AMHR2_RABIT
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 03-AUG-2022, entry version 131.
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.ENSOCUP00000022385; -.
DR GeneID; 100009599; -.
DR KEGG; ocu:100009599; -.
DR CTD; 269; -.
DR eggNOG; KOG3653; Eukaryota.
DR InParanoid; Q28616; -.
DR OrthoDB; 390511at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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 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
