ID   AMHR2_RABIT             Reviewed;         569 AA.
AC   Q28616;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 136.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=7997230; DOI=10.1210/mend.8.8.7997230;
RA   di Clemente N., Wilson C., Faure E., Boussin L., Carmillo P., Tizard R.,
RA   Picard J.-Y., Vigier B., Josso N., Cate R.;
RT   "Cloning, expression, and alternative splicing of the receptor for anti-
RT   Muellerian hormone.";
RL   Mol. Endocrinol. 8:1006-1020(1994).
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; U15025; AAA21875.1; -; mRNA.
DR   RefSeq; NP_001076263.1; NM_001082794.1.
DR   AlphaFoldDB; Q28616; -.
DR   SMR; Q28616; -.
DR   STRING; 9986.ENSOCUP00000041639; -.
DR   GlyCosmos; Q28616; 2 sites, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000022385; -.
DR   GeneID; 100009599; -.
DR   KEGG; ocu:100009599; -.
DR   CTD; 269; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   InParanoid; Q28616; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; PF00069; Pkinase; 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.
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..569
FT                   /note="Anti-Muellerian hormone type-2 receptor"
FT                   /id="PRO_0000260266"
FT   TOPO_DOM        18..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..569
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          201..511
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          512..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   569 AA;  61099 MW;  388800F0ECAA5AAB CRC64;
     MLGTLGLWAL LPAAVQAPPN RRTCVFFEAP GVRGSTKTLG ELLDAGPGPP RVIRCLYSRC
     CFGIWNLTRD QAQVEMQGCR DSDEPGCESL SCDPSPRARA SSGSTLFTCS CGADFCNANY
     SHLPPLGGPG TPGPQGPQAA PGESPWMALA LLGLVLLLLL LLGGIVVALL QRKAYRVQSG
     PEPEPDSGRD CSEELPELPQ LCFSQVIREG GHAAVWAGQL QGELVAIKVF PRRAVAQFRA
     ERALYELPGL QHNHVVRFIA AGQGGPGPLP SGPLLVLELH PKGSLCQYLS QHTSDWGSSL
     RMALSLAQGL AFLHEERWQD GQYKPGIAHR DLSSQNVLIR EDGSCAIGDL GLALVLPGFA
     QPRAWAPPQP RGPAAIMEAG TQRYMAPELL DKSLDLQDWG TALRRADVYS LALLLWEILS
     RCPDLRPDGR PPPFQLAYEA ELGSAPTTCE LWALAVEERR RPDIPSSWCC FATDPGGLRE
     LLEDCWDADP EARLTAECVQ QRLVALVHPQ EAQPCPEGRP HSHPEDWPPA PAPAPALLPG
     SPQPGACHFG VQQGLCSRNP GAACASSDV
//