GenomeNet

Database: UniProt
Entry: Q9NY15
LinkDB: Q9NY15
Original site: Q9NY15 
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   13-FEB-2019, entry version 166.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000312|EMBL:CAB61827.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   VARIANTS 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
RT   hyaluronan 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
RP   VAL-912 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.
RT   The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT   analysis of 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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
RP   VAL-912 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
RT   project: 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.,
RA   Schmuttermaier C., Krusell L., Haus G., Utikal J., Schledzewski K.,
RA   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
RT   lysosomal 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
RT   multiple 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.,
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).
CC   -!- FUNCTION: Acts as a scavenger receptor for acetylated low density
CC       lipoprotein. Binds to both Gram-positive and Gram-negative
CC       bacteria and may play a role in defense against bacterial
CC       infection. When inhibited in endothelial tube formation assays,
CC       there is a marked decrease in cell-cell interactions, suggesting a
CC       role in angiogenesis. Involved in the delivery of newly
CC       synthesized CHID1/SI-CLP from the biosynthetic compartment to the
CC       endosomal/lysosomal system. {ECO:0000269|PubMed:12077138,
CC       ECO:0000269|PubMed:16357325}.
CC   -!- SUBUNIT: Interacts with CHID1. {ECO:0000269|PubMed:16357325}.
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
CC       and 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
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   UniGene; Hs.301989; -.
DR   ProteinModelPortal; Q9NY15; -.
DR   SMR; Q9NY15; -.
DR   BioGrid; 116778; 6.
DR   ELM; Q9NY15; -.
DR   IntAct; Q9NY15; 72.
DR   MINT; Q9NY15; -.
DR   STRING; 9606.ENSP00000312946; -.
DR   GlyConnect; 681; -.
DR   iPTMnet; Q9NY15; -.
DR   PhosphoSitePlus; Q9NY15; -.
DR   UniCarbKB; Q9NY15; -.
DR   BioMuta; STAB1; -.
DR   DMDM; 296452949; -.
DR   EPD; Q9NY15; -.
DR   jPOST; Q9NY15; -.
DR   PaxDb; Q9NY15; -.
DR   PeptideAtlas; Q9NY15; -.
DR   PRIDE; Q9NY15; -.
DR   ProteomicsDB; 83149; -.
DR   ProteomicsDB; 83150; -. [Q9NY15-2]
DR   Ensembl; ENST00000321725; ENSP00000312946; ENSG00000010327. [Q9NY15-1]
DR   GeneID; 23166; -.
DR   KEGG; hsa:23166; -.
DR   UCSC; uc003dej.4; human. [Q9NY15-1]
DR   CTD; 23166; -.
DR   DisGeNET; 23166; -.
DR   EuPathDB; HostDB:ENSG00000010327.10; -.
DR   GeneCards; STAB1; -.
DR   H-InvDB; HIX0003360; -.
DR   HGNC; HGNC:18628; STAB1.
DR   HPA; HPA005434; -.
DR   MIM; 608560; gene.
DR   neXtProt; NX_Q9NY15; -.
DR   OpenTargets; ENSG00000010327; -.
DR   PharmGKB; PA38610; -.
DR   eggNOG; ENOG410IRWH; Eukaryota.
DR   eggNOG; COG2335; LUCA.
DR   GeneTree; ENSGT00940000157928; -.
DR   HOGENOM; HOG000154436; -.
DR   HOVERGEN; HBG079218; -.
DR   InParanoid; Q9NY15; -.
DR   KO; K19020; -.
DR   OMA; HVVGCRQ; -.
DR   OrthoDB; 6428at2759; -.
DR   PhylomeDB; Q9NY15; -.
DR   TreeFam; TF331489; -.
DR   Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
DR   ChiTaRS; STAB1; human.
DR   GeneWiki; STAB1; -.
DR   GenomeRNAi; 23166; -.
DR   PRO; PR:Q9NY15; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000010327; Expressed in 194 organ(s), highest expression level in spleen.
