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{{Infobox_gene}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
'''Activin receptor type-2A''' is a [[protein]] that in humans is encoded by the ''ACVR2A'' [[gene]].<ref name="pmid1314589">{{cite journal | vauthors = Donaldson CJ, Mathews LS, Vale WW | title = Molecular cloning and binding properties of the human type II activin receptor | journal = Biochem. Biophys. Res. Commun. | volume = 184 | issue = 1 | pages = 310–6 | date = May 1992 | pmid = 1314589 | pmc =  | doi = 10.1016/0006-291X(92)91194-U }}</ref><ref name="pmid10702675">{{cite journal | vauthors = Bondestam J, Horelli-Kuitunen N, Hildén K, Ritvos O, Aaltonen J | title = Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH | journal = Cytogenet. Cell Genet. | volume = 87 | issue = 3-4 | pages = 219–20 | date = April 2000 | pmid = 10702675 | pmc =  | doi = 10.1159/000015429 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACVR2A activin A receptor, type IIA| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92| accessdate = }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_ACVR2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bte.
| PDB = {{PDB2|1bte}}, {{PDB2|1lx5}}, {{PDB2|2goo}}
| Name = Activin A receptor, type IIA
| HGNCid = 173
| Symbol = ACVR2A
| AltSymbols =; ACTRII; ACVR2
| OMIM = 102581
| ECnumber = 
| Homologene = 20391
| MGIid = 102806
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0017002 |text = activin receptor activity}} {{GNF_GO|id=GO:0019838 |text = growth factor binding}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0048186 |text = inhibin beta-A binding}}
  | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
  | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007178 |text = transmembrane receptor protein serine/threonine kinase signaling pathway}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0009952 |text = anterior/posterior pattern formation}} {{GNF_GO|id=GO:0045648 |text = positive regulation of erythrocyte differentiation}} {{GNF_GO|id=GO:0048276 |text = gastrulation (sensu Vertebrata)}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 92
    | Hs_Ensembl = ENSG00000121989
    | Hs_RefseqProtein = NP_001607
    | Hs_RefseqmRNA = NM_001616
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 148319067
    | Hs_GenLoc_end = 148404863
    | Hs_Uniprot = P27037
    | Mm_EntrezGene = 11480
    | Mm_Ensembl = ENSMUSG00000052155
    | Mm_RefseqmRNA = NM_007396
    | Mm_RefseqProtein = NP_031422
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 48636166
    | Mm_GenLoc_end = 48724172
    | Mm_Uniprot = Q8BRV4
  }}
}}
{{Protbox
  |Name = Activin receptor type-2A
  |Domains=  [[TS domain]], [[S/T domain]]
  |Taxa = ''[[Homo sapiens]]''; homologs: many [[metazoan]] [[phylum (biology)|phyla]]
  |Cofactors=[[Magnesium]] or [[manganese]]
}}
'''Activin A receptor, type IIA''', also known as '''ACVR2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACVR2A activin A receptor, type IIA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92| accessdate = }}</ref>
ACVR2A is an [[activin type 2 receptor]].
ACVR2A is an [[activin type 2 receptor]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 
{{PBB_Summary
== Function ==
| section_title =
 
| summary_text = This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.<ref name="entrez">{{cite web | title = Entrez Gene: ACVR2A activin A receptor, type IIA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=92| accessdate = }}</ref>
This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the [[transforming growth factor-beta]] (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of [[receptor protein serine/threonine kinase|receptor serine kinases]] which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with [[cysteine]]-rich region, a [[transmembrane domain]], and a [[cytoplasmic]] domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in [[phosphorylation]] of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.<ref name="entrez"/>
}}
 
