ID   ITA3_MOUSE              Reviewed;        1053 AA.
AC   Q62470; Q08441; Q08442; Q5SWA8; Q5SWB9; Q6P6I1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Integrin alpha-3;
DE   AltName: Full=CD49 antigen-like family member C;
DE   AltName: Full=Galactoprotein B3;
DE            Short=GAPB3;
DE   AltName: Full=VLA-3 subunit alpha;
DE   AltName: CD_antigen=CD49c;
DE   Contains:
DE     RecName: Full=Integrin alpha-3 heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-3 light chain;
DE   Flags: Precursor;
GN   Name=Itga3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ;
RX   PubMed=7759572; DOI=10.1002/jcb.240570221;
RA   Takeuchi K., Hirano K., Tuji T., Osawa T., Irimura T.;
RT   "cDNA cloning of mouse VLA-3 alpha subunit.";
RL   J. Cell. Biochem. 57:371-377(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, and Mammary tumor;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 913-1053 (ISOFORM 1), PARTIAL NUCLEOTIDE
RP   SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   PubMed=1946438; DOI=10.1073/pnas.88.22.10183;
RA   Tamura R.N., Cooper H.M., Collo G., Quaranta V.;
RT   "Cell type-specific integrin variants with alternative alpha chain
RT   cytoplasmic domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:10183-10187(1991).
RN   [5]
RP   INTERACTION WITH ITGB1; LGALS3 AND CSPG4.
RX   PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA   Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT   "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT   engagement of galectin-3 and alpha3beta1 integrin.";
RL   Mol. Biol. Cell 15:3580-3590(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-574; ASN-606; ASN-657;
RP   ASN-928 AND ASN-937.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-512; ASN-574; ASN-657;
RP   ASN-937 AND ASN-971.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Integrin alpha-3/beta-1 is a receptor for fibronectin,
CC       laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC       3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC       plasma membranes in a collagen-dependent manner and hence may
CC       participate in the adhesion, formation of invadopodia and matrix
CC       degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC       mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC       migration. {ECO:0000250|UniProtKB:P26006}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC       is composed of a heavy and a light chain linked by a disulfide bond.
CC       Alpha-3 associates with beta-1. Interacts with HPS5. Interacts with FAP
CC       (seprase); the interaction occurs at the cell surface of invadopodia
CC       membrane in a collagen-dependent manner.
CC       {ECO:0000250|UniProtKB:P26006}.
CC   -!- INTERACTION:
CC       Q62470; O35566: Cd151; NbExp=2; IntAct=EBI-8398907, EBI-8369654;
CC       Q62470; P28828: Ptprm; NbExp=3; IntAct=EBI-8398907, EBI-8539266;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell
CC       projection, invadopodium membrane {ECO:0000250|UniProtKB:P26006};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC       filopodium membrane {ECO:0000250|UniProtKB:P26006}; Single-pass type I
CC       membrane protein {ECO:0000255}. Note=Enriched preferentially at
CC       invadopodia, cell membrane protrusions that correspond to sites of cell
CC       invasion, in a collagen-dependent manner.
CC       {ECO:0000250|UniProtKB:P26006}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha-3A;
CC         IsoId=Q62470-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-3B;
CC         IsoId=Q62470-2; Sequence=VSP_002722;
CC       Name=3;
CC         IsoId=Q62470-3; Sequence=VSP_041797;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in heart and
CC       brain. Only isoform 1 is detected in lung.
CC       {ECO:0000269|PubMed:1946438}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR   EMBL; D13867; BAA02980.1; -; mRNA.
DR   EMBL; AL606480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC053031; AAH53031.1; -; mRNA.
DR   EMBL; BC062205; AAH62205.1; -; mRNA.
DR   EMBL; S66292; AAB20356.2; -; mRNA.
DR   EMBL; S66294; AAB20357.2; -; mRNA.
DR   CCDS; CCDS25271.1; -. [Q62470-1]
DR   CCDS; CCDS83877.1; -. [Q62470-3]
DR   CCDS; CCDS83878.1; -. [Q62470-2]
DR   PIR; B41543; B41543.
DR   PIR; I55534; I55534.
DR   RefSeq; NP_001293000.1; NM_001306071.1. [Q62470-3]
DR   RefSeq; NP_001293091.1; NM_001306162.1. [Q62470-2]
DR   RefSeq; NP_038593.1; NM_013565.3. [Q62470-1]
DR   RefSeq; XP_006532373.1; XM_006532310.3. [Q62470-2]
DR   RefSeq; XP_006532374.1; XM_006532311.3. [Q62470-1]
DR   AlphaFoldDB; Q62470; -.