DR   ExpressionAtlas; Q9NY15; baseline and differential.
DR   Genevisible; Q9NY15; HS.
DR   GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 oxidoreductase 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   Gene3D; 2.30.180.10; -; 6.
DR   Gene3D; 3.10.100.10; -; 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; IPR013032; EGF-like_CS.
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; Laminin_EGF.
DR   InterPro; IPR000538; Link_dom.
DR   Pfam; PF12947; EGF_3; 4.
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; SSF56436; 1.
DR   SUPFAM; SSF82153; SSF82153; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Inflammatory response;
KW   Laminin EGF-like domain; Membrane; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   2570       Stabilin-1.
FT                                /FTId=PRO_0000007710.
FT   TOPO_DOM     26   2478       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2479   2499       Helical. {ECO:0000255}.
FT   TOPO_DOM   2500   2570       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      110    148       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      156    193       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      195    229       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      232    271       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      356    494       FAS1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN      506    641       FAS1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN      728    768       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      818    858       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      861    903       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      904    946       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      947    986       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN      988   1118       FAS1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN     1128   1253       FAS1 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN     1327   1392       Laminin EGF-like 1. {ECO:0000305}.
FT   DOMAIN     1416   1454       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     1455   1496       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     1497   1539       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     1540   1582       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     1582   1708       FAS1 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN     1724   1864       FAS1 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   DOMAIN     1966   2031       Laminin EGF-like 2. {ECO:0000305}.
FT   DOMAIN     2056   2090       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     2091   2131       EGF-like 15. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     2132   2174       EGF-like 16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000305}.
FT   DOMAIN     2206   2301       Link. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323, ECO:0000305}.
FT   DOMAIN     2322   2459       FAS1 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00082, ECO:0000305}.
FT   CARBOHYD    133    133       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    286    286       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    312    312       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    413    413       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    606    606       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    673    673       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    712    712       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    745    745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    816    816       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1087   1087       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1096   1096       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1170   1170       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1178   1178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1222   1222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1274   1274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1378   1378       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1471   1471       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1626   1626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1727   1727       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2107   2107       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2222   2222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2261   2261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2290   2290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2334   2334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2347   2347       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2379   2379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2393   2393       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2400   2400       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2424   2424       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   DISULFID    112    126       {ECO:0000250}.
FT   DISULFID    120    136       {ECO:0000250}.
FT   DISULFID    138    147       {ECO:0000250}.
FT   DISULFID    160    171       {ECO:0000250}.
FT   DISULFID    164    181       {ECO:0000250}.
FT   DISULFID    183    192       {ECO:0000250}.
FT   DISULFID    199    210       {ECO:0000250}.
FT   DISULFID    204    217       {ECO:0000250}.
FT   DISULFID    236    247       {ECO:0000250}.
FT   DISULFID    241    257       {ECO:0000250}.
FT   DISULFID    259    270       {ECO:0000250}.
FT   DISULFID    732    746       {ECO:0000250}.
FT   DISULFID    740    756       {ECO:0000250}.
FT   DISULFID    758    767       {ECO:0000250}.
FT   DISULFID    822    837       {ECO:0000250}.
FT   DISULFID    831    846       {ECO:0000250}.
FT   DISULFID    865    879       {ECO:0000250}.
FT   DISULFID    873    889       {ECO:0000250}.
FT   DISULFID    891    902       {ECO:0000250}.
FT   DISULFID    908    922       {ECO:0000250}.
FT   DISULFID    916    932       {ECO:0000250}.
FT   DISULFID    934    945       {ECO:0000250}.
FT   DISULFID    951    964       {ECO:0000250}.
FT   DISULFID    958    974       {ECO:0000250}.
FT   DISULFID   1332   1346       {ECO:0000250}.
FT   DISULFID   1340   1356       {ECO:0000250}.
FT   DISULFID   1358   1367       {ECO:0000250}.
