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Anti-Muellerian hormone type-2 receptor (EC 2.7.11.30) (Anti-Muellerian hormone type II receptor) (AMH type II receptor) (C14) (MIS type II receptor) (MISRII) (MRII)

 AMHR2_RAT               Reviewed;         557 AA.
Q62893; Q63045; Q9R0A7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 146.
RecName: Full=Anti-Muellerian hormone type-2 receptor;
EC=2.7.11.30;
AltName: Full=Anti-Muellerian hormone type II receptor;
Short=AMH type II receptor;
AltName: Full=C14;
AltName: Full=MIS type II receptor;
Short=MISRII;
Short=MRII;
Flags: Precursor;
Name=Amhr2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8536608; DOI=10.1210/endo.137.1.8536608;
Teixeira J., He W.W., Shah P.C., Morikawa N., Lee M.M., Catlin E.A.,
Hudson P.L., Wing J., Maclaughlin D.T., Donahoe P.K.;
"Developmental expression of a candidate Muellerian inhibiting
substance type II receptor.";
Endocrinology 137:160-165(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=8119126;
Baarends W.M., Van Helmond M.J.L., Post M., Van der Schoot P.J.C.M.,
Hoogerbrugge J.W., de Winter J.P., Uilenbroek J.T.J., Karels B.,
Wilming L.G., Meijers J.H.C., Themmem A.P.N., Grootegoed A.J.;
"A novel member of the transmembrane serine/threonine kinase receptor
family is specifically expressed in the gonads and in mesenchymal
cells adjacent to the Muellerian duct.";
Development 120:189-197(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
STRAIN=Sprague-Dawley;
PubMed=10570158; DOI=10.1073/pnas.96.24.13831;
Teixeira J., Kehas D.J., Antun R., Donahoe P.K.;
"Transcriptional regulation of the rat Muellerian inhibiting substance
type II receptor in rodent Leydig cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:13831-13838(1999).
-!- FUNCTION: On ligand binding, forms a receptor complex consisting
of two type II and two type I transmembrane serine/threonine
kinases. Type II receptors phosphorylate and activate type I
receptors which autophosphorylate, then bind and activate SMAD
transcriptional regulators. Receptor for anti-Muellerian hormone.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DEVELOPMENTAL STAGE: Expressed in the mesenchymal cells
surrounding the Muellerian duct at embryonic days 14, 15, and 16
and in tubular and follicular structures of the fetal gonads.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U42427; AAC52343.1; -; mRNA.
EMBL; X71916; CAA50731.1; -; mRNA.
EMBL; AF092445; AAC64138.1; -; Genomic_DNA.
PIR; S41627; S41627.
RefSeq; NP_112260.1; NM_030998.1.
UniGene; Rn.10165; -.
ProteinModelPortal; Q62893; -.
SMR; Q62893; -.
STRING; 10116.ENSRNOP00000020103; -.
PhosphoSitePlus; Q62893; -.
PaxDb; Q62893; -.
PRIDE; Q62893; -.
Ensembl; ENSRNOT00000020103; ENSRNOP00000020103; ENSRNOG00000014850.
GeneID; 29530; -.
KEGG; rno:29530; -.
UCSC; RGD:70964; rat.
CTD; 269; -.
RGD; 70964; Amhr2.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00900000140999; -.
HOGENOM; HOG000033920; -.
HOVERGEN; HBG097461; -.
InParanoid; Q62893; -.
KO; K04672; -.
OMA; CCFGIWN; -.
OrthoDB; EOG091G05X7; -.
PhylomeDB; Q62893; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-201451; Signaling by BMP.
PRO; PR:Q62893; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000014850; -.
ExpressionAtlas; Q62893; baseline and differential.
Genevisible; Q62893; RN.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:1990272; F:anti-Mullerian hormone receptor activity; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042562; F:hormone binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004872; F:receptor activity; ISS:UniProtKB.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IDA:MGI.
GO; GO:1990262; P:anti-Mullerian hormone signaling pathway; ISO:RGD.
GO; GO:0008585; P:female gonad development; IEP:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:RGD.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:1902613; P:negative regulation of anti-Mullerian hormone signaling pathway; ISO:RGD.
GO; GO:0007548; P:sex differentiation; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
InterPro; IPR000472; Activin_recp.
InterPro; IPR015771; Anti-muellerian_hrmn_rcpt_II.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF037392; AMHRII; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Disulfide bond; Glycoprotein; Kinase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 557 Anti-Muellerian hormone type-2 receptor.
/FTId=PRO_0000024409.
TOPO_DOM 18 144 Extracellular. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TOPO_DOM 166 557 Cytoplasmic. {ECO:0000255}.
DOMAIN 201 511 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 207 215 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 331 331 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 228 228 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 79 {ECO:0000250|UniProtKB:P37023}.
DISULFID 92 109 {ECO:0000250|UniProtKB:P37023}.
CONFLICT 527 527 C -> Y (in Ref. 2; CAA50731).
{ECO:0000305}.
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


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