CD49d: Difference between revisions

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{{Infobox_gene}}
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'''CD49d''' is an [[integrin]] alpha subunit. It makes up half of the α4β1 lymphocyte homing receptor.
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== Function ==
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The product of this gene belongs to the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an alpha 4 chain. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. Alpha 4 chain associates with either beta 1 chain or beta 7 chain.<ref>{{cite web | title = Entrez Gene: ITGA4 integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3676| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
CD49d has been shown to [[Protein-protein interaction|interact]] with [[LGALS8]]<ref name="pmid10852818">{{cite journal | vauthors = Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y | title = Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis | journal = J. Cell Sci. | volume = 113 | issue = Pt 13 | pages = 2385–97 | year = 2000 | pmid = 10852818 | doi =  }}</ref> and [[Paxillin]].<ref name=pmid11533025>{{cite journal | vauthors = Han J, Liu S, Rose DM, Schlaepfer DD, McDonald H, Ginsberg MH | title = Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding | language =  | journal = J. Biol. Chem. | volume = 276 | issue = 44 | pages = 40903–9 | date = November 2001 | pmid = 11533025 | doi = 10.1074/jbc.M102665200 }}</ref><ref name=pmid11919182>{{cite journal | vauthors = Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH | title = A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration | language =  | journal = J. Biol. Chem. | volume = 277 | issue = 23 | pages = 20887–94 | date = June 2002 | pmid = 11919182 | doi = 10.1074/jbc.M110928200 }}</ref>
| image =
| image_source = 
| PDB =
| Name = Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)
| HGNCid = 6140
| Symbol = ITGA4
| AltSymbols =; CD49D; IA4; MGC90518
| OMIM = 192975
| ECnumber =
| Homologene = 37364
| MGIid = 96603
| GeneAtlas_image1 = PBB_GE_ITGA4_213416_at_tn.png
  | GeneAtlas_image2 = PBB_GE_ITGA4_205884_at_tn.png
| GeneAtlas_image3 = PBB_GE_ITGA4_205885_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:0042802 |text = identical 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:0001974 |text = blood vessel remodeling}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3676
    | Hs_Ensembl = ENSG00000115232
    | Hs_RefseqProtein = NP_000876
    | Hs_RefseqmRNA = NM_000885
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 182029864
    | Hs_GenLoc_end = 182110711
    | Hs_Uniprot = P13612
    | Mm_EntrezGene = 16401
    | Mm_Ensembl = ENSMUSG00000027009
    | Mm_RefseqmRNA = NM_010576
    | Mm_RefseqProtein = NP_034706
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 79056339
    | Mm_GenLoc_end = 79133962
    | Mm_Uniprot = Q78E20
  }}
}}
'''CD49d''' is an [[integrin]] alpha subunit. It makes up half of the α4β1 lymphocyte homing receptor.


