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Q16671 (AMHR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anti-Muellerian hormone type-2 receptor

EC=2.7.11.30
Alternative name(s):
Anti-Muellerian hormone type II receptor
Short name=AMH type II receptor
MIS type II receptor
Short name=MISRII
Short name=MRII
Gene names
Name:AMHR2
Synonyms:AMHR, MISR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Involvement in disease

Persistent Muellerian duct syndrome 2 (PMDS2) [MIM:261550]: A form of male pseudohermaphroditism characterized by a failure of Muellerian duct regression in otherwise normal males.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-6423788,EBI-352572

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16671-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16671-2)

The sequence of this isoform differs from the canonical sequence as follows:
     430-573: DSSPPPFQLA...PQPACTLSPV → AVHHPSNWPM...GAALPQTLMG
Note: No experimental confirmation available.
Isoform 3 (identifier: Q16671-3)

The sequence of this isoform differs from the canonical sequence as follows:
     381-475: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 573556Anti-Muellerian hormone type-2 receptor
PRO_0000024408

Regions

Topological domain18 – 149132Extracellular Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 573403Cytoplasmic Potential
Domain203 – 518316Protein kinase
Nucleotide binding209 – 2179ATP By similarity

Sites

Active site3331Proton acceptor By similarity
Binding site2301ATP By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence381 – 47595Missing in isoform 3.
VSP_045281
Alternative sequence430 – 573144DSSPP…TLSPV → AVHHPSNWPMRQNWAIPLPL MSYGPWQCRRGGVPTSHPPG AALPQTLMG in isoform 2.
VSP_044548
Natural variant541R → C in PMDS2. Ref.8
VAR_015525
Natural variant1421G → V in PMDS2. Ref.8
VAR_015526
Natural variant2821H → Q in PMDS2. Ref.8
VAR_015527
Natural variant3191R → H. Ref.4
Corresponds to variant rs144236183 [ dbSNP | Ensembl ].
VAR_069048
Natural variant4061R → Q in PMDS2. Ref.9
VAR_015528
Natural variant4261D → G in PMDS2. Ref.8
VAR_015529
Natural variant444 – 4529Missing in PMDS2.
VAR_031057
Natural variant4581V → A in PMDS2. Ref.8
VAR_015530
Natural variant4911D → H in PMDS2. Ref.8
VAR_015531
Natural variant5041R → C in PMDS2. Ref.8
VAR_015532

Experimental info

Sequence conflict1211S → N in AAU21221. Ref.4
Sequence conflict1611L → V in CAA62593. Ref.2
Sequence conflict5011V → A in AAU21221. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1347C10C2942FDBA

FASTA57362,750
        10         20         30         40         50         60 
MLGSLGLWAL LPTAVEAPPN RRTCVFFEAP GVRGSTKTLG ELLDTGTELP RAIRCLYSRC 

        70         80         90        100        110        120 
CFGIWNLTQD RAQVEMQGCR DSDEPGCESL HCDPSPRAHP SPGSTLFTCS CGTDFCNANY 

       130        140        150        160        170        180 
SHLPPPGSPG TPGSQGPQAA PGESIWMALV LLGLFLLLLL LLGSIILALL QRKNYRVRGE 

       190        200        210        220        230        240 
PVPEPRPDSG RDWSVELQEL PELCFSQVIR EGGHAVVWAG QLQGKLVAIK AFPPRSVAQF 

       250        260        270        280        290        300 
QAERALYELP GLQHDHIVRF ITASRGGPGR LLSGPLLVLE LHPKGSLCHY LTQYTSDWGS 

       310        320        330        340        350        360 
SLRMALSLAQ GLAFLHEERW QNGQYKPGIA HRDLSSQNVL IREDGSCAIG DLGLALVLPG 

       370        380        390        400        410        420 
LTQPPAWTPT QPQGPAAIME AGTQRYMAPE LLDKTLDLQD WGMALRRADI YSLALLLWEI 

       430        440        450        460        470        480 
LSRCPDLRPD SSPPPFQLAY EAELGNTPTS DELWALAVQE RRRPYIPSTW RCFATDPDGL 

       490        500        510        520        530        540 
RELLEDCWDA DPEARLTAEC VQQRLAALAH PQESHPFPES CPRGCPPLCP EDCTSIPAPT 

       550        560        570 
ILPCRPQRSA CHFSVQQGPC SRNPQPACTL SPV 

« Hide

Isoform 2 [UniParc].

Checksum: ADCA1BB6AC850665
Show »

FASTA47852,241
Isoform 3 [UniParc].

