Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QUM0 (ITA2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-IIb
Alternative name(s):
GPalpha IIb
Short name=GPIIb
Platelet membrane glycoprotein IIb
CD_antigen=CD41
Gene names
Name:Itga2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1033 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 structure

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 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 By similarity
Chain32 – 10331002Integrin alpha-IIb
PRO_0000016278
Chain32 – ?Integrin alpha-IIb heavy chain By similarityPRO_0000016279
Chain? – 1033Integrin alpha-IIb light chain By similarityPRO_0000016280

Regions

Topological domain32 – 988957Extracellular Potential
Transmembrane989 – 101426Helical; Potential
Topological domain1015 – 103319Cytoplasmic Potential
Repeat35 – 9662FG-GAP 1
Repeat109 – 17365FG-GAP 2
Repeat184 – 23754FG-GAP 3
Repeat252 – 30958FG-GAP 4
Repeat310 – 37061FG-GAP 5
Repeat372 – 43160FG-GAP 6
Repeat433 – 49563FG-GAP 7
Calcium binding273 – 2819 Potential
Calcium binding327 – 3359 Potential
Calcium binding395 – 4039 Potential
Calcium binding456 – 4649 Potential
Motif1017 – 10215GFFKR motif

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation6001N-linked (GlcNAc...) Potential
Glycosylation7101N-linked (GlcNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 96 By similarity
Disulfide bond138 ↔ 161 By similarity
Disulfide bond177 ↔ 197 By similarity
Disulfide bond503 ↔ 514 By similarity
Disulfide bond520 ↔ 575 By similarity
Disulfide bond632 ↔ 638 By similarity
Disulfide bond704 ↔ 717 By similarity
Disulfide bond856 ↔ 905Interchain (between heavy and light chains) By similarity
Disulfide bond911 ↔ 916 By similarity

Experimental info

Sequence conflict2361S → T in AAF06996. Ref.1
Sequence conflict2361S → T in AAD56216. Ref.1
Sequence conflict2701A → S in AAF06996. Ref.1
Sequence conflict2701A → S in AAD56216. Ref.1
Sequence conflict4641D → G in AAF43997. Ref.7
Sequence conflict4711G → W in AAF06996. Ref.1
Sequence conflict4711G → W in AAD56216. Ref.1
Sequence conflict4831V → G in AAF06996. Ref.1
Sequence conflict4831V → G in AAD56216. Ref.1
Sequence conflict8051R → S in AAF06996. Ref.1
Sequence conflict8051R → S in AAD56216. Ref.1
Sequence conflict8341P → H in AAD02339. Ref.6
Sequence conflict848 – 8492VQ → LR in AAD02339. Ref.6
Sequence conflict8651D → E in AAB23054. Ref.5
Sequence conflict9331V → A in AAF06996. Ref.1
Sequence conflict9331V → A in AAD56216. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QUM0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7B4826E32B9130B1

FASTA1,033112,678
        10         20         30         40         50         60 
MARASCAWHS LWLLQWTPLF LGPSAVPPVW ALNLDSEKFS VYAGPNGSHF GFSVDFHKDK 

        70         80         90        100        110        120 
HGSVSIVVGA PRALNASQEE TGAVFLCPWK ANGGKCNPLL FDLRDETRNL GFQIFQTFKT 

       130        140        150        160        170        180 
GQGLGASVVS WNDVIVACAP WQHWNVLEKR DEAEKTPVGG CFLAQLQSGG RAEYSPCRAN 

       190        200        210        220        230        240 
TMSSVYAESF RGDKRYCEAG FSLAVTQAGE LVLGAPGGYF FLGLLARVPI ENIISSYRPG 

       250        260        270        280        290        300 
TLLWHVSNQR FTYDNSNPVF FDGYRGYSVA VGEFDGDPST TEYVSGAPTW SWTLGAVEIL 

       310        320        330        340        350        360 
DSYYQPLHRL HGEQMASYFG HSVAVTDVNG DGRHDLLVGA PLYMESRADR KLAEVGRVYL 

       370        380        390        400        410        420 
FLQPKGPQAL STPTLLLTGT QLYGRFGSAI APLGDLNRDG YNDIAVAAPY GGPSGQGQVL 

       430        440        450        460        470        480 
IFLGQSEGLS PRPSQVLDSP FPTGSGFGFS LRGAVDIDDN GYPDLIVGAY GASKVAVYRA 

