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   24-JAN-2024, entry version 159.
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   GlyCosmos; Q8K592; 2 sites, No reported glycans.
DR   GlyGen; Q8K592; 2 sites.
DR   iPTMnet; Q8K592; -.
DR   PhosphoSitePlus; Q8K592; -.
DR   SwissPalm; Q8K592; -.
DR   PaxDb; 10090-ENSMUSP00000023809; -.
DR   ProteomicsDB; 296402; -.
DR   Antibodypedia; 27053; 385 antibodies from 33 providers.
DR   DNASU; 110542; -.
DR   Ensembl; ENSMUST00000023809.11; ENSMUSP00000023809.5; ENSMUSG00000023047.12.
DR   GeneID; 110542; -.
DR   KEGG; mmu:110542; -.
DR   UCSC; uc007xvq.2; mouse.
DR   AGR; MGI:105062; -.
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; RCPDLWP; -.
DR   OrthoDB; 3900892at2759; -.
DR   PhylomeDB; Q8K592; -.
DR   TreeFam; TF314724; -.
DR   Reactome; R-MMU-201451; Signaling by BMP.
DR   BioGRID-ORCS; 110542; 2 hits in 79 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 109 other cell types or tissues.
DR   ExpressionAtlas; Q8K592; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; 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:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR   GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; ISO:MGI.
DR   GO; GO:1990262; P:anti-Mullerian hormone signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015771; Anti-muellerian_hrmn_rcpt_II.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF49; ANTI-MUELLERIAN HORMONE TYPE-2 RECEPTOR; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF037392; AMHRII; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; Q8K592; MM.
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
//