Checksum: C0FA484B50E52A97
Show »

FASTA47851,827

References

« Hide 'large scale' references
[1]"Insensitivity to anti-Muellerian hormone due to a mutation in the human anti-Muellerian hormone receptor."
Imbeaud S., Faure E., Lamarre I., Mattei M.-G., di Clemente N., Tizard R., Carre-Eusebe D., Belville C., Tragethon L., Tonkin C., Nelson J., McAuliffe M., Bidart J.-M., Lababidi A., Josso N., Cate R.L., Picard J.-Y.
Nat. Genet. 11:382-388(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and chromosomal localization of the human anti-Muellerian hormone type II receptor gene."
Visser J.A., McLuskey A., van Beers T., Weghuis D.O., van Kessel A.G., Grootegoed J.A., Themmen A.P.N.
Biochem. Biophys. Res. Commun. 215:1029-1036(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human ovarian cancer, cell lines, and primary ascites cells express the human Muellerian inhibiting substance (MIS) type II receptor, bind, and are responsive to MIS."
Masiakos P.T., MacLaughlin D.T., Maheswaran S., Teixeira J., Fuller A.F. Jr., Shah P.C., Kehas D.J., Kenneally M.K., Dombkowski D.M., Ha T.U., Preffer F.I., Donahoe P.K.
Clin. Cancer Res. 5:3488-3499(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]Li H., Ke R., Shen C., Zhou G., Zhong G., Lin L., Yang S.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT HIS-319.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[8]"A 27 base-pair deletion of the anti-Muellerian type II receptor gene is the most common cause of the persistent Muellerian duct syndrome."
Imbeaud S., Belville C., Messika-Zeitoun L., Rey R., di Clemente N., Josso N., Picard J.-Y.
Hum. Mol. Genet. 5:1269-1277(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PMDS2 CYS-54; VAL-142; GLN-282; GLY-426; 444-LEU--GLU-452 DEL; ALA-458; HIS-491 AND CYS-504.
[9]"Autosomal recessive segregation of a truncating mutation of anti-Muellerian type II receptor in a family affected by the persistent Muellerian duct syndrome contrasts with its dominant negative activity in vitro."
Messika-Zeitoun L., Gouedard L., Belville C., Dutertre M., Lins L., Imbeaud S., Hughes I.A., Picard J.-Y., Josso N., di Clemente N.
J. Clin. Endocrinol. Metab. 86:4390-4397(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PMDS2 GLN-406.
+Additional computationally mapped references.

Web resources

Wikipedia

Anti-Mullerian hormone entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89013 Genomic DNA. Translation: CAA61418.1.
U29700 Genomic DNA. Translation: AAC50328.1.
X91156 expand/collapse EMBL AC list , X91157, X91158, X91159, X91160, X91161, X91162, X91163, X91164, X91165, X91166 Genomic DNA. Translation: CAA62593.1.
AF172932 mRNA. Translation: AAD48497.1.
AY714878 mRNA. Translation: AAU21221.1.
AK313593 mRNA. No translation available.
AC068889 Genomic DNA. No translation available.
BC126316 mRNA. Translation: AAI26317.1.
BC136356 mRNA. Translation: AAI36357.1.
CCDSCCDS53798.1. [Q16671-3]
CCDS55829.1. [Q16671-2]
CCDS8858.1. [Q16671-1]
PIRJC4335.
RefSeqNP_001158162.1. NM_001164690.1. [Q16671-2]
NP_001158163.1. NM_001164691.1. [Q16671-3]
NP_065434.1. NM_020547.2. [Q16671-1]
UniGeneHs.659889.

3D structure databases

ProteinModelPortalQ16671.
SMRQ16671. Positions 199-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106766. 2 interactions.
IntActQ16671. 1 interaction.
STRING9606.ENSP00000257863.

Chemistry

DrugBankDB00171. Adenosine triphosphate.

PTM databases

PhosphoSiteQ16671.

Polymorphism databases

DMDM9087133.

Proteomic databases

PaxDbQ16671.
PRIDEQ16671.

Protocols and materials databases

DNASU269.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257863; ENSP00000257863; ENSG00000135409. [Q16671-1]
ENST00000379791; ENSP00000369117; ENSG00000135409. [Q16671-3]
ENST00000550311; ENSP00000446661; ENSG00000135409. [Q16671-2]
GeneID269.
KEGGhsa:269.
UCSCuc001scx.2. human. [Q16671-1]

Organism-specific databases

CTD269.
GeneCardsGC12P053823.
HGNCHGNC:465. AMHR2.
MIM261550. phenotype.
600956. gene.
neXtProtNX_Q16671.
Orphanet2856. Persistent Mullerian duct syndrome.
PharmGKBPA24770.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243040.
HOGENOMHOG000033920.
HOVERGENHBG097461.
InParanoidQ16671.
KOK04672.
OMACNANYSH.
OrthoDBEOG7WHH97.
PhylomeDBQ16671.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
SignaLinkQ16671.

Gene expression databases

ArrayExpressQ16671.
BgeeQ16671.
CleanExHS_AMHR2.
GenevestigatorQ16671.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR015771. Anti-muellerian_hrmn_rcpt_II.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037392. AMHRII. 1 hit.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi269.
NextBio1057.
PROQ16671.
SOURCESearch...

Entry information

Entry nameAMHR2_HUMAN
AccessionPrimary (citable) accession number: Q16671
Secondary accession number(s): A0AVE1 expand/collapse secondary AC list , B9EGB7, E9PGD2, F8W1D2, Q13762, Q647K2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM