AMHR2_RAT
ID AMHR2_RAT Reviewed; 557 AA.
AC Q62893; Q63045; Q9R0A7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
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=C14;
DE AltName: Full=MIS type II receptor;
DE Short=MISRII;
DE Short=MRII;
DE Flags: Precursor;
GN Name=Amhr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8536608; DOI=10.1210/endo.137.1.8536608;
RA Teixeira J., He W.W., Shah P.C., Morikawa N., Lee M.M., Catlin E.A.,
RA Hudson P.L., Wing J., Maclaughlin D.T., Donahoe P.K.;
RT "Developmental expression of a candidate Muellerian inhibiting substance
RT type II receptor.";
RL Endocrinology 137:160-165(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8119126; DOI=10.1242/dev.120.1.189;
RA Baarends W.M., Van Helmond M.J.L., Post M., Van der Schoot P.J.C.M.,
RA Hoogerbrugge J.W., de Winter J.P., Uilenbroek J.T.J., Karels B.,
RA Wilming L.G., Meijers J.H.C., Themmem A.P.N., Grootegoed A.J.;
RT "A novel member of the transmembrane serine/threonine kinase receptor
RT family is specifically expressed in the gonads and in mesenchymal cells
RT adjacent to the Muellerian duct.";
RL Development 120:189-197(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC STRAIN=Sprague-Dawley;
RX PubMed=10570158; DOI=10.1073/pnas.96.24.13831;
RA Teixeira J., Kehas D.J., Antun R., Donahoe P.K.;
RT "Transcriptional regulation of the rat Muellerian inhibiting substance type
RT II receptor in rodent Leydig cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13831-13838(1999).
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; Single-pass type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed in the mesenchymal cells surrounding the
CC Muellerian duct at embryonic days 14, 15, and 16 and in tubular and
CC follicular structures of the fetal gonads.
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; U42427; AAC52343.1; -; mRNA.
DR EMBL; X71916; CAA50731.1; -; mRNA.
DR EMBL; AF092445; AAC64138.1; -; Genomic_DNA.
DR PIR; S41627; S41627.
DR RefSeq; NP_112260.1; NM_030998.1.
DR AlphaFoldDB; Q62893; -.
DR SMR; Q62893; -.
DR STRING; 10116.ENSRNOP00000020103; -.
DR GlyGen; Q62893; 2 sites.
DR PhosphoSitePlus; Q62893; -.
DR PaxDb; Q62893; -.
DR Ensembl; ENSRNOT00000020103; ENSRNOP00000020103; ENSRNOG00000014850.
DR GeneID; 29530; -.
DR KEGG; rno:29530; -.
DR UCSC; RGD:70964; rat.
DR CTD; 269; -.
DR RGD; 70964; Amhr2.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000160885; -.
DR InParanoid; Q62893; -.
DR OMA; LTQPPTW; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q62893; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 5301.
DR Reactome; R-RNO-201451; Signaling by BMP.
DR PRO; PR:Q62893; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000014850; Expressed in ovary and 15 other tissues.
DR ExpressionAtlas; Q62893; baseline and differential.
DR Genevisible; Q62893; RN.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IDA: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; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:1902613; P:negative regulation of anti-Mullerian hormone signaling pathway; ISO:RGD.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
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; PF01064; Activin_recp; 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 2: Evidence at transcript 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..557
FT /note="Anti-Muellerian hormone type-2 receptor"
FT /id="PRO_0000024409"
FT TOPO_DOM 18..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 201..511
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 228
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 527
FT /note="C -> Y (in Ref. 2; CAA50731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 59749 MW; 8EDEE9C0C32EBDD5 CRC64;
MLGTLGLWTL LPAAAQVSPN RRTCVFFEAP GVRGSTKTLG EVVDAGPGPP KGIRCLYSHC
CFGIWNLTHG RAQVEMQGCL DSDEPGCESL HCDPVPRAHP SPSSTLFTCS CGTDFCNANY
SHLPPSGNRG APGPQEPQAT PGGPIWMAQL LLGVFLVLLL SIIILALLQR KACRVQGGSD
PEPEPGSGGD CSEELPELAE LRFSQVIQEG GHAVVWAGRL QGEMVAIKAF PPRAVAQFRA
ERAVYQLLGL QHNHIVRFIT AGQGGPGPLP SGPLLVLELY PKGSLCHYLT QYTSDWGSSL
RMALSLAEGL AFLHGERWQD GQYKPGIAHR DLSSQNVLIR EDRSCAIGDL GLALVLPGLA
QPPALAPTQP RGPAAILEAG TQRYMAPELL DKTLDLQDWG TALQRADVYS LALLLWEILS
RCSDLRPDHR PPPFQLAYEA ELGSNPSACE LWALAVAERK RPNIPSSWSC SATDPRGLRE
LLEDCWDADP EARLTAECVQ QRLAALAYPQ VASSFPESCP QGCPENCPAA PASAAFPCRP
QQSSCLLSVQ QGSGSKS