       490        500        510        520        530        540 
QPVVMATVQL MVQDSLNPTL KNCVLDQTKT PVSCFNIQMC VGATGHNIPQ KLHLKAELQL 

       550        560        570        580        590        600 
DLQKPRQGRR VLLLASQQAS LTLSLDLGGR DKPICHTTGA FLRDEADFRD KLSPIVLSLN 

       610        620        630        640        650        660 
VSLPPEETGG APAVVLHGET HVQEQTRIIL DCGEDDLCVP QLRLTATAGD SPLLIGADNV 

       670        680        690        700        710        720 
LELKIEAAND GEGAYEAELA VHLPPGAHYM RALSNIEGFE RLVCTQKKEN ESRVALCELG 

       730        740        750        760        770        780 
NPMKKDTRIG ITMLVSVENL EEAGESVSFQ LQVRSKNSQN PNSKVVMLPV AIQAEATVEL 

       790        800        810        820        830        840 
RGNSFPASLV VAAEEGDREQ EDLDRWVSRL EHTYELHNIG PGTVNGLRLL IHIPGQSQPS 

       850        860        870        880        890        900 
DLLYILDVQP QGGLLCSTQP SPKVDWKLST PSPSSIRPVH HQRERRQAFL QGPKPGQQDP 

       910        920        930        940        950        960 
VLVSCDGSAS CTVVECELRE MVRGQRAMVT VQVMLGLSSL RQRPQEQFVL QSHAWFNVSS 

       970        980        990       1000       1010       1020 
LPYSVPVVSL PSGQARVQTQ LLRALEERAI PVWWVLVGVL GGLLLLTLLV LAMWKAGFFK 

      1030 
RNRPPLEEDE EEE 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the murine platelet alphaIIb gene and encoded cDNA."
Thornton M.A., Poncz M.
Blood 94:3947-3950(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Heart.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Identification of the alpha IIb beta 3 integrin in murine tumor cells."
Chen Y.Q., Gao X., Timar J., Tang D., Grossi I.M., Chelladurai M., Kunicki T.J., Fligiel S.E., Taylor J.D., Honn K.V.
J. Biol. Chem. 267:17314-17320(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 805-865.
[6]Rout U.K., Armant D.R.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 790-1022.
[7]"Multiple discontinuous ligand-mimetic antibody binding sites define a ligand binding pocket in integrin alphaIIbbeta3."
Puzon-McLaughlin W., Kamata T., Takada Y.
J. Biol. Chem. 275:7795-7802(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-484.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF169829 Genomic DNA. Translation: AAF06996.1.
AF170316 mRNA. Translation: AAD56216.1.
AK142289 mRNA. Translation: BAE25013.1.
AK154619 mRNA. Translation: BAE32718.1.
AL596258 Genomic DNA. Translation: CAM18010.1.
BC120493 mRNA. Translation: AAI20494.1.
S43388 mRNA. Translation: AAB23054.2.
AF045019 mRNA. Translation: AAD02339.1.
AF166384 mRNA. Translation: AAF43997.1.
PIRA43430.
RefSeqNP_034705.2. NM_010575.2.
UniGeneMm.26646.

3D structure databases

ProteinModelPortalQ9QUM0.
SMRQ9QUM0. Positions 32-1024.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QUM0. 1 interaction.
MINTMINT-4098793.

PTM databases

PhosphoSiteQ9QUM0.

Proteomic databases

PaxDbQ9QUM0.
PRIDEQ9QUM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103086; ENSMUSP00000099375; ENSMUSG00000034664.
GeneID16399.
KEGGmmu:16399.
UCSCuc007lrx.2. mouse.

Organism-specific databases

CTD3674.
MGIMGI:96601. Itga2b.

Phylogenomic databases

eggNOGNOG26407.
GeneTreeENSGT00750000117267.
HOGENOMHOG000231603.
HOVERGENHBG006186.
InParanoidQ3U3R7.
KOK06476.
OMACFNIQMC.
OrthoDBEOG7TMZQZ.
TreeFamTF105391.

Gene expression databases

BgeeQ9QUM0.
CleanExMM_ITGA2B.
GenevestigatorQ9QUM0.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289549.
PROQ9QUM0.
SOURCESearch...

Entry information

Entry nameITA2B_MOUSE
AccessionPrimary (citable) accession number: Q9QUM0
Secondary accession number(s): Q3U3R7, Q64229, Q9Z2M0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot