ITGA9: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Integrin alpha-9''' is a [[protein]] that in humans is encoded by the ''ITGA9'' [[gene]].<ref name="pmid8245132">{{cite journal |vauthors=Palmer EL, Rüegg C, Ferrando R, Pytela R, Sheppard D | title = Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle | journal = J Cell Biol | volume = 123 | issue = 5 | pages = 1289–97 | date = Jan 1994 | pmid = 8245132 | pmc = 2119880 | doi = 10.1083/jcb.123.5.1289 }}</ref><ref name="pmid8290272">{{cite journal |vauthors=Hibi K, Yamakawa K, Ueda R, Horio Y, Murata Y, Tamari M, Uchida K, Takahashi T, Nakamura Y, Takahashi T | title = Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer | journal = Oncogene | volume = 9 | issue = 2 | pages = 611–9 | date = Feb 1994 | pmid = 8290272 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ITGA9 integrin, alpha 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3680| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Integrin, alpha 9
| HGNCid = 6145
| Symbol = ITGA9
| AltSymbols =; ALPHA-RLC; ITGA4L; RLC
| OMIM = 603963
| ECnumber = 
| Homologene = 1664
| MGIid = 104756
| GeneAtlas_image1 = PBB_GE_ITGA9_gnf1h04097_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3680
    | Hs_Ensembl = ENSG00000144668
    | Hs_RefseqProtein = NP_002198
    | Hs_RefseqmRNA = NM_002207
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 37468817
    | Hs_GenLoc_end = 37836285
    | Hs_Uniprot = Q13797
    | Mm_EntrezGene = 104099
    | Mm_Ensembl = ENSMUSG00000039115
    | Mm_RefseqmRNA = XM_985968
    | Mm_RefseqProtein = XP_991062
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 118455407
    | Mm_GenLoc_end = 118747637
    | Mm_Uniprot = 
  }}
}}
'''Integrin, alpha 9''', also known as '''ITGA9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGA9 integrin, alpha 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3680| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
==Interactions==
| summary_text = 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 VCAM1, cytotactin and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.<ref name="entrez">{{cite web | title = Entrez Gene: ITGA9 integrin, alpha 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3680| accessdate = }}</ref>
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|tenascin-C]], [[ADAM Protein|ADAMs]], EMELIN1, [[osteopontin]], and [[VEGF]].<ref>{{cite journal |vauthors=Høye AM, Couchman JR, Wewer UM, Fukami K, Yoneda A | title = The newcomer in the integrin family: integrin α9 in biology and cancer. | journal = Advances in biological regulation | volume = 52 | issue = 2 | pages = 326–39 | date = May 2012 | pmid = 22781746 | doi = 10.1016/j.jbior.2012.03.004 }}</ref> α9β1 binding is independent of the RGD peptide sequence.
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | author = Evans JP | title = Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. | journal = BioEssays | volume = 23 | issue = 7 | pages = 628–39 | year = 2001 | pmid = 11462216 | doi = 10.1002/bies.1088 }}
| citations =
*{{cite journal |vauthors=Yamakawa K, Takahashi T, Horio Y, Murata Y, Takahashi E, Hibi K, Yokoyama S, Ueda R, Takahashi T, Nakamura Y | title = Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22. | journal = Oncogene | volume = 8 | issue = 2 | pages = 327–30 | year = 1993 | pmid = 8381220 | doi =  }}
*{{cite journal | author=Evans JP |title=Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. |journal=Bioessays |volume=23 |issue= 7 |pages= 628-39 |year= 2001 |pmid= 11462216 |doi= 10.1002/bies.1088 }}
