AMHR2_HUMAN
ID AMHR2_HUMAN Reviewed; 573 AA.
AC Q16671; A0AVE1; B9EGB7; E9PGD2; F8W1D2; Q13762; Q647K2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 210.
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; Synonyms=AMHR, MISR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7493017; DOI=10.1038/ng1295-382;
RA Imbeaud S., Faure E., Lamarre I., Mattei M.-G., di Clemente N., Tizard R.,
RA Carre-Eusebe D., Belville C., Tragethon L., Tonkin C., Nelson J.,
RA McAuliffe M., Bidart J.-M., Lababidi A., Josso N., Cate R.L., Picard J.-Y.;
RT "Insensitivity to anti-Muellerian hormone due to a mutation in the human
RT anti-Muellerian hormone receptor.";
RL Nat. Genet. 11:382-388(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7488027; DOI=10.1006/bbrc.1995.2567;
RA Visser J.A., McLuskey A., van Beers T., Weghuis D.O., van Kessel A.G.,
RA Grootegoed J.A., Themmen A.P.N.;
RT "Structure and chromosomal localization of the human anti-Muellerian
RT hormone type II receptor gene.";
RL Biochem. Biophys. Res. Commun. 215:1029-1036(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10589763;
RA Masiakos P.T., MacLaughlin D.T., Maheswaran S., Teixeira J.,
RA Fuller A.F. Jr., Shah P.C., Kehas D.J., Kenneally M.K., Dombkowski D.M.,
RA Ha T.U., Preffer F.I., Donahoe P.K.;
RT "Human ovarian cancer, cell lines, and primary ascites cells express the
RT human Muellerian inhibiting substance (MIS) type II receptor, bind, and are
RT responsive to MIS.";
RL Clin. Cancer Res. 5:3488-3499(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT HIS-319.
RA Li H., Ke R., Shen C., Zhou G., Zhong G., Lin L., Yang S.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH ACVR1.
RX PubMed=17911401; DOI=10.1677/joe-07-0281;
RA Renlund N., O'Neill F.H., Zhang L., Sidis Y., Teixeira J.;
RT "Activin receptor-like kinase-2 inhibits activin signaling by blocking the
RT binding of activin to its type II receptor.";
RL J. Endocrinol. 195:95-103(2007).
RN [9]
RP VARIANTS PMDS2 CYS-54; VAL-142; GLN-282; GLY-426; 445-GLY--LEU-453 DEL;
RP ALA-458; HIS-491 AND CYS-504.
RX PubMed=8872466; DOI=10.1093/hmg/5.9.1269;
RA Imbeaud S., Belville C., Messika-Zeitoun L., Rey R., di Clemente N.,
RA Josso N., Picard J.-Y.;
RT "A 27 base-pair deletion of the anti-Muellerian type II receptor gene is
RT the most common cause of the persistent Muellerian duct syndrome.";
RL Hum. Mol. Genet. 5:1269-1277(1996).
RN [10]
RP VARIANT PMDS2 GLN-406.
RX PubMed=11549681; DOI=10.1210/jcem.86.9.7839;
RA Messika-Zeitoun L., Gouedard L., Belville C., Dutertre M., Lins L.,
RA Imbeaud S., Hughes I.A., Picard J.-Y., Josso N., di Clemente N.;
RT "Autosomal recessive segregation of a truncating mutation of anti-
RT Muellerian type II receptor in a family affected by the persistent
RT Muellerian duct syndrome contrasts with its dominant negative activity in
RT vitro.";
RL J. Clin. Endocrinol. Metab. 86:4390-4397(2001).
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:0000269|PubMed:17911401}.
CC -!- INTERACTION:
CC Q16671; P08238: HSP90AB1; NbExp=2; IntAct=EBI-6423788, EBI-352572;
CC Q16671; P21145: MAL; NbExp=3; IntAct=EBI-6423788, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16671-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16671-2; Sequence=VSP_044548;
CC Name=3;
CC IsoId=Q16671-3; Sequence=VSP_045281;
CC -!- DISEASE: Persistent Muellerian duct syndrome 2 (PMDS2) [MIM:261550]: A
CC form of male pseudohermaphroditism characterized by a failure of
CC Muellerian duct regression in otherwise normal males.
CC {ECO:0000269|PubMed:11549681, ECO:0000269|PubMed:8872466}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Anti-Mullerian hormone entry;
CC URL="https://en.wikipedia.org/wiki/Anti-m%C3%BCllerian_hormone";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X89013; CAA61418.1; -; Genomic_DNA.
DR EMBL; U29700; AAC50328.1; -; Genomic_DNA.
DR EMBL; X91156; CAA62593.1; -; Genomic_DNA.
DR EMBL; X91157; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91158; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91159; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91160; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91161; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91162; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91163; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91164; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91165; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; X91166; CAA62593.1; JOINED; Genomic_DNA.
DR EMBL; AF172932; AAD48497.1; -; mRNA.
