ITA5_MOUSE
ID ITA5_MOUSE Reviewed; 1053 AA.
AC P11688; E9QN40;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Integrin alpha-5;
DE AltName: Full=CD49 antigen-like family member E;
DE AltName: Full=Fibronectin receptor subunit alpha;
DE AltName: Full=Integrin alpha-F;
DE AltName: Full=VLA-5;
DE AltName: CD_antigen=CD49e;
DE Contains:
DE RecName: Full=Integrin alpha-5 heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-5 light chain;
DE Flags: Precursor;
GN Name=Itga5;
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].
RC TISSUE=Bone marrow;
RA Morrisey E., Dutt P., Patel V.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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 [MRNA] OF 645-1053.
RC STRAIN=BALB/cJ;
RX PubMed=2523953; DOI=10.1084/jem.169.5.1589;
RA Holers V.M., Ruff T.G., Parks D.L., McDonald J.A., Ballard L.L.,
RA Brown E.J.;
RT "Molecular cloning of a murine fibronectin receptor and its expression
RT during inflammation. Expression of VLA-5 is increased in activated
RT peritoneal macrophages in a manner discordant from major histocompatibility
RT complex class II.";
RL J. Exp. Med. 169:1589-1605(1989).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=7508365; DOI=10.1242/dev.119.4.1093;
RA Yang J.T., Rayburn H., Hynes R.O.;
RT "Embryonic mesodermal defects in alpha 5 integrin-deficient mice.";
RL Development 119:1093-1105(1993).
RN [5]
RP INTERACTION WITH NISCH.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11121431; DOI=10.1083/jcb.151.6.1141;
RA Alahari S.K., Lee J.W., Juliano R.L.;
RT "Nischarin, a novel protein that interacts with the integrin alpha5 subunit
RT and inhibits cell migration.";
RL J. Cell Biol. 151:1141-1154(2000).
RN [6]
RP INTERACTION WITH NISCH.
RX PubMed=14535848; DOI=10.1042/bj20030411;
RA Alahari S.K., Nasrallah H.;
RT "A membrane proximal region of the integrin alpha5 subunit is important for
RT its interaction with nischarin.";
RL Biochem. J. 377:449-457(2004).
RN [7]
RP INTERACTION WITH NISCH.
RX PubMed=15229651; DOI=10.1038/sj.emboj.7600291;
RA Alahari S.K., Reddig P.J., Juliano R.L.;
RT "The integrin-binding protein Nischarin regulates cell migration by
RT inhibiting PAK.";
RL EMBO J. 23:2777-2788(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300; ASN-310; ASN-596; ASN-612
RP AND ASN-678.
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-596; ASN-612; ASN-678;
RP ASN-715 AND ASN-727.
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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-5/beta-1 (ITGA5:ITGB1) is a receptor for
CC fibronectin and fibrinogen. It recognizes the sequence R-G-D in its
CC ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is
CC distinct from the classical ligand-binding site (site 1) and this
CC induces integrin conformational changes and enhanced ligand binding to
CC site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and
CC mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a
CC receptor for IL1B and binding is essential for IL1B signaling.
CC ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for
CC CD40/CD40LG signaling (By similarity). {ECO:0000250|UniProtKB:P08648}.
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-5 associates with beta-1. Interacts with NISCH (PubMed:11121431,
CC PubMed:14535848, PubMed:15229651). Interacts with HPS5 (By similarity).
CC Interacts with RAB21 and COMP. Interacts with CIB1 (By similarity).
CC ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA5:ITGB1 interacts
CC with FBN1 (By similarity). ITGA5:ITGB1 interacts with IL1B (By
CC similarity). ITGA5:ITGB1 interacts with ACE2 (By similarity). Interacts
CC with ANGPT2 (By similarity). {ECO:0000250|UniProtKB:P08648,
CC ECO:0000269|PubMed:11121431, ECO:0000269|PubMed:14535848,
CC ECO:0000269|PubMed:15229651}.
CC -!- INTERACTION:
CC P11688; P68254: Ywhaq; NbExp=2; IntAct=EBI-6477055, EBI-400675;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:P08648}. Cell
CC surface {ECO:0000250|UniProtKB:P08648}.
CC -!- PTM: Proteolytic cleavage by PCSK5 mediates activation of the
CC precursor. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die at 10-11 dpc. They show both
CC extraembryonic and embryonic vascular defects, and severe abnormalities
CC in the development of the posterior trunk.
CC {ECO:0000269|PubMed:7508365}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; X79003; CAA55638.1; -; mRNA.
DR EMBL; AC131721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X15203; CAA33273.1; -; mRNA.
DR CCDS; CCDS27903.1; -.
DR PIR; S44250; S44250.
DR RefSeq; NP_034707.5; NM_010577.4.
DR AlphaFoldDB; P11688; -.
DR SMR; P11688; -.
DR BioGRID; 200818; 35.
DR ComplexPortal; CPX-3027; Integrin alpha5-beta1 complex.
DR CORUM; P11688; -.
DR IntAct; P11688; 32.
DR MINT; P11688; -.
DR STRING; 10090.ENSMUSP00000023128; -.
DR GlyConnect; 2398; 1 N-Linked glycan (1 site).
DR GlyGen; P11688; 14 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P11688; -.
DR PhosphoSitePlus; P11688; -.
DR jPOST; P11688; -.
DR MaxQB; P11688; -.
DR PaxDb; P11688; -.
DR PeptideAtlas; P11688; -.
DR PRIDE; P11688; -.
DR ProteomicsDB; 301685; -.