*{{cite journal |vauthors=Yokosaki Y, Monis H, Chen J, Sheppard D | title = Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains. | journal = J. Biol. Chem. | volume = 271 | issue = 39 | pages = 24144–50 | year = 1996 | pmid = 8798654 | doi = 10.1074/jbc.271.39.24144 }}
*{{cite journal | author=Palmer EL, Rüegg C, Ferrando R, ''et al.'' |title=Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle. |journal=J. Cell Biol. |volume=123 |issue= 5 |pages= 1289-97 |year= 1994 |pmid= 8245132 |doi=  }}
*{{cite journal |vauthors=Yokosaki Y, Matsuura N, Sasaki T, Murakami I, Schneider H, Higashiyama S, Saitoh Y, Yamakido M, Taooka Y, Sheppard D | title = The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. | journal = J. Biol. Chem. | volume = 274 | issue = 51 | pages = 36328–34 | year = 2000 | pmid = 10593924 | doi = 10.1074/jbc.274.51.36328 }}
*{{cite journal  | author=Hibi K, Yamakawa K, Ueda R, ''et al.'' |title=Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer. |journal=Oncogene |volume=9 |issue= 2 |pages= 611-9 |year= 1994 |pmid= 8290272 |doi=  }}
*{{cite journal |vauthors=Young BA, Taooka Y, Liu S, Askins KJ, Yokosaki Y, Thomas SM, Sheppard D | title = 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. | journal = Mol. Biol. Cell | volume = 12 | issue = 10 | pages = 3214–25 | year = 2002 | pmid = 11598204 | pmc = 60168 | doi = 10.1091/mbc.12.10.3214 }}
*{{cite journal  | author=Yamakawa K, Takahashi T, Horio Y, ''et al.'' |title=Frequent homozygous deletions in lung cancer cell lines detected by a DNA marker located at 3p21.3-p22. |journal=Oncogene |volume=8 |issue= 2 |pages= 327-30 |year= 1993 |pmid= 8381220 |doi=  }}
*{{cite journal |vauthors=Eto K, Huet C, Tarui T, Kupriyanov S, Liu HZ, Puzon-McLaughlin W, Zhang XP, Sheppard D, Engvall E, Takada Y | title = 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. | journal = J. Biol. Chem. | volume = 277 | issue = 20 | pages = 17804–10 | year = 2002 | pmid = 11882657 | doi = 10.1074/jbc.M200086200 }}
*{{cite journal | author=Yokosaki Y, Monis H, Chen J, Sheppard D |title=Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 24144-50 |year= 1996 |pmid= 8798654 |doi= }}
*{{cite journal |vauthors=Majumdar M, Tarui T, Shi B, Akakura N, Ruf W, Takada Y | title = Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1). | journal = J. Biol. Chem. | volume = 279 | issue = 36 | pages = 37528–34 | year = 2004 | pmid = 15247268 | doi = 10.1074/jbc.M401372200 }}
*{{cite journal | author=Yokosaki Y, Matsuura N, Sasaki T, ''et al.'' |title=The integrin alpha(9)beta(1) binds to a novel recognition sequence (SVVYGLR) in the thrombin-cleaved amino-terminal fragment of osteopontin. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36328-34 |year= 2000 |pmid= 10593924 |doi= }}
*{{cite journal |vauthors=Chen C, Young BA, Coleman CS, Pegg AE, Sheppard D | title = Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration. | journal = J. Cell Biol. | volume = 167 | issue = 1 | pages = 161–70 | year = 2004 | pmid = 15479742 | pmc = 2172529 | doi = 10.1083/jcb.200312166 }}
*{{cite journal | author=Young BA, Taooka Y, Liu S, ''et al.'' |title=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. |journal=Mol. Biol. Cell |volume=12 |issue= 10 |pages= 3214-25 |year= 2002 |pmid= 11598204 |doi= }}
*{{cite journal |vauthors=Vlahakis NE, Young BA, Atakilit A, Sheppard D | title = The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1. | journal = J. Biol. Chem. | volume = 280 | issue = 6 | pages = 4544–52 | year = 2005 | pmid = 15590642 | pmc = 1368959 | doi = 10.1074/jbc.M412816200 }}