==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ACVR2A has been shown to [[Protein-protein interaction|interact]] with:
* [[ACVR1B]],<ref name = pmid9892009>{{cite journal | vauthors = Lebrun JJ, Takabe K, Chen Y, Vale W | title = Roles of pathway-specific and inhibitory Smads in activin receptor signaling | journal = Mol. Endocrinol. | volume = 13 | issue = 1 | pages = 15–23  | date = January 1999 | pmid = 9892009 | doi = 10.1210/mend.13.1.0218 }}</ref><ref name = pmid8612709>{{cite journal | vauthors = De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ | title = Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors | journal = Exp. Cell Res. | volume = 224 | issue = 2 | pages = 323–34  | date = May 1996 | pmid = 8612709 | doi = 10.1006/excr.1996.0142 }}</ref>
* [[INHBA]],<ref name = pmid10746731>{{cite journal | vauthors = Lewis KA, Gray PC, Blount AL, MacConell LA, Wiater E, Bilezikjian LM, Vale W | title = Betaglycan binds inhibin and can mediate functional antagonism of activin signalling | journal = Nature | volume = 404 | issue = 6776 | pages = 411–4  | date = March 2000 | pmid = 10746731 | doi = 10.1038/35006129 }}</ref><ref name = pmid9202237>{{cite journal | vauthors = Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH | title = Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells | journal = Endocrinology | volume = 138 | issue = 7 | pages = 2928–36  | date = July 1997 | pmid = 9202237 | doi = 10.1210/endo.138.7.5250 }}</ref>  and
* [[SYNJ2BP]].<ref name = pmid15451561>{{cite journal | vauthors = Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H | title = Novel factors in regulation of activin signaling | journal = Mol. Cell. Endocrinol. | volume = 225 | issue = 1-2 | pages = 1–8  | date = October 2004 | pmid = 15451561 | doi = 10.1016/j.mce.2004.02.006 }}</ref><ref name = pmid11882656>{{cite journal | vauthors = Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H | title = Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway | journal = J. Biol. Chem. | volume = 277 | issue = 21 | pages = 19008–18  | date = May 2002 | pmid = 11882656 | doi = 10.1074/jbc.M112472200 }}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ACVR2A}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Welt CK | title = The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction | journal = Curr. Opin. Obstet. Gynecol. | volume = 14 | issue = 3 | pages = 317–23 | year = 2002 | pmid = 12032389 | doi = 10.1097/00001703-200206000-00012 }}
| citations =
* {{cite journal | vauthors = Matzuk MM, Bradley A | title = Cloning of the human activin receptor cDNA reveals high evolutionary conservation | journal = Biochim. Biophys. Acta | volume = 1130 | issue = 1 | pages = 105–8 | year = 1992 | pmid = 1311955 | doi = 10.1016/0167-4781(92)90472-C }}
*{{cite journal | author=Welt CK |title=The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction. |journal=Curr. Opin. Obstet. Gynecol. |volume=14 |issue= 3 |pages= 317-23 |year= 2002 |pmid= 12032389 |doi= }}
* {{cite journal | vauthors = Mathews LS, Vale WW | title = Expression cloning of an activin receptor, a predicted transmembrane serine kinase | journal = Cell | volume = 65 | issue = 6 | pages = 973–82 | year = 1991 | pmid = 1646080 | doi = 10.1016/0092-8674(91)90549-E }}
*{{cite journal | author=Matzuk MM, Bradley A |title=Cloning of the human activin receptor cDNA reveals high evolutionary conservation. |journal=Biochim. Biophys. Acta |volume=1130 |issue= 1 |pages= 105-8 |year= 1992 |pmid= 1311955 |doi= }}
* {{cite journal | vauthors = Xu J, McKeehan K, Matsuzaki K, McKeehan WL | title = Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism | journal = J. Biol. Chem. | volume = 270 | issue = 11 | pages = 6308–13 | year = 1995 | pmid = 7890768 | doi = 10.1074/jbc.270.11.6308 }}
*{{cite journal | author=Donaldson CJ, Mathews LS, Vale WW |title=Molecular cloning and binding properties of the human type II activin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 1 |pages= 310-6 |year= 1992 |pmid= 1314589 |doi= }}
* {{cite journal | vauthors = Attisano L, Cárcamo J, Ventura F, Weis FM, Massagué J, Wrana JL | title = Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors | journal = Cell | volume = 75 | issue = 4 | pages = 671–80 | year = 1993 | pmid = 8242742 | doi = 10.1016/0092-8674(93)90488-C }}
*{{cite journal | author=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase. |journal=Cell |volume=65 |issue= 6 |pages= 973-82 |year= 1991 |pmid= 1646080 |doi= }}
* {{cite journal | vauthors = Peng C, Huang TH, Jeung EB, Donaldson CJ, Vale WW, Leung PC | title = Expression of the type II activin receptor gene in the human placenta | journal = Endocrinology | volume = 133 | issue = 6 | pages = 3046–9 | year = 1993 | pmid = 8243335 | doi = 10.1210/en.133.6.3046 }}
*{{cite journal | author=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308-13 |year= 1995 |pmid= 7890768 |doi= }}
* {{cite journal | vauthors = De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ | title = Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors | journal = Exp. Cell Res. | volume = 224 | issue = 2 | pages = 323–34 | year = 1996 | pmid = 8612709 | doi = 10.1006/excr.1996.0142 }}
*{{cite journal | author=Attisano L, Cárcamo J, Ventura F, ''et al.'' |title=Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors. |journal=Cell |volume=75 |issue= 4 |pages= 671-80 |year= 1993 |pmid= 8242742 |doi= }}
* {{cite journal | vauthors = Attisano L, Wrana JL, Montalvo E, Massagué J | title = Activation of signalling by the activin receptor complex | journal = Mol. Cell. Biol. | volume = 16 | issue = 3 | pages = 1066–73 | year = 1996 | pmid = 8622651 | pmc = 231089 | doi =  }}
*{{cite journal | author=Peng C, Huang TH, Jeung EB, ''et al.'' |title=Expression of the type II activin receptor gene in the human placenta. |journal=Endocrinology |volume=133 |issue= 6 |pages= 3046-9 |year= 1994 |pmid= 8243335 |doi= }}