DR Antibodypedia; 1221; 1177 antibodies from 47 providers.
DR DNASU; 16402; -.
DR Ensembl; ENSMUST00000023128; ENSMUSP00000023128; ENSMUSG00000000555.
DR GeneID; 16402; -.
DR KEGG; mmu:16402; -.
DR UCSC; uc007xyb.3; mouse.
DR CTD; 3678; -.
DR MGI; MGI:96604; Itga5.
DR VEuPathDB; HostDB:ENSMUSG00000000555; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000158061; -.
DR HOGENOM; CLU_004111_4_0_1; -.
DR InParanoid; P11688; -.
DR OMA; KPPLYQP; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; P11688; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-1566977; Fibronectin matrix formation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-445144; Signal transduction by L1.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR BioGRID-ORCS; 16402; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Itga5; mouse.
DR PRO; PR:P11688; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P11688; protein.
DR Bgee; ENSMUSG00000000555; Expressed in embryonic post-anal tail and 155 other tissues.
DR ExpressionAtlas; P11688; baseline and differential.
DR Genevisible; P11688; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; ISO:MGI.
DR GO; GO:0008305; C:integrin complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0023035; P:CD40 signaling pathway; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:MGI.
DR GO; GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IGI:BHF-UCL.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IEA:Ensembl.
DR Gene3D; 2.130.10.130; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000250"
FT CHAIN 45..1053
FT /note="Integrin alpha-5"
FT /id="PRO_0000016252"
FT CHAIN 45..898
FT /note="Integrin alpha-5 heavy chain"
FT /id="PRO_0000016253"
FT CHAIN 899..1053
FT /note="Integrin alpha-5 light chain"
FT /id="PRO_0000016254"
FT TOPO_DOM 45..999
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1000..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 46..111
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 131..191
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 196..248
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 262..314
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 315..380
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 381..440
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 444..507
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 879..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1024..1028
FT /note="GFFKR motif"
FT BINDING 265
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /ligand_part_note="Arg of R-G-D sequence recognized in
FT fibronectin and fibrinogen"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /ligand_part_note="Arg of R-G-D sequence recognized in
FT fibronectin and fibrinogen"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 470
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 776
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..111
FT /evidence="ECO:0000250"
FT DISULFID 159..179
FT /evidence="ECO:0000250"
FT DISULFID 195..208
FT /evidence="ECO:0000250"
FT DISULFID 516..525
FT /evidence="ECO:0000250"
FT DISULFID 531..587
FT /evidence="ECO:0000250"
FT DISULFID 648..654
FT /evidence="ECO:0000250"
FT DISULFID 721..734
FT /evidence="ECO:0000250"
FT DISULFID 873..915
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 920..925
FT /evidence="ECO:0000250"
FT CONFLICT 68
FT /note="E -> Q (in Ref. 1; CAA55638)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="G -> A (in Ref. 1; CAA55638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 115043 MW; 8624AEF83E4A9C07 CRC64;
MGSWTPRSPR SPLHAVLLRW GPRRLPPLLP LLLLLWPPPL QVGGFNLDAE APAVLSGPPG
SLFGFSVEFY RPGRDGVSVL VGAPKANTSQ PGVLQGGAVY VCPWGTSPIQ CTTIQFDSKG
SRILESSLYS AKGEEPVEYK SLQWFGATVR AHGSSILACA PLYSWRTEKD PQNDPVGTCY
LSTENFTRIL EYAPCRSDFG SAAGQGYCQG GFSAEFTKTG RVVLGGPGSY FWQGQILSAT
QEQISESYYP EYLINPVQGQ LQTRQASSVY DDSYLGYSVA VGEFSGDDTE DFVAGVPKGN
LTYGYVTVLN GSDIHSLYNV SGEQMASYFG YAVAATDTNG DGLDDLLVGA PLLMERTADG
RPQEVGRVYI YLQRPAGIDP TPTLTLTGQD EFSRFGSSLT PLGDLDQDGY NDVAIGAPFG
GEAQQGVVFI FPGGPGGLST KPSQVLQPLW AAGRTPDFFG SALRGGRDLD GNGYPDLIVG
SFGVDKALVY RGRPIISASA SLTIFPSMFN PEERSCSLEG NPVSCINLSF CLNASGKHVP
NSIGFEVELQ LDWQKQKGGV RRALFLTSKQ ATLTQTLLIQ NGAREDCREM KIYLRNESEF
RDKLSPIHIA LNFSLDPKAP MDSHGLRPVL HYQSKSRIED KAQILLDCGE DNICVPDLQL
DVYGEKKHVY LGDKNALNLT FHAQNLGEGG AYEAELRVTA PLEAEYSGLV RHPGNFSSLS
CDYFAVNQSR QLVCDLGNPM KAGTSLWGGL RFTVPHLQDT KKTIQFDFQI LSKNLNNSQS
NVVSFPLSVE AQAQVSLNGV SKPEAVIFPV SDWNPQDQPQ KEEDLGPAVH HVYELINQGP
SSISQGVLEL SCPQALEGQQ LLYVTKVTGL SNCTSNYTPN SQGLELDPET SPHHLQKREA
PGRSSTASGT QVLKCPEAKC FRLRCEFGPL HRQESRSLQL HFRVWAKTFL QREYQPFSLQ
CEAVYEALKM PYQILPRQLP QKKLQVATAV QWTKAEGSNG VPLWIIILAI LFGLLLLGLL
IYVLYKLGFF KRSLPYGTAM EKAQLKPPAT SDA
