STAB1_HUMAN
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 03-AUG-2022, entry version 186.
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 -!- 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};
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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; 9.
DR ELM; Q9NY15; -.
DR IntAct; Q9NY15; 74.
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 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; Q9NY15; -.
DR PeptideAtlas; Q9NY15; -.
DR PRIDE; Q9NY15; -.
DR ProteomicsDB; 83149; -. [Q9NY15-1]
DR ProteomicsDB; 83150; -. [Q9NY15-2]
DR Antibodypedia; 1505; 153 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 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; PNANCIQ; -.
DR OrthoDB; 6428at2759; -.
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; 18 hits in 1072 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 151 other tissues.
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 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; -; 7.
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; 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 Pfam; PF12947; EGF_3; 6.
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; 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
