ITA2B_HUMAN » Integrin alpha-IIb

ITA2B_HUMAN » Integrin alpha-IIb
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
ITA2B_HUMAN » Integrin alpha-IIb » Platelet membrane glycoprotein IIb;GPalpha IIb;GPIIb;
Hydrophobic Thickness 37.6 ± 2.2 Å
Tilt Angle 2 ± 1°
ΔGtransfer -54.9 kcal/mol
ΔGfold -21.9 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 996-1025 (994-1027)
Pathways

Abciximab Pathway (SMPDB)

Arrhythmogenic right ventricular cardiomyopathy (KEGG)

Developmental Biology (Reactome)

Dilated cardiomyopathy (KEGG)

ECM-receptor interaction (KEGG)

Eptifibatide Pathway (SMPDB)

Focal adhesion (KEGG)

Hematopoietic cell lineage (KEGG)

Hemostasis (Reactome)

Hypertrophic cardiomyopathy (KEGG)

Pathways in cancer (KEGG)

PI3K-Akt signaling pathway (KEGG)

Regulation of actin cytoskeleton (KEGG)

Signal Transduction (Reactome)

Small cell lung cancer (KEGG)

Tirofiban Pathway (SMPDB)

PDB 1dpq (1020-1039), 1s4w (1020-1039), 1dpk (1020-1039), 2k1a (989-1029), 1tye (A/C/E=32-483), 3fcu (A/C/E=32-488), 3nid (A/C=32-488), 3nif (A/C=32-488), 3nig (A/C=32-488), 3t3m (A/C=32-488), 3t3p (A/C=32-488), 3zdx (A/C=32-488), 3zdy (A/C=32-488), 3zdz (A/C=32-488), 3ze0 (A/C=32-488), 3ze1 (A/C=32-488), 3ze2 (A/C=32-488), 3fcs (A/C=32-989), 1kuz (A=1018-1028), 1kup (A=1018-1028), 1m8o (A=1020-1039), 2vdp (A=32-483), 2vdr (A=32-483), 2vdq (A=32-483), 2vdo (A=32-483), 2vdn (A=32-483), 2vdm (A=32-483), 2vdl (A=32-483), 2vdk (A=32-483), 2vc2 (A=32-483), 4cak (A=32-989), 2k9j (A=989-1029), 2knc (A=991-1039)
OPM 1s4w, 2k1a, 2k9j, 2knc
Complexes

ITA2B:ITB3_HUMAN

ITA2B:ITB3:IGKC_HUMAN

FIBG:ITA2B:ITB3:IGKC_HUMAN

Interactions

AUP1, Complex: AUP1:ITA2B, PubMed

ICAM4, Complex: ICAM4:ITB3:ITA2B

IL7RA, Complex: ITA2B:IL7RA, PubMed

ITB3, Complex: IGKC:ITA2B:ITB3, PDBID: 2vc2

Domains

AA: 320-362, PDBID: 1TYE, Subunit C, Seq Identity:100%, FG-GAP repeat

AA: 387-423, PDBID: 1TYE, Subunit C, Seq Identity:100%, FG-GAP repeat

AA: 481-921, PDBID: 1TYE, Subunit C, Seq Identity:100%, Integrin alpha

AA: 1020-1034, PDBID: 1DPK, Subunit A, Seq Identity:100%, Integrin alpha cytoplasmic region

UniProt annotation for ITA2B_HUMAN » Integrin alpha-IIb
FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha- IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.

SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. Interacts (via C-terminus cytoplasmic tail region) with CIB1; the interaction is direct and calcium- dependent. Interacts (via C-terminus cytoplasmic tail region) with CIB2, CIB3 and CIB4; the interactions are stabilized/increased in a calcium and magnesium-dependent manner.

TISSUE SPECIFICITY: Isoform 1 and isoform 2 were identified in platelets and megakaryocytes, but not in reticulocytes or in Jurkat and U-937 white blood cell line. Isoform 3 is expressed by leukemia, prostate adenocarcinoma and melanoma cells but not by platelets or normal prostate or breast epithelial cells.

DISEASE: Glanzmann thrombasthenia (GT) OMIM: A common inherited disease of platelet aggregation. It is characterized by mucocutaneous bleeding of mild-to-moderate severity. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the GPIIb-IIIa complex at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. mutations affecting the gene represented in this entry.

DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16) OMIM: An autosomal dominant form of congenital macrothrombocytopenia associated with platelet anisocytosis. It is a disorder of platelet production. Affected individuals may have no or only mildly increased bleeding tendency. In vitro studies show mild platelet functional abnormalities. Note=The disease is caused by mutations affecting the gene represented in this entry.

UniProt features for ITA2B_HUMAN » Integrin alpha-IIb
SIGNAL 1 31
CHAIN 32 1039 Integrin alpha-IIb.
CHAIN 32 887 Integrin alpha-IIb heavy chain.
CHAIN 891 1039 Integrin alpha-IIb light chain, form 1.
CHAIN 903 1039 Integrin alpha-IIb light chain, form 2.
REPEAT 35 96 FG-GAP 1.
REPEAT 110 173 FG-GAP 2.
REPEAT 186 238 FG-GAP 3.
REPEAT 251 310 FG-GAP 4.
REPEAT 311 371 FG-GAP 5.
REPEAT 373 432 FG-GAP 6.
REPEAT 434 496 FG-GAP 7.
MOTIF 1022 1026 GFFKR motif.
DISULFID 87 96
DISULFID 138 161
DISULFID 177 198
DISULFID 504 515
DISULFID 521 576
DISULFID 633 639
DISULFID 705 718
DISULFID 857 911 Interchain (between heavy and light chains).
DISULFID 916 921
Amino Acid Sequence for ITA2B_HUMAN » Integrin alpha-IIb
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV LVGVLGGLLL LTILVLAMWK VGFFKRNRPP LEEDDEEGE