DR PROSITE; PS01241; LINK_1; 1. DR PROSITE; PS50963; LINK_2; 1. DR Genevisible; Q9NY15; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein; KW Inflammatory response; Laminin EGF-like domain; Membrane; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..2570 FT /note="Stabilin-1" FT /id="PRO_0000007710" FT TOPO_DOM 26..2478 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2479..2499 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2500..2570 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 110..148 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 156..193 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 195..229 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 232..271 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 356..494 FT /note="FAS1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 506..641 FT /note="FAS1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 728..768 FT /note="EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 818..858 FT /note="EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 861..903 FT /note="EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 904..946 FT /note="EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 947..986 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 988..1118 FT /note="FAS1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 1128..1253 FT /note="FAS1 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 1327..1392 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000305" FT DOMAIN 1416..1454 FT /note="EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 1455..1496 FT /note="EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 1497..1539 FT /note="EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 1540..1582 FT /note="EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 1582..1708 FT /note="FAS1 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 1724..1864 FT /note="FAS1 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT DOMAIN 1966..2031 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000305" FT DOMAIN 2056..2090 FT /note="EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 2091..2131 FT /note="EGF-like 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 2132..2174 FT /note="EGF-like 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076, FT ECO:0000305" FT DOMAIN 2206..2301 FT /note="Link" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000305" FT DOMAIN 2322..2459 FT /note="FAS1 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082, FT ECO:0000305" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 286 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 312 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 606 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 673 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 712 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 745 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 816 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1087 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1096 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1170 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1178 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1378 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1471 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1626 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1727 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2222 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2261 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2290 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2334 