*{{cite journal | author=Eto K, Huet C, Tarui T, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17804-10 |year= 2002 |pmid= 11882657 |doi= 10.1074/jbc.M200086200 }}
*{{cite journal |vauthors=Yokosaki Y, Tanaka K, Higashikawa F, Yamashita K, Eboshida A | title = Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin. | journal = Matrix Biol. | volume = 24 | issue = 6 | pages = 418–27 | year = 2005 | pmid = 16005200 | doi = 10.1016/j.matbio.2005.05.005 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal |vauthors=Gulubova M, Vlaykova T | title = Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases. | journal = Acta Histochem. | volume = 108 | issue = 1 | pages = 25–35 | year = 2006 | pmid = 16430945 | doi = 10.1016/j.acthis.2005.12.001 }}
*{{cite journal  | author=Majumdar M, Tarui T, Shi B, ''et al.'' |title=Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin alpha(9)beta(1). |journal=J. Biol. Chem. |volume=279 |issue= 36 |pages= 37528-34 |year= 2004 |pmid= 15247268 |doi= 10.1074/jbc.M401372200 }}
*{{cite journal | author=Chen C, Young BA, Coleman CS, ''et al.'' |title=Spermidine/spermine N1-acetyltransferase specifically binds to the integrin alpha9 subunit cytoplasmic domain and enhances cell migration. |journal=J. Cell Biol. |volume=167 |issue= 1 |pages= 161-70 |year= 2004 |pmid= 15479742 |doi= 10.1083/jcb.200312166 }}
*{{cite journal | author=Vlahakis NE, Young BA, Atakilit A, Sheppard D |title=The lymphangiogenic vascular endothelial growth factors VEGF-C and -D are ligands for the integrin alpha9beta1. |journal=J. Biol. Chem. |volume=280 |issue= 6 |pages= 4544-52 |year= 2005 |pmid= 15590642 |doi= 10.1074/jbc.M412816200 }}
*{{cite journal | author=Yokosaki Y, Tanaka K, Higashikawa F, ''et al.'' |title=Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin. |journal=Matrix Biol. |volume=24 |issue= 6 |pages= 418-27 |year= 2005 |pmid= 16005200 |doi= 10.1016/j.matbio.2005.05.005 }}
*{{cite journal | author=Gulubova M, Vlaykova T |title=Immunohistochemical assessment of fibronectin and tenascin and their integrin receptors alpha5beta1 and alpha9beta1 in gastric and colorectal cancers with lymph node and liver metastases. |journal=Acta Histochem. |volume=108 |issue= 1 |pages= 25-35 |year= 2006 |pmid= 16430945 |doi= 10.1016/j.acthis.2005.12.001 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3680 ITGA9] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
 
{{Integrins}}
 
[[Category:Integrins]]
 
 
{{gene-3-stub}}

Latest revision as of 16:50, 16 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene.[1][2][3]

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.[3]

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.[4] α9β1 binding is independent of the RGD peptide sequence.

References

  1. ↑ Palmer EL, Rüegg C, Ferrando R, Pytela R, Sheppard D (Jan 1994). "Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle". J Cell Biol. 123 (5): 1289–97. doi:10.1083/jcb.123.5.1289. PMC 2119880. PMID 8245132.
  2. ↑ Hibi K, Yamakawa K, Ueda R, Horio Y, Murata Y, Tamari M, Uchida K, Takahashi T, Nakamura Y, Takahashi T (Feb 1994). "Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer". Oncogene. 9 (2): 611–9. PMID 8290272.
  3. ↑ 3.0 3.1 "Entrez Gene: ITGA9 integrin, alpha 9".
  4. ↑ Høye AM, Couchman JR, Wewer UM, Fukami K, Yoneda A (May 2012). "The newcomer in the integrin family: integrin α9 in biology and cancer". Advances in biological regulation. 52 (2): 326–39. doi:10.1016/j.jbior.2012.03.004. PMID 22781746.

Further reading

External links


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