DR   SMR; Q62470; -.
DR   BioGRID; 200816; 6.
DR   ComplexPortal; CPX-3117; Integrin alpha3-beta1 complex.
DR   CORUM; Q62470; -.
DR   IntAct; Q62470; 6.
DR   STRING; 10090.ENSMUSP00000113556; -.
DR   GlyConnect; 2423; 6 N-Linked glycans (5 sites). [Q62470-2]
DR   GlyCosmos; Q62470; 13 sites, 6 glycans.
DR   GlyGen; Q62470; 13 sites, 6 N-linked glycans (5 sites).
DR   iPTMnet; Q62470; -.
DR   PhosphoSitePlus; Q62470; -.
DR   SwissPalm; Q62470; -.
DR   EPD; Q62470; -.
DR   jPOST; Q62470; -.
DR   MaxQB; Q62470; -.
DR   PaxDb; 10090-ENSMUSP00000001548; -.
DR   PeptideAtlas; Q62470; -.
DR   ProteomicsDB; 301682; -. [Q62470-1]
DR   ProteomicsDB; 301683; -. [Q62470-2]
DR   ProteomicsDB; 301684; -. [Q62470-3]
DR   Pumba; Q62470; -.
DR   Antibodypedia; 18000; 1122 antibodies from 42 providers.
DR   DNASU; 16400; -.
DR   Ensembl; ENSMUST00000001548.14; ENSMUSP00000001548.8; ENSMUSG00000001507.17. [Q62470-1]
DR   Ensembl; ENSMUST00000107739.8; ENSMUSP00000103368.2; ENSMUSG00000001507.17. [Q62470-3]
DR   Ensembl; ENSMUST00000120375.8; ENSMUSP00000113556.2; ENSMUSG00000001507.17. [Q62470-2]
DR   GeneID; 16400; -.
DR   KEGG; mmu:16400; -.
DR   UCSC; uc007kzv.1; mouse. [Q62470-3]
DR   UCSC; uc007kzw.1; mouse. [Q62470-1]
DR   UCSC; uc007kzx.1; mouse. [Q62470-2]
DR   AGR; MGI:96602; -.
DR   CTD; 3675; -.
DR   MGI; MGI:96602; Itga3.
DR   VEuPathDB; HostDB:ENSMUSG00000001507; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000157746; -.
DR   HOGENOM; CLU_004111_1_0_1; -.
DR   InParanoid; Q62470; -.
DR   OMA; RYNHTGA; -.
DR   OrthoDB; 3816176at2759; -.
DR   TreeFam; TF105391; -.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR   BioGRID-ORCS; 16400; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Itga3; mouse.
DR   PRO; PR:Q62470; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q62470; Protein.
DR   Bgee; ENSMUSG00000001507; Expressed in undifferentiated genital tubercle and 299 other cell types or tissues.
DR   ExpressionAtlas; Q62470; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0071944; C:cell periphery; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:1990812; C:growth cone filopodium; ISO:MGI.
DR   GO; GO:0034667; C:integrin alpha3-beta1 complex; ISO:MGI.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR   GO; GO:0005518; F:collagen binding; ISO:MGI.
DR   GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0043236; F:laminin binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0097062; P:dendritic spine maintenance; IMP:MGI.
DR   GO; GO:0035640; P:exploration behavior; IGI:MGI.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0050900; P:leukocyte migration; IBA:GO_Central.
DR   GO; GO:0030324; P:lung development; ISO:MGI.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0031345; P:negative regulation of cell projection organization; ISO:MGI.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IGI:MGI.
DR   GO; GO:0072006; P:nephron development; ISO:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; ISO:MGI.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0097205; P:renal filtration; ISO:MGI.
DR   GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007266; P:Rho protein signal transduction; IGI:MGI.
DR   GO; GO:0043588; P:skin development; ISO:MGI.
