ITA2_BOVIN
ID ITA2_BOVIN Reviewed; 1170 AA.
AC P53710;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Integrin alpha-2;
DE AltName: Full=CD49 antigen-like family member B;
DE AltName: Full=Collagen receptor;
DE AltName: Full=Platelet membrane glycoprotein Ia;
DE Short=GPIa;
DE AltName: Full=VLA-2 subunit alpha;
DE AltName: CD_antigen=CD49b;
DE Flags: Precursor; Fragment;
GN Name=ITGA2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7511592; DOI=10.1016/s0021-9258(17)36932-6;
RA Kamata T., Puzon W., Takada Y.;
RT "Identification of putative ligand binding sites within I domain of
RT integrin alpha 2 beta 1 (VLA-2, CD49b/CD29).";
RL J. Biol. Chem. 269:9659-9663(1994).
CC -!- FUNCTION: Integrin alpha-2/beta-1 is a receptor for laminin, collagen,
CC collagen C-propeptides, fibronectin and E-cadherin. It recognizes the
CC proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is
CC responsible for adhesion of platelets and other cells to collagens,
CC modulation of collagen and collagenase gene expression, force
CC generation and organization of newly synthesized extracellular matrix.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-2 associates
CC with beta-1. Interacts with HPS5 and RAB21 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; L25886; AAB59255.1; -; mRNA.
DR PIR; I45914; I45914.
DR AlphaFoldDB; P53710; -.
DR SMR; P53710; -.
DR STRING; 9913.ENSBTAP00000025685; -.
DR PaxDb; P53710; -.
DR PeptideAtlas; P53710; -.
DR PRIDE; P53710; -.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; P53710; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 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 InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL <1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1170
FT /note="Integrin alpha-2"
FT /id="PRO_0000016232"
FT TOPO_DOM 19..1121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1122..1143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1144..1170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 23..81
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 90..150
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 177..354
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 355..409
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 412..464
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 466..528
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 529..587
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 591..653
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 472..474
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1146..1150
FT /note="GFFKR motif"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 554
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 618
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 620
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 624
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..81
FT /evidence="ECO:0000250"
FT DISULFID 669..726
FT /evidence="ECO:0000250"
FT DISULFID 778..784
FT /evidence="ECO:0000250"
FT DISULFID 854..865
FT /evidence="ECO:0000250"
FT DISULFID 1008..1039
FT /evidence="ECO:0000250"
FT DISULFID 1044..1049
FT /evidence="ECO:0000250"
FT VARIANT 580
FT /note="G -> V"
FT VARIANT 588
FT /note="R -> K"
FT VARIANT 725
FT /note="R -> S"
FT NON_TER 1
SQ SEQUENCE 1170 AA; 128929 MW; EECEF1C5F2448FB1 CRC64;
PLQLVLVFSQ GILNCCVAYN VGLPKAKIFS GPSSEQFGYA VQQFINPKGN WLLVGSPWSG
FPKNRMGDVY KCPVDLSTTT CEKLNLQTST SMSNVTEMKT NMSLGLTLTR NVGTGGFLTC
GPLWAQQCGS QYYTTGVCSD VSPDFQLRTS FAPAVQTCPS FIDVVVVCDE SNSIYPWDAV
KNFLEKFVQG LDIGPTKTQM GLIQYANNPR VVFNLNTFKS KDEMIKATSQ TFQYGGDLTN
TFKAIQYARD TAYSTAAGGR PGATKVMVVV TDGESHDGSK LKAVIDQCNK DNILRFGIAV
LGYLNRNALD TKNLIKEIKA IASIPTERHF FNVSDEADLL EKAGTIGEQI FSIEGTVQGG
DNFQMEMSQV GFSAEYSPQN NILMLGAVGA YDWSGTVVQK TPHGHLIFSK QAFEQILQDR
NHSSYLGYSV ASISTGNSVH FVAGAPRANY TGQIVLYSVN ENGNVTVIQS QRGDQIGSYF
GSVLCAVDVN KDTITDVLLV GAPMYMNDLK KEEGRVYLFT ITKGILNWHQ FLEGPNGLEN
ARFGSAIAAL SDINMDGFND VIVGSPLENQ NSGAVYIYNG HEGMIRLRYS QKILGSDRAF
SSHLQYFGRS LDGYGDLNGD SITDVSVGAF GQVVQLWSQS IADVSVDASF TPKKITLLNK
NAEIKLKLCF SAKFRPTNQN NQVAIVYNIT IDEDQFSSRV ISRGLFKENN ERCLQKTMIV
SQAQRCSEYI IHIQEPSDII SPLNLCMNIS LENPGTNPAL EAYSETVKVF SIPFHKDCGD
DGVCISDLVL NVQQLPATQQ QPFIVSNQNK RLTFSVQLKN KKESAYNTEI VVDFSENLFF
ASWSMPVDGT EVTCQIASSQ KSVTCNVGYP ALKSKQQVTF TINFDFNLQN LQNQASISFR
ALSESQEENM ADNSVNLKLS LLYDAEIHIT RSTNINFYEV SLDGNVSSVV HSFEDIGPKF
IFSIKVTTGS VPVSMASVII HIPQYTKDKN PLMYLTGVHT DQAGDISCEA EINPLKIGQT
SSSVSFKSEN FRHIKELNCR TASCSNIMCW LRDLQVKGEY FLNVSTRIWN GTFAASTFQT
VQLTAAAEID TYNPQIYVIE ENTVTIPLTI MKPHEKVEVP TGVIVGSVIA GILLLLALVA
ILWKLGFFKR KYEKMAKNPD ETDETTELNS