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = The product of this gene belongs to the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an alpha 4 chain. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. Alpha 4 chain associates with either beta 1 chain or beta 7 chain.<ref>{{cite web | title = Entrez Gene: ITGA4 integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3676| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Humphries MJ, Sheridan J, Mould AP, Newham P | title = Mechanisms of VCAM-1 and fibronectin binding to integrin alpha 4 beta 1: implications for integrin function and rational drug design. | journal = Ciba Found. Symp. | volume = 189 | issue =  | pages = 177–91; discussion 191–9 | year = 1995 | pmid = 7587632 | doi =  }}
| citations =
* {{cite journal | vauthors = Oostendorp RA, Dörmer P | title = VLA-4-mediated interactions between normal human hematopoietic progenitors and stromal cells. | journal = Leuk. Lymphoma | volume = 24 | issue = 5-6 | pages = 423–35 | year = 1997 | pmid = 9086434 | doi = 10.3109/10428199709055581 }}
*{{cite journal | author=Humphries MJ, Sheridan J, Mould AP, Newham P |title=Mechanisms of VCAM-1 and fibronectin binding to integrin alpha 4 beta 1: implications for integrin function and rational drug design. |journal=Ciba Found. Symp. |volume=189 |issue=  |pages= 177-91; discussion 191-9 |year= 1995 |pmid= 7587632 |doi=  }}
* {{cite journal | vauthors = Porter JC, Hogg N | title = Integrins take partners: cross-talk between integrins and other membrane receptors. | journal = Trends Cell Biol. | volume = 8 | issue = 10 | pages = 390–6 | year = 1999 | pmid = 9789327 | doi = 10.1016/S0962-8924(98)01344-0 }}
*{{cite journal | author=Oostendorp RA, Dörmer P |title=VLA-4-mediated interactions between normal human hematopoietic progenitors and stromal cells. |journal=Leuk. Lymphoma |volume=24 |issue= 5-6 |pages= 423-35 |year= 1997 |pmid= 9086434 |doi= }}
* {{cite journal | vauthors = Rose DM, Han J, Ginsberg MH | title = Alpha4 integrins and the immune response. | journal = Immunol. Rev. | volume = 186 | issue = 1 | pages = 118–24 | year = 2003 | pmid = 12234367 | doi = 10.1034/j.1600-065X.2002.18611.x }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
* {{cite journal | vauthors = O'Connor P | title = Natalizumab and the role of alpha 4-integrin antagonism in the treatment of multiple sclerosis. | journal = Expert opinion on biological therapy | volume = 7 | issue = 1 | pages = 123–36 | year = 2007 | pmid = 17150024 | doi = 10.1517/14712598.7.1.123 }}
*{{cite journal | author=Rose DM, Han J, Ginsberg MH |title=Alpha4 integrins and the immune response. |journal=Immunol. Rev. |volume=186 |issue= |pages= 118-24 |year= 2003 |pmid= 12234367 |doi= }}
* {{cite journal | vauthors = Chan BM, Elices MJ, Murphy E, Hemler ME | title = Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of alpha 4 beta 1 (VLA-4) and alpha 4 beta 7 on the human B cell line JY. | journal = J. Biol. Chem. | volume = 267 | issue = 12 | pages = 8366–70 | year = 1992 | pmid = 1373725 | doi =  }}
*{{cite journal | author=O'Connor P |title=Natalizumab and the role of alpha 4-integrin antagonism in the treatment of multiple sclerosis. |journal=Expert opinion on biological therapy |volume=7 |issue= 1 |pages= 123-36 |year= 2007 |pmid= 17150024 |doi= 10.1517/14712598.7.1.123 }}
* {{cite journal | vauthors = Fernández-Ruiz E, Pardo-Manuel de Villena F, Rubio MA, Corbí AL, Rodriguez de Córdoba S, Sánchez-Madrid F | title = Mapping of the human VLA-alpha 4 gene to chromosome 2q31-q32. | journal = Eur. J. Immunol. | volume = 22 | issue = 2 | pages = 587–90 | year = 1992 | pmid = 1537388 | doi = 10.1002/eji.1830220243 }}
*{{cite journal | author=Chan BM, Elices MJ, Murphy E, Hemler ME |title=Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of alpha 4 beta 1 (VLA-4) and alpha 4 beta 7 on the human B cell line JY. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8366-70 |year= 1992 |pmid= 1373725 |doi=  }}
