[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1210/en.137.1.160; PubMed=8536608 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1073/pnas.96.24.13831; PubMed=10570158 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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: Magnesium or manganese (By similarity).
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.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U42427; AAC52343.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X71916; CAA50731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF092445; AAC64138.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S41627; S41627.

NP_112260.1; -.

3D structure databases

HSSP

P36897; 1IAS. [HSSP ENTRY / PDB]

ModBase

Q62893.

Organism-specific databases

RGD

70964; Amhr2.

Gene expression databases

ArrayExpress

Q62893; -.

GermOnline

ENSRNOG00000014850; Rattus norvegicus.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (inferred from direct assay from MGI).
GO:0042562;	Molecular function: hormone binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005026;	Molecular function: transforming growth factor beta receptor activity, type II (inferred from direct assay from MGI).
GO:0007548;	Biological process: sex differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0007179;	Biological process: transforming growth factor beta receptor signaling pathway (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR017193; Anti-muellerian_hrmn_rcpt_II.
IPR015771; Anti-muellerian_hrmn_rcpt_II_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

PANTHER

PTHR23255:SF4; MIS_II_R; 1.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037392; AMHRII; 1.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q62893.

Genome annotation databases

Ensembl

ENSRNOG00000014850; Rattus norvegicus. [Contig view]

GeneID

29530; -.

KEGG

rno:29530; -.

Phylogenomic databases

HOVERGEN

Q62893; -.

Other

ProtoNet

Q62893.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`CHAIN`	`18 557`	`540`	`Anti-Muellerian hormone type-2 receptor.`	`PRO_0000024409`
`TOPO_DOM`	`18 144`	`127`	`Extracellular (Potential).`
`TRANSMEM`	`145 165`	`21`	`Potential.`
`TOPO_DOM`	`166 557`	`392`	`Cytoplasmic (Potential).`
`DOMAIN`	`201 511`	`311`	`Protein kinase.`
`NP_BIND`	`207 215`	`9`	`ATP (By similarity).`
`ACT_SITE`	`331 331`		`Proton acceptor (By similarity).`
`BINDING`	`228 228`		`ATP (By similarity).`
`CARBOHYD`	`66 66`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`119 119`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`527 527`		`C -> Y (in Ref. 2; CAA50731).`

Sequence information

Length: 557 AA [This is the length of the unprocessed precursor]

Molecular weight: 59749 Da [This is the MW of the unprocessed precursor]

CRC64: 8EDEE9C0C32EBDD5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGTLGLWTL LPAAAQVSPN RRTCVFFEAP GVRGSTKTLG EVVDAGPGPP KGIRCLYSHC 

        70         80         90        100        110        120 
CFGIWNLTHG RAQVEMQGCL DSDEPGCESL HCDPVPRAHP SPSSTLFTCS CGTDFCNANY 

       130        140        150        160        170        180 
SHLPPSGNRG APGPQEPQAT PGGPIWMAQL LLGVFLVLLL SIIILALLQR KACRVQGGSD 

       190        200        210        220        230        240 
PEPEPGSGGD CSEELPELAE LRFSQVIQEG GHAVVWAGRL QGEMVAIKAF PPRAVAQFRA 

       250        260        270        280        290        300 
ERAVYQLLGL QHNHIVRFIT AGQGGPGPLP SGPLLVLELY PKGSLCHYLT QYTSDWGSSL 

       310        320        330        340        350        360 
RMALSLAEGL AFLHGERWQD GQYKPGIAHR DLSSQNVLIR EDRSCAIGDL GLALVLPGLA 

       370        380        390        400        410        420 
QPPALAPTQP RGPAAILEAG TQRYMAPELL DKTLDLQDWG TALQRADVYS LALLLWEILS 

       430        440        450        460        470        480 
RCSDLRPDHR PPPFQLAYEA ELGSNPSACE LWALAVAERK RPNIPSSWSC SATDPRGLRE 

       490        500        510        520        530        540 
LLEDCWDADP EARLTAECVQ QRLAALAYPQ VASSFPESCP QGCPENCPAA PASAAFPCRP 

       550 
QQSSCLLSVQ QGSGSKS

Q62893 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools