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   24-JAN-2024, entry version 174.
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   GlyCosmos; Q62893; 2 sites, No reported glycans.
DR   GlyGen; Q62893; 2 sites.
DR   PhosphoSitePlus; Q62893; -.
DR   PaxDb; 10116-ENSRNOP00000020103; -.
DR   Ensembl; ENSRNOT00000020103.6; ENSRNOP00000020103.4; ENSRNOG00000014850.6.
DR   Ensembl; ENSRNOT00055047289; ENSRNOP00055038869; ENSRNOG00055027289.
DR   Ensembl; ENSRNOT00060025514; ENSRNOP00060020346; ENSRNOG00060014906.
DR   Ensembl; ENSRNOT00065038390; ENSRNOP00065031100; ENSRNOG00065022490.
DR   GeneID; 29530; -.
DR   KEGG; rno:29530; -.
DR   UCSC; RGD:70964; rat.
DR   AGR; RGD:70964; -.
DR   CTD; 269; -.
DR   RGD; 70964; Amhr2.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000160885; -.
DR   InParanoid; Q62893; -.
DR   OMA; RCPDLWP; -.
DR   OrthoDB; 3900892at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; Q62893; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA: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:RGD.
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; IDA: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; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; Q62893; RN.
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
//