* {{cite journal | vauthors = Rubio M, Nueda A, Vara A, Corbí Lopez AL | title = A single mRNA encodes the alpha 150 and alpha 80/70 forms of the alpha subunit of VLA4. | journal = Eur. J. Immunol. | volume = 22 | issue = 4 | pages = 1099–102 | year = 1992 | pmid = 1551405 | doi = 10.1002/eji.1830220434 }}
*{{cite journal | author=Fernández-Ruiz E, Pardo-Manuel de Villena F, Rubio MA, ''et al.'' |title=Mapping of the human VLA-alpha 4 gene to chromosome 2q31-q32. |journal=Eur. J. Immunol. |volume=22 |issue= 2 |pages= 587-90 |year= 1992 |pmid= 1537388 |doi= }}
* {{cite journal | vauthors = Sonnenberg A, Linders CJ, Modderman PW, Damsky CH, Aumailley M, Timpl R | title = Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8. | journal = J. Cell Biol. | volume = 110 | issue = 6 | pages = 2145–55 | year = 1990 | pmid = 1693624 | pmc = 2116116 | doi = 10.1083/jcb.110.6.2145 }}
*{{cite journal | author=Rubio M, Nueda A, Vara A, Corbí Lopez AL |title=A single mRNA encodes the alpha 150 and alpha 80/70 forms of the alpha subunit of VLA4. |journal=Eur. J. Immunol. |volume=22 |issue= 4 |pages= 1099-102 |year= 1992 |pmid= 1551405 |doi= }}
* {{cite journal | vauthors = Teixidó J, Parker CM, Kassner PD, Hemler ME | title = Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage. | journal = J. Biol. Chem. | volume = 267 | issue = 3 | pages = 1786–91 | year = 1992 | pmid = 1730718 | doi =  }}
*{{cite journal | author=Sonnenberg A, Linders CJ, Modderman PW, ''et al.'' |title=Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8. |journal=J. Cell Biol. |volume=110 |issue= 6 |pages= 2145-55 |year= 1990 |pmid= 1693624 |doi= }}
* {{cite journal | vauthors = Rosemblatt M, Vuillet-Gaugler MH, Leroy C, Coulombel L | title = Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells. | journal = J. Clin. Invest. | volume = 87 | issue = 1 | pages = 6–11 | year = 1991 | pmid = 1824634 | pmc = 294977 | doi = 10.1172/JCI115002 }}
*{{cite journal | author=Teixidó J, Parker CM, Kassner PD, Hemler ME |title=Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage. |journal=J. Biol. Chem. |volume=267 |issue= 3 |pages= 1786-91 |year= 1992 |pmid= 1730718 |doi=  }}
* {{cite journal | vauthors = Rosen GD, Birkenmeier TM, Dean DC | title = Characterization of the alpha 4 integrin gene promoter. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 10 | pages = 4094–8 | year = 1991 | pmid = 2034655 | pmc = 51604 | doi = 10.1073/pnas.88.10.4094 }}
*{{cite journal | author=Rosemblatt M, Vuillet-Gaugler MH, Leroy C, Coulombel L |title=Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 6-11 |year= 1991 |pmid= 1824634 |doi= }}
* {{cite journal | vauthors = Takada Y, Elices MJ, Crouse C, Hemler ME | title = The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function. | journal = EMBO J. | volume = 8 | issue = 5 | pages = 1361–8 | year = 1989 | pmid = 2788572 | pmc = 400962 | doi =  }}
*{{cite journal | author=Rosen GD, Birkenmeier TM, Dean DC |title=Characterization of the alpha 4 integrin gene promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 10 |pages= 4094-8 |year= 1991 |pmid= 2034655 |doi= }}
* {{cite journal | vauthors = Takada Y, Strominger JL, Hemler ME | title = The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 84 | issue = 10 | pages = 3239–43 | year = 1987 | pmid = 3033641 | pmc = 304844 | doi = 10.1073/pnas.84.10.3239 }}
*{{cite journal | author=Takada Y, Elices MJ, Crouse C, Hemler ME |title=The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function. |journal=EMBO J. |volume=8 |issue= 5 |pages= 1361-8 |year= 1989 |pmid= 2788572 |doi=  }}
* {{cite journal | vauthors = Hemler ME, Huang C, Schwarz L | title = The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. | journal = J. Biol. Chem. | volume = 262 | issue = 7 | pages = 3300–9 | year = 1987 | pmid = 3546305 | doi =  }}
*{{cite journal | author=Takada Y, Strominger JL, Hemler ME |title=The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3239-43 |year= 1987 |pmid= 3033641 |doi= }}