FT   DISULFID   1379   1390       {ECO:0000250}.
FT   DISULFID   1383   1400       {ECO:0000250}.
FT   DISULFID   1402   1411       {ECO:0000250}.
FT   DISULFID   1420   1430       {ECO:0000250}.
FT   DISULFID   1424   1440       {ECO:0000250}.
FT   DISULFID   1442   1453       {ECO:0000250}.
FT   DISULFID   1459   1472       {ECO:0000250}.
FT   DISULFID   1466   1482       {ECO:0000250}.
FT   DISULFID   1484   1495       {ECO:0000250}.
FT   DISULFID   1501   1514       {ECO:0000250}.
FT   DISULFID   1508   1524       {ECO:0000250}.
FT   DISULFID   1526   1538       {ECO:0000250}.
FT   DISULFID   1544   1557       {ECO:0000250}.
FT   DISULFID   1551   1567       {ECO:0000250}.
FT   DISULFID   1569   1581       {ECO:0000250}.
FT   DISULFID   1971   1985       {ECO:0000250}.
FT   DISULFID   1979   1995       {ECO:0000250}.
FT   DISULFID   1997   2006       {ECO:0000250}.
FT   DISULFID   2018   2029       {ECO:0000250}.
FT   DISULFID   2023   2039       {ECO:0000250}.
FT   DISULFID   2041   2050       {ECO:0000250}.
FT   DISULFID   2060   2070       {ECO:0000250}.
FT   DISULFID   2064   2076       {ECO:0000250}.
FT   DISULFID   2078   2089       {ECO:0000250}.
FT   DISULFID   2095   2108       {ECO:0000250}.
FT   DISULFID   2102   2117       {ECO:0000250}.
FT   DISULFID   2119   2130       {ECO:0000250}.
FT   DISULFID   2136   2150       {ECO:0000250}.
FT   DISULFID   2144   2160       {ECO:0000250}.
FT   DISULFID   2162   2173       {ECO:0000250}.
FT   DISULFID   2230   2299       {ECO:0000250}.
FT   DISULFID   2254   2275       {ECO:0000250}.
FT   VAR_SEQ     746    803       CSDGIQGNGACLCFPDYKGIACHICSNPNKHGEQCQEDCGC
FT                                VHGLCDNRPGSGGVCQQ -> VSPILSWGEVWGTQGLLHRL
FT                                ASDWLCVWAKPATLALGFSYLCSGKLDQIISHILIKNN
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:12077138}.
FT                                /FTId=VSP_050764.
FT   VAR_SEQ     804   2570       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12077138}.
FT                                /FTId=VSP_050765.
FT   VARIANT     672    672       L -> M (in dbSNP:rs12636502).
FT                                /FTId=VAR_060338.
FT   VARIANT     912    912       M -> V (in dbSNP:rs9835659).
FT                                {ECO:0000269|PubMed:11829752,
FT                                ECO:0000269|PubMed:12077138,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9039502}.
FT                                /FTId=VAR_060339.
FT   VARIANT    1127   1127       G -> R (in dbSNP:rs2286786).
FT                                /FTId=VAR_055774.
FT   VARIANT    1833   1833       A -> P (in dbSNP:rs7630214).
FT                                {ECO:0000269|PubMed:11829752,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9039502}.
FT                                /FTId=VAR_060340.
FT   VARIANT    2282   2282       I -> V (in dbSNP:rs4434138).
FT                                {ECO:0000269|PubMed:11829752}.
FT                                /FTId=VAR_055775.
FT   VARIANT    2506   2506       M -> T (in dbSNP:rs13303).
FT                                /FTId=VAR_019078.
FT   CONFLICT    913    913       R -> G (in Ref. 1; CAB61827).
FT                                {ECO:0000305}.
FT   CONFLICT   2200   2200       L -> Q (in Ref. 1; CAB61827).
FT                                {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
//
DBGET integrated database retrieval system