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2347 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 2379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2400 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2424 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 112..126 FT /evidence="ECO:0000250" FT DISULFID 120..136 FT /evidence="ECO:0000250" FT DISULFID 138..147 FT /evidence="ECO:0000250" FT DISULFID 160..171 FT /evidence="ECO:0000250" FT DISULFID 164..181 FT /evidence="ECO:0000250" FT DISULFID 183..192 FT /evidence="ECO:0000250" FT DISULFID 199..210 FT /evidence="ECO:0000250" FT DISULFID 204..217 FT /evidence="ECO:0000250" FT DISULFID 236..247 FT /evidence="ECO:0000250" FT DISULFID 241..257 FT /evidence="ECO:0000250" FT DISULFID 259..270 FT /evidence="ECO:0000250" FT DISULFID 732..746 FT /evidence="ECO:0000250" FT DISULFID 740..756 FT /evidence="ECO:0000250" FT DISULFID 758..767 FT /evidence="ECO:0000250" FT DISULFID 822..837 FT /evidence="ECO:0000250" FT DISULFID 831..846 FT /evidence="ECO:0000250" FT DISULFID 865..879 FT /evidence="ECO:0000250" FT DISULFID 873..889 FT /evidence="ECO:0000250" FT DISULFID 891..902 FT /evidence="ECO:0000250" FT DISULFID 908..922 FT /evidence="ECO:0000250" FT DISULFID 916..932 FT /evidence="ECO:0000250" FT DISULFID 934..945 FT /evidence="ECO:0000250" FT DISULFID 951..964 FT /evidence="ECO:0000250" FT DISULFID 958..974 FT /evidence="ECO:0000250" FT DISULFID 1332..1346 FT /evidence="ECO:0000250" FT DISULFID 1340..1356 FT /evidence="ECO:0000250" FT DISULFID 1358..1367 FT /evidence="ECO:0000250" FT DISULFID 1379..1390 FT /evidence="ECO:0000250" FT DISULFID 1383..1400 FT /evidence="ECO:0000250" FT DISULFID 1402..1411 FT /evidence="ECO:0000250" FT DISULFID 1420..1430 FT /evidence="ECO:0000250" FT DISULFID 1424..1440 FT /evidence="ECO:0000250" FT DISULFID 1442..1453 FT /evidence="ECO:0000250" FT DISULFID 1459..1472 FT /evidence="ECO:0000250" FT DISULFID 1466..1482 FT /evidence="ECO:0000250" FT DISULFID 1484..1495 FT /evidence="ECO:0000250" FT DISULFID 1501..1514 FT /evidence="ECO:0000250" FT DISULFID 1508..1524 FT /evidence="ECO:0000250" FT DISULFID 1526..1538 FT /evidence="ECO:0000250" FT DISULFID 1544..1557 FT /evidence="ECO:0000250" FT DISULFID 1551..1567 FT /evidence="ECO:0000250" FT DISULFID 1569..1581 FT /evidence="ECO:0000250" FT DISULFID 1971..1985 FT /evidence="ECO:0000250" FT DISULFID 1979..1995 FT /evidence="ECO:0000250" FT DISULFID 1997..2006 FT /evidence="ECO:0000250" FT DISULFID 2018..2029 FT /evidence="ECO:0000250" FT DISULFID 2023..2039 FT /evidence="ECO:0000250" FT DISULFID 2041..2050 FT /evidence="ECO:0000250" FT DISULFID 2060..2070 FT /evidence="ECO:0000250" FT DISULFID 2064..2076 FT /evidence="ECO:0000250" FT DISULFID 2078..2089 FT /evidence="ECO:0000250" FT DISULFID 2095..2108 FT /evidence="ECO:0000250" FT DISULFID 2102..2117 FT /evidence="ECO:0000250" FT DISULFID 2119..2130 FT /evidence="ECO:0000250" FT DISULFID 2136..2150 FT /evidence="ECO:0000250" FT DISULFID 2144..2160 FT /evidence="ECO:0000250" FT DISULFID 2162..2173 FT /evidence="ECO:0000250" FT DISULFID 2230..2299 FT /evidence="ECO:0000250" FT DISULFID 2254..2275 FT /evidence="ECO:0000250" FT VAR_SEQ 746..803 FT /note="CSDGIQGNGACLCFPDYKGIACHICSNPNKHGEQCQEDCGCVHGLCDNRPGS FT GGVCQQ -> VSPILSWGEVWGTQGLLHRLASDWLCVWAKPATLALGFSYLCSGKLDQI FT ISHILIKNN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12077138" FT /id="VSP_050764" FT VAR_SEQ 804..2570 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12077138" FT /id="VSP_050765" FT VARIANT 672 FT /note="L -> M (in dbSNP:rs12636502)" FT /id="VAR_060338" FT VARIANT 912 FT /note="M -> V (in