DR   GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF89; INTEGRIN ALPHA-3; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF20806; Integrin_A_Ig_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   Genevisible; Q62470; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Integrin; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..1053
FT                   /note="Integrin alpha-3"
FT                   /id="PRO_0000016241"
FT   CHAIN           33..874
FT                   /note="Integrin alpha-3 heavy chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016242"
FT   CHAIN           878..1053
FT                   /note="Integrin alpha-3 light chain"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016243"
FT   TOPO_DOM        33..993
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        994..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1022..1053
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          38..103
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          110..171
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          185..235
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          236..293
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          294..355
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          357..412
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          416..478
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REGION          865..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1018
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        574
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        606
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        843
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        859
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        925
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        928
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        937
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        971
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   DISULFID        94..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        140..162
FT                   /evidence="ECO:0000250"
FT   DISULFID        185..197
FT                   /evidence="ECO:0000250"
FT   DISULFID        486..491
FT                   /evidence="ECO:0000250"
FT   DISULFID        497..551
FT                   /evidence="ECO:0000250"
FT   DISULFID        616..622
FT                   /evidence="ECO:0000250"
FT   DISULFID        695..704
FT                   /evidence="ECO:0000250"
FT   DISULFID        848..906
FT                   /note="Interchain (between heavy and light chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        913..918
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..69
FT                   /note="MGPGPCRVPRAPGWLLRALALMVAACGRVAFAFNLDTRFLVVKEAVNPGSLF
FT                   GYSVALHRQTERQQRYL -> MSYLQTLVWSPCSESVDLQADWREACKARLTHPPSFSS
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041797"
FT   VAR_SEQ         1019..1053
FT                   /note="GFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY -> DFFKPTRYYRIMP
FT                   KYHAVRIREEDRYPPPGSTLPTKKHWVTSWQIRDRYY (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002722"
FT   CONFLICT        975
FT                   /note="W -> C (in Ref. 4; AAB20356/AAB20357)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        979
FT                   /note="D -> N (in Ref. 4; AAB20356/AAB20357)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1002
FT                   /note="G -> S (in Ref. 4; AAB20356/AAB20357)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1053 AA;  116745 MW;  6A5E8FBDBA86D6E5 CRC64;
     MGPGPCRVPR APGWLLRALA LMVAACGRVA FAFNLDTRFL VVKEAVNPGS LFGYSVALHR
     QTERQQRYLL LAGAPRDLAV GDDYTNRTGA VYLCPLTAHK DDCERMDISE KSDPDHHIIE
     DMWLGVTVAS QGPAGRVLVC AHRYTKVLWS GLEDQRRMVG KCYVRGNDLQ LDPGDDWQTY
     HNEMCNSNTD YLQTGMCQLG TSGGFTQNTV YFGAPGAYNW KGNSYMIQRK DWDLSEYSYR
     GSEEQGNLYI GYTVQVGNAI LHPTDIITVV TGAPRHQHMG AVFLLKQESG GDLQRKQVLK
     GTQVGAYFGS AIALADLNND GWQDLLVGAP YYFERKEEVG GAVYVFMNQA GASFPDQPSL
     LLHGPSRSAF GISIASIGDI NQDGFQDIAV GAPFEGLGKV YIYHSSSGGL LRQPQQIIHG
     EKLGLPGLAT FGYSLSGKMD VDENLYPDLL VGSLSDHIVL LRARPVINIL HRTLVARPAV
     LDPALCTATS CVQVELCFAY NQSAGNPNYR RNITLAYTLE ADRDRRPPRL RFARSQSSVF
     HGFFSMPETH CQTLELLLMD NVRDKLRPIV IAMNYSLPLR MPDRLKLGLR SLDAYPVLNQ
     AQAMENHTEV HFQKECGPDN KCDSNLQMRA AFLSEQLQPL SRLQYSRDTK KLFLSINVTN
     SPSSQRAGED AHEALLTLEV PSALLLSSVR PSGTCQANNE TILCELGNPF KRNQRMELLI
     AFEVIGVTLH TRDLPVLLQL STSSHQDNLQ PVLLTLQVDY TLQASLSLMN HRLQSFFGGT
     VMGEAAMKTA EDVGSPLKYE FQVSPVGDGL AALGTLVLGL EWPYEVTNGK WLLYPTEITI
     HSNGSWPCQP SGNLVNPLNL TLSDPGVTPL SPQRRRRQLD PGGDQSSPPV TLAAAKKAKS
     ETVLTCSNGR ARCVWLECPL PDTSNITNVT VKARVWNSTF IEDYKDFDRV RVDGWATLFL
     RTSIPTINME NKTTWFSVDI DSELVEELPA EIELWLVLVA VGAGLLLLGL IILLLWKCGF
     FKRARTRALY EAKRQKAEMK SQPSETERLT DDY
//