ITA2B_PAPCY
ID ITA2B_PAPCY Reviewed; 604 AA.
AC P53711;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Integrin alpha-IIb;
DE AltName: Full=GPalpha IIb;
DE Short=GPIIb;
DE AltName: Full=Platelet membrane glycoprotein IIb;
DE AltName: CD_antigen=CD41;
DE Contains:
DE RecName: Full=Integrin alpha-IIb heavy chain;
DE Contains:
DE RecName: Full=Integrin alpha-IIb light chain;
DE Flags: Fragment;
GN Name=ITGA2B;
OS Papio cynocephalus (Yellow baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9556;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828888; DOI=10.1016/0378-1119(94)90669-6;
RA Hayzer D.J., Shoji M., Kim T.M., Runge M.S., Hanson S.R.;
RT "Alternative splicing of the mRNA encoding baboon glycoprotein receptor
RT GPIIb.";
RL Gene 151:267-271(1994).
CC -!- FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin,
CC fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin.
CC It recognizes the sequence R-G-D in a wide array of ligands. It
CC recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma
CC chain. Following activation integrin alpha-IIb/beta-3 brings about
CC platelet/platelet interaction through binding of soluble fibrinogen.
CC This step leads to rapid platelet aggregation which physically plugs
CC ruptured endothelial cell surface.
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-IIb associates with beta-3. Directly interacts with RNF181.
CC Interacts (via C-terminus cytoplasmic tail region) with CIB1; the
CC interaction is direct and calcium-dependent. Interacts (via C-terminus
CC cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are
CC stabilized/increased in a calcium and magnesium-dependent manner (By
CC similarity). ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction is
CC ROS and PPIase activity-dependent and is increased in the presence of
CC thrombin (By similarity). {ECO:0000250|UniProtKB:P08514,
CC ECO:0000250|UniProtKB:Q9QUM0}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; L12233; AAA65936.1; -; mRNA.
DR PIR; I36917; I36917.
DR AlphaFoldDB; P53711; -.
DR BMRB; P53711; -.
DR SMR; P53711; -.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.130; -; 1.
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; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 1.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW Metal-binding; Receptor; Transmembrane; Transmembrane helix.
FT CHAIN <1..467
FT /note="Integrin alpha-IIb heavy chain"
FT /id="PRO_0000016281"
FT CHAIN 468..604
FT /note="Integrin alpha-IIb light chain"
FT /id="PRO_0000016282"
FT TOPO_DOM <1..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 1..61
FT /note="FG-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 587..591
FT /note="GFFKR motif"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..80
FT /evidence="ECO:0000250"
FT DISULFID 86..141
FT /evidence="ECO:0000250"
FT DISULFID 198..204
FT /evidence="ECO:0000250"
FT DISULFID 270..283
FT /evidence="ECO:0000250"
FT DISULFID 422..476
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250"
FT DISULFID 481..486
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 604 AA; 66066 MW; 0B13BD1BD9E37F88 CRC64;
QVLDSPFPTG SAFGFSLRGA VDIDDNGYPD LIVGAYGANQ VAVYRAQPVV KASVQLLVQD
SLNPAVKSCV LPQTKTPVSC FKIQMCVGAT GHNIPQKLSL NAELQLDRQK PRQGRRVLLL
GSQQAGTTLN LDLGGKHSPI CHTTMAFLRD EADIRDKLSP IVLSLNVSLP PTEAGMAPAV
VLHGDTHVQE QTRIVLDCGE DDVCVPQLQL TASVTGSPLL VGADNVLELQ MDTANEGEGA
YEAELAVHLP QGAHYMRARS NVEGFERLIC NQKKENETRV VLCELGNPMK KNTQIGIAML
VSVGNLEEAG ESVSFQLQIR SKNSQNPNSK IVLLDVPVRA EAQVELRGNS FPASLVVAAE
EGDREQNSLD SWGPKVEHTY ELHNNGPGTV NGLHLSIHLP GQSQHSDLLY ILDIQPQGGL
QCFPQPPVNP LKVDWGLPTP SPSPVHPAHH KRDRRQIFLP EPEQPSRLQD PVLVSCDSAP
CTVVQCDLQE MARGQRAMVT VLAFLWLPSL HQRPLDQFVL QSQAWFNVSS LPYAVPPLSL
PRGEAQVRTQ LLRALEERAI PIWWVLVGVL GGLLLLTILV LAMWKVGFFK RNRPPLEEDD
EEGE