* {{cite journal | vauthors = Gailit J, Pierschbacher M, Clark RA | title = Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts. | journal = J. Invest. Dermatol. | volume = 100 | issue = 3 | pages = 323–8 | year = 1993 | pmid = 8440915 | doi = 10.1111/1523-1747.ep12470011 }}
*{{cite journal | author=Hemler ME, Huang C, Schwarz L |title=The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3300-9 |year= 1987 |pmid= 3546305 |doi=  }}
* {{cite journal | vauthors = Pujades C, Teixidó J, Bazzoni G, Hemler ME | title = Integrin alpha 4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to alpha 4/180 formation. | journal = Biochem. J. | volume = ( Pt 3) | issue =  | pages = 899–908 | year = 1996 | pmid = 8611173 | pmc = 1216996 | doi =  | series = 313 }}
*{{cite journal | author=Gailit J, Pierschbacher M, Clark RA |title=Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts. |journal=J. Invest. Dermatol. |volume=100 |issue= 3 |pages= 323-8 |year= 1993 |pmid= 8440915 |doi= }}
* {{cite journal | vauthors = Szabo M, McIntyre BW | title = Identification of two variants of the human integrin alpha 4 subunit. | journal = Mol. Immunol. | volume = 32 | issue = 17-18 | pages = 1453–4 | year = 1996 | pmid = 8643114 | doi = 10.1016/0161-5890(96)00001-6 }}
*{{cite journal | author=Pujades C, Teixidó J, Bazzoni G, Hemler ME |title=Integrin alpha 4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to alpha 4/180 formation. |journal=Biochem. J. |volume=313 ( Pt 3) |issue=  |pages= 899-908 |year= 1996 |pmid= 8611173 |doi=  }}
* {{cite journal | vauthors = Mannion BA, Berditchevski F, Kraeft SK, Chen LB, Hemler ME | title = Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). | journal = J. Immunol. | volume = 157 | issue = 5 | pages = 2039–47 | year = 1996 | pmid = 8757325 | doi =  }}
*{{cite journal | author=Szabo M, McIntyre BW |title=Identification of two variants of the human integrin alpha 4 subunit. |journal=Mol. Immunol. |volume=32 |issue= 17-18 |pages= 1453-4 |year= 1996 |pmid= 8643114 |doi= }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi=  }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|CD49d+antigen}}
* {{MeshName|CD49d+antigen}}
*[http://cmkb.cellmigration.org/report.cgi?report=orth_overview&gene_id=3676 ITGA4] Info with links in the [http://www.cellmigration.org/index.shtml Cell Migration Gateway]
* {{UCSC gene info|ITGA4}}


{{immunology-stub}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Integrins}}
[[Category:Integrins]]
[[Category:Clusters of differentiation]]


[[ca:CD49d]]
{{immunology-stub}}
{{WikiDoc Sources}}

Latest revision as of 19:29, 8 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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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

CD49d is an integrin alpha subunit. It makes up half of the α4β1 lymphocyte homing receptor.

Function

The product of this gene belongs to the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an alpha 4 chain. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. Alpha 4 chain associates with either beta 1 chain or beta 7 chain.[1]

Interactions

CD49d has been shown to interact with LGALS8[2] and Paxillin.[3][4]

References

  1. ↑ "Entrez Gene: ITGA4 integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)".
  2. ↑ Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". J. Cell Sci. 113 (Pt 13): 2385–97. PMID 10852818.
  3. ↑ Han J, Liu S, Rose DM, Schlaepfer DD, McDonald H, Ginsberg MH (November 2001). "Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates paxillin binding". J. Biol. Chem. 276 (44): 40903–9. doi:10.1074/jbc.M102665200. PMID 11533025.
  4. ↑ Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH (June 2002). "A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration". J. Biol. Chem. 277 (23): 20887–94. doi:10.1074/jbc.M110928200. PMID 11919182.

Further reading

External links


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