CD61

Integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)

PDB rendering based on 1jv2.

Available structures
PDB	1JV2, 1KUP, 1KUZ, 1L5G, 1M1X, 1M8O, 1MK7, 1MK9, 1RN0, 1S4X, 1TYE, 1U8C, 2INI, 2K9J, 2KNC, 2L1C, 2Q6W, 2RMZ, 2RN0, 2VC2, 2VDK, 2VDL, 2VDM, 2VDN, 2VDO, 2VDP, 2VDQ, 2VDR, 3FCS, 3FCU, 3IJE

Identifiers

Symbols

ITGB3; CD61; GP3A; GPIIIa

External IDs

OMIM: 173470 MGI: 96612 HomoloGene: 55444 GeneCards: ITGB3 Gene

Gene Ontology
Molecular function	• receptor activity • platelet-derived growth factor receptor binding • protein binding • identical protein binding • vascular endothelial growth factor receptor 2 binding • vascular endothelial growth factor receptor 2 binding • cell adhesion molecule binding
Cellular component	• plasma membrane • plasma membrane • integral to plasma membrane • integrin complex • platelet alpha granule membrane • alphav-beta3 integrin-vitronectin complex
Biological process	• positive regulation of protein phosphorylation • positive regulation of endothelial cell proliferation • platelet degranulation • cell adhesion • cell-matrix adhesion • integrin-mediated signaling pathway • axon guidance • blood coagulation • positive regulation of endothelial cell migration • negative regulation of macrophage derived foam cell differentiation • negative regulation of lipid storage • smooth muscle cell migration • platelet activation • positive regulation of vascular endothelial growth factor receptor signaling pathway • activation of protein kinase activity • negative regulation of lipid transport • tube development • wound healing • interspecies interaction between organisms • regulation of bone resorption • negative regulation of low-density lipoprotein particle receptor biosynthetic process • positive regulation of peptidyl-tyrosine phosphorylation • negative regulation of lipoprotein metabolic process • leukocyte migration • angiogenesis involved in wound healing
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
45.33 – 45.39 Mb

Chr 11:
104.47 – 104.53 Mb

PubMed search

[1]

[2]

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene.^[1] CD61 is a cluster of differentiation found on thrombocytes.

1 Structure and function
2 Role in endometriosis
3 Interactions
4 See also
5 References
6 Further reading
7 External links

Structure and function

The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.^[2]

Role in endometriosis

Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.^[3]

Interactions

CD61 has been shown to interact with PTK2,^[4]^[5] ITGB3BP,^[6]^[7] TLN1^[8]^[9] and CIB1.^[10]

References

^ Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS, et al. (Aug 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". J Clin Invest 81 (6): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442653.
^ "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3690.
^ May, K. E.; Villar, J.; Kirtley, S.; Kennedy, S. H.; Becker, C. M. (2011). "Endometrial alterations in endometriosis: A systematic review of putative biomarkers". Human Reproduction Update 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902. edit
^ Eliceiri, Brian P; Puente Xose S, Hood John D, Stupack Dwayne G, Schlaepfer David D, Huang Xiaozhu Z, Sheppard Dean, Cheresh David A (Apr. 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". J. Cell Biol. (United States) 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173263.
^ Chung, J; Gao A G, Frazier W A (Jun. 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. (UNITED STATES) 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439.
^ Fujimoto, Tetsuro-Takahiro; Katsutani Shinya, Shimomura Takeshi, Fujimura Kingo (Jan. 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thromb. Res. (United States) 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. ISSN 0049-3848. PMID 11864709.
^ Shattil, S J; O'Toole T, Eigenthaler M, Thon V, Williams M, Babior B M, Ginsberg M H (Nov. 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". J. Cell Biol. (UNITED STATES) 131 (3): 807–16. doi:10.1083/jcb.131.3.807. ISSN 0021-9525. PMC 2120613. PMID 7593198. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120613.
^ Patil, S; Jedsadayanmata A, Wencel-Drake J D, Wang W, Knezevic I, Lam S C (Oct. 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". J. Biol. Chem. (UNITED STATES) 274 (40): 28575–83. doi:10.1074/jbc.274.40.28575. ISSN 0021-9258. PMID 10497223.
^ Calderwood, David A; Yan Boxu, de Pereda Jose M, Alvarez Begoña García, Fujioka Yosuke, Liddington Robert C, Ginsberg Mark H (Jun. 2002). "The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. (United States) 277 (24): 21749–58. doi:10.1074/jbc.M111996200. ISSN 0021-9258. PMID 11932255.
^ Naik, U P; Patel P M, Parise L V (Feb. 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J. Biol. Chem. (UNITED STATES) 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. ISSN 0021-9258. PMID 9030514.