dbSNP:rs9835659)" FT /evidence="ECO:0000269|PubMed:11829752, FT ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9039502" FT /id="VAR_060339" FT VARIANT 1127 FT /note="G -> R (in dbSNP:rs2286786)" FT /id="VAR_055774" FT VARIANT 1833 FT /note="A -> P (in dbSNP:rs7630214)" FT /evidence="ECO:0000269|PubMed:11829752, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9039502" FT /id="VAR_060340" FT VARIANT 2282 FT /note="I -> V (in dbSNP:rs4434138)" FT /evidence="ECO:0000269|PubMed:11829752" FT /id="VAR_055775" FT VARIANT 2506 FT /note="M -> T (in dbSNP:rs13303)" FT /id="VAR_019078" FT CONFLICT 913 FT /note="R -> G (in Ref. 1; CAB61827)" FT /evidence="ECO:0000305" FT CONFLICT 2200 FT /note="L -> Q (in Ref. 1; CAB61827)" FT /evidence="ECO:0000305" SQ SEQUENCE 2570 AA; 275482 MW; FA55D191D9D30FAD CRC64; MAGPRGLLPL CLLAFCLAGF SFVRGQVLFK GCDVKTTFVT HVPCTSCAAI KKQTCPSGWL RELPDQITQD CRYEVQLGGS MVSMSGCRRK CRKQVVQKAC CPGYWGSRCH ECPGGAETPC NGHGTCLDGM DRNGTCVCQE NFRGSACQEC QDPNRFGPDC QSVCSCVHGV CNHGPRGDGS CLCFAGYTGP HCDQELPVCQ ELRCPQNTQC SAEAPSCRCL PGYTQQGSEC RAPNPCWPSP CSLLAQCSVS PKGQAQCHCP ENYHGDGMVC LPKDPCTDNL GGCPSNSTLC VYQKPGQAFC TCRPGLVSIN SNASAGCFAF CSPFSCDRSA TCQVTADGKT SCVCRESEVG DGRACYGHLL HEVQKATQTG RVFLQLRVAV AMMDQGCREI LTTAGPFTVL VPSVSSFSSR TMNASLAQQL CRQHIIAGQH ILEDTRTQQT RRWWTLAGQE ITVTFNQFTK YSYKYKDQPQ QTFNIYKANN IAANGVFHVV TGLRWQAPSG TPGDPKRTIG QILASTEAFS RFETILENCG LPSILDGPGP FTVFAPSNEA VDSLRDGRLI YLFTAGLSKL QELVRYHIYN HGQLTVEKLI SKGRILTMAN QVLAVNISEE GRILLGPEGV PLQRVDVMAA NGVIHMLDGI LLPPTILPIL PKHCSEEQHK IVAGSCVDCQ ALNTSTCPPN SVKLDIFPKE CVYIHDPTGL NVLKKGCASY CNQTIMEQGC CKGFFGPDCT QCPGGFSNPC YGKGNCSDGI QGNGACLCFP DYKGIACHIC SNPNKHGEQC QEDCGCVHGL CDNRPGSGGV CQQGTCAPGF SGRFCNESMG DCGPTGLAQH CHLHARCVSQ EGVARCRCLD GFEGDGFSCT PSNPCSHPDR GGCSENAECV PGSLGTHHCT CHKGWSGDGR VCVAIDECEL DMRGGCHTDA LCSYVGPGQS RCTCKLGFAG DGYQCSPIDP CRAGNGGCHG LATCRAVGGG QRVCTCPPGF GGDGFSCYGD IFRELEANAH FSIFYQWLKS AGITLPADRR VTALVPSEAA VRQLSPEDRA FWLQPRTLPN LVRAHFLQGA LFEEELARLG GQEVATLNPT TRWEIRNISG RVWVQNASVD VADLLATNGV LHILSQVLLP PRGDVPGGQG LLQQLDLVPA FSLFRELLQH HGLVPQIEAA TAYTIFVPTN RSLEAQGNSS HLDADTVRHH VVLGEALSME TLRKGGHRNS LLGPAHWIVF YNHSGQPEVN HVPLEGPMLE APGRSLIGLS GVLTVGSSRC LHSHAEALRE KCVNCTRRFR CTQGFQLQDT PRKSCVYRSG FSFSRGCSYT CAKKIQVPDC CPGFFGTLCE PCPGGLGGVC SGHGQCQDRF LGSGECHCHE GFHGTACEVC ELGRYGPNCT GVCDCAHGLC QEGLQGDGSC VCNVGWQGLR CDQKITSPQC PRKCDPNANC VQDSAGASTC ACAAGYSGNG IFCSEVDPCA HGHGGCSPHA NCTKVAPGQR TCTCQDGYMG DGELCQEINS CLIHHGGCHI HAECIPTGPQ QVSCSCREGY SGDGIRTCEL LDPCSKNNGG CSPYATCKST GDGQRTCTCD TAHTVGDGLT CRARVGLELL RDKHASFFSL RLLEYKELKG DGPFTIFVPH ADLMSNLSQD ELARIRAHRQ LVFRYHVVGC RRLRSEDLLE QGYATALSGH PLRFSEREGS IYLNDFARVV SSDHEAVNGI LHFIDRVLLP PEALHWEPDD APIPRRNVTA AAQGFGYKIF SGLLKVAGLL PLLREASHRP FTMLWPTDAA FRALPPDRQA WLYHEDHRDK LAAILRGHMI RNVEALASDL PNLGPLRTMH GTPISFSCSR TRAGELMVGE DDARIVQRHL PFEGGLAYGI DQLLEPPGLG ARCDHFETRP LRLNTCSICG LEPPCPEGSQ EQGSPEACWR FYPKFWTSPP LHSLGLRSVW VHPSLWGRPQ GLGRGCHRNC VTTTWKPSCC PGHYGSECQA CPGGPSSPCS DRGVCMDGMS GSGQCLCRSG FAGTACELCA PGAFGPHCQA CRCTVHGRCD EGLGGSGSCF CDEGWTGPRC EVQLELQPVC TPPCAPEAVC RAGNSCECSL GYEGDGRVCT VADLCQDGHG GCSEHANCSQ VGTMVTCTCL PDYEGDGWSC RARNPCTDGH RGGCSEHANC LSTGLNTRRC ECHAGYVGDG LQCLEESEPP VDRCLGQPPP CHSDAMCTDL HFQEKRAGVF HLQATSGPYG LNFSEAEAAC EAQGAVLASF PQLSAAQQLG FHLCLMGWLA NGSTAHPVVF PVADCGNGRV GIVSLGARKN LSERWDAYCF RVQDVACRCR NGFVGDGIST CNGKLLDVLA ATANFSTFYG MLLGYANATQ RGLDFLDFLD DELTYKTLFV PVNEGFVDNM TLSGPDLELH ASNATLLSAN ASQGKLLPAH SGLSLIISDA GPDNSSWAPV APGTVVVSRI IVWDIMAFNG IIHALASPLL APPQPQAVLA PEAPPVAAGV GAVLAAGALL GLVAGALYLR ARGKPMGFGF SAFQAEDDAD DDFSPWQEGT NPTLVSVPNP VFGSDTFCEP FDDSLLEEDF PDTQRILTVK //