* {{cite journal | vauthors = Liu QY, Niranjan B, Gomes P, Gomm JJ, Davies D, Coombes RC, Buluwela L | title = Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells | journal = Cancer Res. | volume = 56 | issue = 5 | pages = 1155–63 | year = 1996 | pmid = 8640777 | doi =  }}
*{{cite journal | author=De Winter JP, De Vries CJ, Van Achterberg TA, ''et al.'' |title=Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors. |journal=Exp. Cell Res. |volume=224 |issue= 2 |pages= 323-34 |year= 1996 |pmid= 8612709 |doi=  }}
* {{cite journal | vauthors = Nishitoh H, Ichijo H, Kimura M, Matsumoto T, Makishima F, Yamaguchi A, Yamashita H, Enomoto S, Miyazono K | title = Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5 | journal = J. Biol. Chem. | volume = 271 | issue = 35 | pages = 21345–52 | year = 1996 | pmid = 8702914 | doi = 10.1074/jbc.271.35.21345 }}
*{{cite journal | author=Attisano L, Wrana JL, Montalvo E, Massagué J |title=Activation of signalling by the activin receptor complex. |journal=Mol. Cell. Biol. |volume=16 |issue= 3 |pages= 1066-73 |year= 1996 |pmid= 8622651 |doi=  }}
* {{cite journal | vauthors = Lebrun JJ, Vale WW | title = Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation | journal = Mol. Cell. Biol. | volume = 17 | issue = 3 | pages = 1682–91 | year = 1997 | pmid = 9032295 | pmc = 231893 | doi =  }}
*{{cite journal | author=Liu QY, Niranjan B, Gomes P, ''et al.'' |title=Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells. |journal=Cancer Res. |volume=56 |issue= 5 |pages= 1155-63 |year= 1996 |pmid= 8640777 |doi= }}
* {{cite journal | vauthors = Macías-Silva M, Hoodless PA, Tang SJ, Buchwald M, Wrana JL | title = Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2 | journal = J. Biol. Chem. | volume = 273 | issue = 40 | pages = 25628–36 | year = 1998 | pmid = 9748228 | doi = 10.1074/jbc.273.40.25628 }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi=  }}
* {{cite journal | vauthors = Barbara NP, Wrana JL, Letarte M | title = Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily | journal = J. Biol. Chem. | volume = 274 | issue = 2 | pages = 584–94 | year = 1999 | pmid = 9872992 | doi = 10.1074/jbc.274.2.584 }}
*{{cite journal | author=Lebrun JJ, Vale WW |title=Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation. |journal=Mol. Cell. Biol. |volume=17 |issue= 3 |pages= 1682-91 |year= 1997 |pmid= 9032295 |doi= }}
* {{cite journal | vauthors = Lux A, Attisano L, Marchuk DA | title = Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1 | journal = J. Biol. Chem. | volume = 274 | issue = 15 | pages = 9984–92 | year = 1999 | pmid = 10187774 | doi = 10.1074/jbc.274.15.9984 }}
*{{cite journal | author=Macías-Silva M, Hoodless PA, Tang SJ, ''et al.'' |title=Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25628-36 |year= 1998 |pmid= 9748228 |doi= }}
* {{cite journal | vauthors = D'Abronzo FH, Swearingen B, Klibanski A, Alexander JM | title = Mutational analysis of activin/transforming growth factor-beta type I and type II receptor kinases in human pituitary tumors | journal = J. Clin. Endocrinol. Metab. | volume = 84 | issue = 5 | pages = 1716–21 | year = 1999 | pmid = 10323406 | doi = 10.1210/jc.84.5.1716 }}
*{{cite journal | author=Barbara NP, Wrana JL, Letarte M |title=Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 584-94 |year= 1999 |pmid= 9872992 |doi= }}
* {{cite journal | vauthors = Ebisawa T, Tada K, Kitajima I, Tojo K, Sampath TK, Kawabata M, Miyazono K, Imamura T | title = Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation | journal = J. Cell Sci. | volume = 112 | issue = 20 | pages = 3519–27 | year = 1999 | pmid = 10504300 | doi =  }}
*{{cite journal | author=Lux A, Attisano L, Marchuk DA |title=Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9984-92 |year= 1999 |pmid= 10187774 |doi= }}
* {{cite journal | vauthors = van Schaik RH, Wierikx CD, Timmerman MA, Oomen MH, van Weerden WM, van der Kwast TH, van Steenbrugge GJ, de Jong FH | title = Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues | journal = Br. J. Cancer | volume = 82 | issue = 1 | pages = 112–7 | year = 2000 | pmid = 10638976 | pmc = 2363208 | doi = 10.1054/bjoc.1999.0886 }}
*{{cite journal | author=D'Abronzo FH, Swearingen B, Klibanski A, Alexander JM |title=Mutational analysis of activin/transforming growth factor-beta type I and type II receptor kinases in human pituitary tumors. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 5 |pages= 1716-21 |year= 1999 |pmid= 10323406 |doi=  }}
* {{cite journal | vauthors = Shoji H, Tsuchida K, Kishi H, Yamakawa N, Matsuzaki T, Liu Z, Nakamura T, Sugino H | title = Identification and characterization of a PDZ protein that interacts with activin type II receptors | journal = J. Biol. Chem. | volume = 275 | issue = 8 | pages = 5485–92 | year = 2000 | pmid = 10681527 | doi = 10.1074/jbc.275.8.5485 }}
*{{cite journal | author=Ebisawa T, Tada K, Kitajima I, ''et al.'' |title=Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue= |pages= 3519-27 |year= 2000 |pmid= 10504300 |doi= }}
*{{cite journal | author=van Schaik RH, Wierikx CD, Timmerman MA, ''et al.'' |title=Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues. |journal=Br. J. Cancer |volume=82 |issue= 1 |pages= 112-7 |year= 2000 |pmid= 10638976 |doi= 10.1054/bjoc.1999.0886 }}
*{{cite journal  | author=Shoji H, Tsuchida K, Kishi H, ''et al.'' |title=Identification and characterization of a PDZ protein that interacts with activin type II receptors. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5485-92 |year= 2000 |pmid= 10681527 |doi=  }}
*{{cite journal  | author=Bondestam J, Horelli-Kuitunen N, Hildén K, ''et al.'' |title=Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 219-20 |year= 2000 |pmid= 10702675 |doi=  }}
}}
{{refend}}
{{refend}}