External links

MeSH CD61+Antigens
ITGB3 Info with links in the Cell Migration Gateway

PDB gallery

1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3

1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND

1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+

1m8o: Platelet integrin alfaIIb-beta3 cytoplasmic domain

1txv:

1ty3:

1ty5:

1ty6:

1ty7:

1tye: Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen

1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure

Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 (a-c, 1A, 1D, 1E) · CD2 · CD3 (γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 (a) · CD9 · CD10 · CD11 (a, b, c) · CD13 · CD14 · CD15 · CD16 (A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 (A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 (a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 (a, b, c, d, e, f) · CD50

51-100	CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 (E, L, P) · CD63 · CD64 (A, B, C) · CD66 (a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 (a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 (a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100

101-150	CD101 · CD102 · CD103 · CD104 · CD105 · CD106 · CD107 (a, b) · CD108 · CD109 · CD110 · CD111 · CD112 · CD113 · CD114 · CD115 · CD116 · CD117 · CD118 · CD119 · CD120 (a, b) · CD121 (a, b) · CD122 · CD123 · CD124 · CD125 · CD126 · CD127 · CD129 · CD130 · CD131 · CD132 · CD133 · CD134 · CD135 · CD136 · CD137 · CD138 · CD140b · CD141 · CD142 · CD143 · CD144 · CD146 · CD147 · CD148 · CD150

151-200	CD151 · CD152 · CD153 · CD154 · CD155 · CD156 (a, b, c) · CD157 · CD158 (a, d, e, i, k) · CD159 (a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 (a, b) · CD168 · CD169 · CD170 · CD171 · CD172 (a, b, g) · CD174 · CD177 · CD178 · CD179 (a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200

201-250	CD201 · CD202b · CD204 · CD205 · CD206 · CD207 · CD208 · CD209 · CDw210 (a, b) · CD212 · CD213a (1, 2) · CD217 · CD218 (a, b) · CD220 · CD221 · CD222 · CD223 · CD224 · CD225 · CD226 · CD227 · CD228 · CD229 · CD230 · CD233 · CD234 · CD235 (a, b) · CD236 · CD238 · CD239 · CD240CE · CD240D · CD241 · CD243 · CD244 · CD246 · CD247- CD248 · CD249

251-300	CD252 · CD253 · CD254 · CD256 · CD257 · CD258 · CD261 · CD262 · CD264 · CD265 · CD266 · CD267 · CD268 · CD269 · CD271 · CD272 · CD273 · CD274 · CD275 · CD276 · CD278 · CD279 · CD280 · CD281 · CD282 · CD283 · CD284 · CD286 · CD288 · CD289 · CD290 · CD292 · CDw293 · CD294 · CD295 · CD297 · CD298 · CD299

301-350	CD300A · CD301 · CD302 · CD303 · CD304 · CD305 · CD306 · CD307 · CD309 · CD312 · CD314 · CD315 · CD316 · CD317 · CD318 · CD320 · CD321 · CD322 · CD324 · CD325 · CD326 · CD328 · CD329 · CD331 · CD332 · CD333 · CD334 · CD335 · CD336 · CD337 · CD338 · CD339 · CD340 · CD344 · CD349 · CD350

Proteins: coagulation

Coagulation factors

Primary hemostasis	vWF platelet membrane glycoproteins: Ib (A, B, IX) · IIb/IIIa (IIb, IIIa) · VI

Intrinsic pathway	HMWK/Bradykinin · Prekallikrein/Kallikrein · XII "Hageman" XI · IX · VIII

Extrinsic pathway	III "Tissue factor" · VII

Common pathway	X · V · II "(Pro)thrombin" · I "Fibrin" · Fibrinogen (FGA, FGG) XIII

Coagulation inhibitors

Antithrombin (inhibits II, IX, X, XI, XII) · Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) · Protein Z (inhibits X) · ZPI (inhibits X, XI) · TFPI (inhibits III)

Thrombolysis/fibrinolysis

Plasmin · tPA/urokinase · PAI-1/2 · α2-AP · α2-macroglobulin · TAFI

M: MYL

cell/phys (coag, heme, immu, gran), csfs

rbmg/mogr/tumr/hist, sysi/epon, btst

drug (B1/2/3+5+6), btst, trns

Integrins

Alpha	A1 · A2 · A3 · A4 · A5 · A6 · A7 · A8 · A9 · A10 · A11 · AD · AE · AL · AM · AV · AX

Beta	B1 · B2 · B3 · B4 · B5 · B6 · B7 · B8

Dimers	Cytoadhesin receptor: Integrin alpha6beta4 · Glycoprotein IIb/IIIa (ITGA2B+ITGB3) Fibrinogen receptor: Macrophage-1 antigen (CD11b+CD18) Fibronectin receptor: Integrin alpha2beta1 · Integrin alpha4beta1 · Integrin alpha5beta1 Leukocyte-adhesion receptor: LFA-1 (CD11a+CD18) · Macrophage-1 antigen (CD11b+CD18) · Integrin alphaXbeta2 (CD11c+CD18) Very late antigen receptor: Integrin alpha1beta1 · Integrin alpha2beta1 · Integrin alpha3beta1 · VLA-4 (CD49d+CD29) · Alpha-5 beta-1 · Integrin alpha6beta1 Vitronectin receptor: Alpha-v beta-3 · Alpha-v beta-5

see also cell surface receptor deficiencies B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

CD61

Contents

Structure and function

Role in endometriosis

Interactions

See also

References

Further reading

External links