Integrin alpha 9

ITGA9
Identifiers
Aliases	ITGA9, ALPHA-RLC, ITGA4L, RLC, integrin subunit alpha 9
External IDs	OMIM: 603963; MGI: 104756; HomoloGene: 1664; GeneCards: ITGA9; OMA:ITGA9 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p22.2 Start 37,452,115 bp End 37,823,507 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 F3|9 70.32 cM Start 118,435,758 bp End 118,730,071 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in urethra saphenous vein visceral pleura right ventricle Descending thoracic aorta tendon of biceps brachii vena cava ascending aorta thyroid gland right lobe of thyroid gland Top expressed in zygote ascending aorta secondary oocyte primary oocyte aortic valve Gonadal ridge external carotid artery internal carotid artery genital tubercle interventricular septum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function metal ion binding laminin binding collagen binding Cellular component integrin complex basal plasma membrane plasma membrane membrane integrin alpha9-beta1 complex integral component of membrane Biological process wound healing integrin-mediated signaling pathway extracellular matrix organization neutrophil chemotaxis cell adhesion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3680 104099 Ensembl ENSG00000144668 ENSMUSG00000039115 UniProt Q13797 B8JK39 RefSeq (mRNA) NM_002207 NM_001113514 NM_133721 RefSeq (protein) NP_002198 NP_001106986 NP_598482 Location (UCSC) Chr 3: 37.45 – 37.82 Mb Chr 9: 118.44 – 118.73 Mb PubMed search
Wikidata
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Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene. Cytogenetic location: 3p22.2

Function

This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for tenascin-C, VCAM1 and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.

Interactions

The α9 subunit forms a heterodimeric complex with a β1 subunit to form the α9β1 integrin. This integrin participates in cell adhesion with various ligands in the extracellular matrix (ECM), including extra domain A (EDA) fibronectin, tenascin-C, ADAMs, EMELIN1, osteopontin, and VEGF. α9β1 binding is independent of the RGD peptide sequence.

Further reading

• Evans JP (2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization". BioEssays. 23 (7): 628–39. doi:10.1002/bies.1088. PMID 11462216. S2CID 23712246.
• Yamakawa K, Takahashi T, Horio Y, Murata Y, Takahashi E, Hibi K, Yokoyama S, Ueda R, Takahashi T, Nakamura Y (1993). "Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22". Oncogene. 8 (2): 327–30. PMID 8381220.
• Yokosaki Y, Monis H, Chen J, Sheppard D (1996). "Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains". J. Biol. Chem. 271 (39): 24144–50. doi:10.1074/jbc.271.39.24144. PMID 8798654.
• Yokosaki Y, Matsuura N, Sasaki T, Murakami I, Schneider H, Higashiyama S, Saitoh Y, Yamakido M, Taooka Y, Sheppard D (2000). "The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin". J. Biol. Chem. 274 (51): 36328–34. doi:10.1074/jbc.274.51.36328. PMID 10593924.
• Young BA, Taooka Y, Liu S, Askins KJ, Yokosaki Y, Thomas SM, Sheppard D (2002). "The cytoplasmic domain of the integrin alpha9 subunit requires the adaptor protein paxillin to inhibit cell spreading but promotes cell migration in a paxillin-independent manner". Mol. Biol. Cell. 12 (10): 3214–25. doi:10.1091/mbc.12.10.3214. PMC 60168. PMID 11598204.
• Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions". J. Biol. Chem. 277 (20): 17804–10. doi:10.1074/jbc.M200086200. PMID 11882657.
• Majumdar M, Tarui T, Shi B, Akakura N, Ruf W, Takada Y (2004). "Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1)". J. Biol. Chem. 279 (36): 37528–34. doi:10.1074/jbc.M401372200. PMID 15247268.
• Chen C, Young BA, Coleman CS, Pegg AE, Sheppard D (2004). "Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration". J. Cell Biol. 167 (1): 161–70. doi:10.1083/jcb.200312166. PMC 2172529. PMID 15479742.
• Vlahakis NE, Young BA, Atakilit A, Sheppard D (2005). "The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1". J. Biol. Chem. 280 (6): 4544–52. doi:10.1074/jbc.M412816200. PMC 1368959. PMID 15590642.
• Yokosaki Y, Tanaka K, Higashikawa F, Yamashita K, Eboshida A (2005). "Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin". Matrix Biol. 24 (6): 418–27. doi:10.1016/j.matbio.2005.05.005. PMID 16005200.
• Gulubova M, Vlaykova T (2006). "Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases". Acta Histochem. 108 (1): 25–35. doi:10.1016/j.acthis.2005.12.001. PMID 16430945.

External links

• ITGA9 Info with links in the Cell Migration Gateway Archived 2014-12-11 at the Wayback Machine