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Latest revision as of 19:15, 8 November 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
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View/Edit Human

Activin receptor type-2A is a protein that in humans is encoded by the ACVR2A gene.[1][2][3] ACVR2A is an activin type 2 receptor.

Function

This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.[3]

Interactions

ACVR2A has been shown to interact with:

References

  1. ↑ Donaldson CJ, Mathews LS, Vale WW (May 1992). "Molecular cloning and binding properties of the human type II activin receptor". Biochem. Biophys. Res. Commun. 184 (1): 310–6. doi:10.1016/0006-291X(92)91194-U. PMID 1314589.
  2. ↑ Bondestam J, Horelli-Kuitunen N, Hildén K, Ritvos O, Aaltonen J (April 2000). "Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH". Cytogenet. Cell Genet. 87 (3–4): 219–20. doi:10.1159/000015429. PMID 10702675.
  3. ↑ 3.0 3.1 "Entrez Gene: ACVR2A activin A receptor, type IIA".
  4. ↑ Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor signaling". Mol. Endocrinol. 13 (1): 15–23. doi:10.1210/mend.13.1.0218. PMID 9892009.
  5. ↑ De Winter JP, De Vries CJ, Van Achterberg TA, Ameerun RF, Feijen A, Sugino H, De Waele P, Huylebroeck D, Verschueren K, Van Den Eijden-Van Raaij AJ (May 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors". Exp. Cell Res. 224 (2): 323–34. doi:10.1006/excr.1996.0142. PMID 8612709.
  6. ↑ Lewis KA, Gray PC, Blount AL, MacConell LA, Wiater E, Bilezikjian LM, Vale W (March 2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. 404 (6776): 411–4. doi:10.1038/35006129. PMID 10746731.
  7. ↑ Martens JW, de Winter JP, Timmerman MA, McLuskey A, van Schaik RH, Themmen AP, de Jong FH (July 1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". Endocrinology. 138 (7): 2928–36. doi:10.1210/endo.138.7.5250. PMID 9202237.
  8. ↑ Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H (October 2004). "Novel factors in regulation of activin signaling". Mol. Cell. Endocrinol. 225 (1–2): 1–8. doi:10.1016/j.mce.2004.02.006. PMID 15451561.
  9. ↑ Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (May 2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". J. Biol. Chem. 277 (21): 19008–18. doi:10.1074/jbc.M112472200. PMID 11882656.

External links

Further reading

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