Integrin alpha 3

Mammalian protein found in Homo sapiens
ITGA3
Identifiers
AliasesITGA3, CD49C, GAP-B3, GAPB3, ILNEB, MSK18, VCA-2, VL3A, VLA3a, FRP-2, integrin subunit alpha 3, JEB7
External IDsOMIM: 605025; MGI: 96602; HomoloGene: 21129; GeneCards: ITGA3; OMA:ITGA3 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for ITGA3
Genomic location for ITGA3
Band17q21.33Start50,055,968 bp[1]
End50,090,481 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for ITGA3
Genomic location for ITGA3
Band11 D|11 59.01 cMStart94,935,300 bp[2]
End94,967,627 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • metanephric glomerulus

  • right coronary artery

  • upper lobe of left lung

  • Descending thoracic aorta

  • popliteal artery

  • tibial arteries

  • right lung

  • right lobe of thyroid gland

  • ascending aorta

  • left lobe of thyroid gland
Top expressed in
  • genital tubercle

  • lumbar spinal ganglion

  • decidua

  • tail of embryo

  • corneal stroma

  • yolk sac

  • crypt of lieberkuhn of small intestine

  • right lung lobe

  • epithelium of lens

  • ileum
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • protein domain specific binding
  • laminin binding
  • collagen binding
  • protease binding
  • protein heterodimerization activity
  • integrin binding
  • fibronectin binding
  • protein binding
Cellular component
  • extracellular exosome
  • synapse
  • integral component of membrane
  • cell projection
  • cell periphery
  • cell junction
  • growth cone
  • membrane
  • focal adhesion
  • cell surface
  • receptor complex
  • synaptic membrane
  • perinuclear region of cytoplasm
  • excitatory synapse
  • integrin complex
  • basolateral plasma membrane
  • filopodium membrane
  • external side of plasma membrane
  • integrin alpha3-beta1 complex
  • plasma membrane
  • growth cone filopodium
Biological process
  • positive regulation of neuron projection development
  • extracellular matrix organization
  • lung development
  • mesodermal cell differentiation
  • skin development
  • maternal process involved in female pregnancy
  • cell-matrix adhesion
  • negative regulation of cell projection organization
  • positive regulation of cell-substrate adhesion
  • heart development
  • dendritic spine maintenance
  • positive regulation of gene expression
  • nephron development
  • memory
  • integrin-mediated signaling pathway
  • response to gonadotropin
  • leukocyte migration
  • renal filtration
  • regulation of transforming growth factor beta receptor signaling pathway
  • regulation of Wnt signaling pathway
  • regulation of BMP signaling pathway
  • negative regulation of Rho protein signal transduction
  • exploration behavior
  • positive regulation of epithelial cell migration
  • neuron migration
  • cell adhesion
  • positive regulation of protein localization to plasma membrane
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3675

16400

Ensembl

ENSG00000005884

ENSMUSG00000001507

UniProt

P26006

Q62470

RefSeq (mRNA)

NM_002204
NM_005501

NM_013565
NM_001306071
NM_001306162

RefSeq (protein)

NP_002195

NP_001293000
NP_001293091
NP_038593

Location (UCSC)Chr 17: 50.06 – 50.09 MbChr 11: 94.94 – 94.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Integrin alpha-3 is a protein that in humans is encoded by the ITGA3 gene.[5][6] ITGA3 is an integrin alpha subunit. Together with beta-1 subunit, it makes up half of the α3β1 integrin duplex that plays a role in neural migration and corticogenesis, acted upon by such factors as netrin-1 and reelin.

ITGA3 encodes the integrin alpha 3 chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 3 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form an integrin that interacts with many extracellular matrix proteins.

Alternative names

The alpha 3 beta 1 integrin is known variously as: very late (activation) antigen 3 ('VLA-3'), very common antigen 2 ('VCA-2'), extracellular matrix receptor 1 ('ECMR1'), and galactoprotein b3 ('GAPB3').[7]

Interactions

CD49c has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000005884 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001507 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Takada Y, Murphy E, Pil P, Chen C, Ginsberg MH, Hemler ME (October 1991). "Molecular cloning and expression of the cDNA for alpha 3 subunit of human alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen". J Cell Biol. 115 (1): 257–66. doi:10.1083/jcb.115.1.257. PMC 2289928. PMID 1655803.
  6. ^ Jones SD, van der Flier A, Sonnenberg A (September 1998). "Genomic organization of the human alpha 3 integrin subunit gene". Biochem Biophys Res Commun. 248 (3): 896–8. doi:10.1006/bbrc.1998.9071. PMID 9704023.
  7. ^ "Entrez Gene: ITGA3 integrin, alpha 3 (antigen CD49C, alpha 3 subunit of VLA-3 receptor)".
  8. ^ Park KR, Inoue T, Ueda M, Hirano T, Higuchi T, Maeda M, Konishi I, Fujiwara H, Fujii S (March 2000). "CD9 is expressed on human endometrial epithelial cells in association with integrins alpha(6), alpha(3) and beta(1)". Mol. Hum. Reprod. 6 (3): 252–7. doi:10.1093/molehr/6.3.252. PMID 10694273.
  9. ^ Hirano T, Higuchi T, Ueda M, Inoue T, Kataoka N, Maeda M, Fujiwara H, Fujii S (February 1999). "CD9 is expressed in extravillous trophoblasts in association with integrin alpha3 and integrin alpha5". Mol. Hum. Reprod. 5 (2): 162–7. doi:10.1093/molehr/5.2.162. PMID 10065872.
  10. ^ Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M (October 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem. 275 (43): 33669–78. doi:10.1074/jbc.M002519200. PMID 10906324.
  11. ^ Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (July 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". J. Cell Sci. 113 (13): 2385–97. doi:10.1242/jcs.113.13.2385. PMID 10852818.
  12. ^ Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (November 1997). "NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins". J. Biol. Chem. 272 (46): 29181–9. doi:10.1074/jbc.272.46.29181. PMID 9360996.

Further reading

  • Bosman FT (1993). "Integrins: cell adhesives and modulators of cell function". Histochem. J. 25 (7): 469–77. doi:10.1007/BF00159282. PMID 8407358. S2CID 19661102.
  • Fornaro M, Languino LR (1998). "Alternatively spliced variants: a new view of the integrin cytoplasmic domain". Matrix Biol. 16 (4): 185–93. doi:10.1016/S0945-053X(97)90007-X. PMID 9402008.
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Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:
see also cell surface receptor deficiencies


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