AMHR2_MOUSE
ID AMHR2_MOUSE Reviewed; 568 AA.
AC Q8K592; Q0VDQ4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Anti-Muellerian hormone type-2 receptor;
DE EC=2.7.11.30;
DE AltName: Full=Anti-Muellerian hormone type II receptor;
DE Short=AMH type II receptor;
DE AltName: Full=MIS type II receptor;
DE Short=MISRII;
DE Short=MRII;
DE Flags: Precursor;
GN Name=Amhr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9299437; DOI=10.1006/bbrc.1997.7224;
RA Mishina Y., Tizard R., Deng J.M., Pathak B.G., Copeland N.G., Jenkins N.A.,
RA Cate R.L., Behringer R.R.;
RT "Sequence, genomic organization, and chromosomal location of the mouse
RT Muellerian-inhibiting substance type II receptor gene.";
RL Biochem. Biophys. Res. Commun. 237:741-746(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Receptor for anti-Muellerian hormone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with type I receptor ACVR1.
CC {ECO:0000250|UniProtKB:Q16671}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; AF503863; AAM28608.1; -; mRNA.
DR EMBL; BC119571; AAI19572.1; -; mRNA.
DR CCDS; CCDS27882.1; -.
DR PIR; JC5629; JC5629.
DR RefSeq; NP_653130.2; NM_144547.2.
DR RefSeq; XP_006520356.1; XM_006520293.2.
DR AlphaFoldDB; Q8K592; -.
DR SMR; Q8K592; -.
DR IntAct; Q8K592; 1.
DR STRING; 10090.ENSMUSP00000023809; -.
DR GlyGen; Q8K592; 2 sites.
DR iPTMnet; Q8K592; -.
DR PhosphoSitePlus; Q8K592; -.
DR PaxDb; Q8K592; -.
DR PRIDE; Q8K592; -.
DR ProteomicsDB; 296402; -.
DR Antibodypedia; 27053; 302 antibodies from 32 providers.
DR DNASU; 110542; -.
DR Ensembl; ENSMUST00000023809; ENSMUSP00000023809; ENSMUSG00000023047.
DR GeneID; 110542; -.
DR KEGG; mmu:110542; -.
DR UCSC; uc007xvq.2; mouse.
DR CTD; 269; -.
DR MGI; MGI:105062; Amhr2.
DR VEuPathDB; HostDB:ENSMUSG00000023047; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000160885; -.
DR HOGENOM; CLU_000288_8_4_1; -.
DR InParanoid; Q8K592; -.
DR OMA; LTQPPTW; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q8K592; -.
DR TreeFam; TF314724; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 110542; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Amhr2; mouse.
DR PRO; PR:Q8K592; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8K592; protein.
DR Bgee; ENSMUSG00000023047; Expressed in seminiferous tubule of testis and 107 other tissues.
DR ExpressionAtlas; Q8K592; baseline and differential.
DR Genevisible; Q8K592; MM.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:1990272; F:anti-Mullerian hormone receptor activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042562; F:hormone binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; TAS:MGI.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; ISO:MGI.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1990262; P:anti-Mullerian hormone signaling pathway; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR015771; Anti-muellerian_hrmn_rcpt_II.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037392; AMHRII; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..568
FT /note="Anti-Muellerian hormone type-2 receptor"
FT /id="PRO_0000260265"
FT TOPO_DOM 16..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 199..504
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 205..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..79
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT DISULFID 92..109
FT /evidence="ECO:0000250|UniProtKB:P37023"
FT CONFLICT 240
FT /note="R -> G (in Ref. 1; AAM28608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 61195 MW; AE89AA1727600E5E CRC64;
MLGTLGLWTL LPAAAQVSPN RRTCVFFEAP GVRGSTKTLG EMVDAGPGPP KGIRCLYSHC
CFGIWNLTHG RAQVEMQGCR DSDEPGCESL HCDPVPRAHP NPSSTLFTCS CGTDFCNANY
SHLPPSGNQG APGPQEPQAT PGGPVWMALL LLGMFLVLLL SSIILALLQR KACRVQGGSD
PEPGSGGDCS EELPELAELR FSQVIQEGGH AVVWAGRLQG EMVAIKAFPP RAVAQFRAER
AVYQLLGLQH DHIVRFITAG QGGPGPLPSG PLLVLELYPK GSLCHYLTQY TSDWGSSLRM
ALSLAEGLAF LHEERWQDGQ YKPGIAHRDL SSQNVLIRED RSCAIGDLGL ALVLPGLAQP
PALAPTQPRG PAAILEAGTQ RYMAPELLDK TLDLQDWGTA LQRADVYSLA LLLWEILSRC
SDLRPDHRPP PFQLAYEAEL GSNPSACELW ALAVEERKRP NIPSTWSCSA TDPRGLRELL
EDCWDADPEA RLTAECVQQR LAALAYPHGA SSFPESPQGC PENCLSAPAS AVFPCRPQQS
SCLLSVQQGP GSRSPDPVGD TVQVYVNE