DR EMBL; AY714878; AAU21221.1; -; mRNA.
DR EMBL; AK313593; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126316; AAI26317.1; -; mRNA.
DR EMBL; BC136356; AAI36357.1; -; mRNA.
DR CCDS; CCDS53798.1; -. [Q16671-3]
DR CCDS; CCDS55829.1; -. [Q16671-2]
DR CCDS; CCDS8858.1; -. [Q16671-1]
DR PIR; JC4335; JC4335.
DR RefSeq; NP_001158162.1; NM_001164690.2. [Q16671-2]
DR RefSeq; NP_001158163.1; NM_001164691.2. [Q16671-3]
DR RefSeq; NP_065434.1; NM_020547.3. [Q16671-1]
DR PDB; 7L0J; X-ray; 2.60 A; B=18-124.
DR PDBsum; 7L0J; -.
DR AlphaFoldDB; Q16671; -.
DR SMR; Q16671; -.
DR BioGRID; 106766; 58.
DR IntAct; Q16671; 5.
DR STRING; 9606.ENSP00000257863; -.
DR DrugBank; DB00171; ATP.
DR GlyGen; Q16671; 2 sites.
DR iPTMnet; Q16671; -.
DR PhosphoSitePlus; Q16671; -.
DR BioMuta; AMHR2; -.
DR DMDM; 9087133; -.
DR MassIVE; Q16671; -.
DR PaxDb; Q16671; -.
DR PeptideAtlas; Q16671; -.
DR PRIDE; Q16671; -.
DR ProteomicsDB; 20294; -.
DR ProteomicsDB; 29591; -.
DR ProteomicsDB; 61030; -. [Q16671-1]
DR ABCD; Q16671; 5 sequenced antibodies.
DR Antibodypedia; 27053; 302 antibodies from 32 providers.
DR DNASU; 269; -.
DR Ensembl; ENST00000257863.9; ENSP00000257863.3; ENSG00000135409.11. [Q16671-1]
DR Ensembl; ENST00000379791.7; ENSP00000369117.3; ENSG00000135409.11. [Q16671-3]
DR Ensembl; ENST00000550311.5; ENSP00000446661.1; ENSG00000135409.11. [Q16671-2]
DR GeneID; 269; -.
DR KEGG; hsa:269; -.
DR MANE-Select; ENST00000257863.9; ENSP00000257863.3; NM_020547.3; NP_065434.1.
DR UCSC; uc001scx.2; human. [Q16671-1]
DR CTD; 269; -.
DR DisGeNET; 269; -.
DR GeneCards; AMHR2; -.
DR HGNC; HGNC:465; AMHR2.
DR HPA; ENSG00000135409; Tissue enhanced (adrenal gland, ovary).
DR MalaCards; AMHR2; -.
DR MIM; 261550; phenotype.
DR MIM; 600956; gene.
DR neXtProt; NX_Q16671; -.
DR OpenTargets; ENSG00000135409; -.
DR Orphanet; 2856; Persistent Muellerian duct syndrome.
DR PharmGKB; PA24770; -.
DR VEuPathDB; HostDB:ENSG00000135409; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000160885; -.
DR HOGENOM; CLU_000288_8_4_1; -.
DR InParanoid; Q16671; -.
DR OMA; LTQPPTW; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; Q16671; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 2681.
DR PathwayCommons; Q16671; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR SignaLink; Q16671; -.
DR SIGNOR; Q16671; -.
DR BioGRID-ORCS; 269; 16 hits in 1105 CRISPR screens.
DR GenomeRNAi; 269; -.
DR Pharos; Q16671; Tbio.
DR PRO; PR:Q16671; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16671; protein.
DR Bgee; ENSG00000135409; Expressed in right adrenal gland cortex and 100 other tissues.
DR ExpressionAtlas; Q16671; baseline and differential.
DR Genevisible; Q16671; HS.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR GO; GO:1990272; F:anti-Mullerian hormone receptor activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042562; F:hormone binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IDA:UniProtKB.
DR GO; GO:0032924; P:activin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1990262; P:anti-Mullerian hormone signaling pathway; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0001880; P:Mullerian duct regression; NAS:UniProtKB.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
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; PF01064; Activin_recp; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Disease variant;
KW Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Pseudohermaphroditism; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..573
FT /note="Anti-Muellerian hormone type-2 receptor"
FT /id="PRO_0000024408"
FT TOPO_DOM 18..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
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"
FT VAR_SEQ 381..475
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045281"
FT VAR_SEQ 430..573
FT /note="DSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLR
FT ELLEDCWDADPEARLTAECVQQRLAALAHPQESHPFPESCPRGCPPLCPEDCTSIPAPT
FT ILPCRPQRSACHFSVQQGPCSRNPQPACTLSPV -> AVHHPSNWPMRQNWAIPLPLMS
FT YGPWQCRRGGVPTSHPPGAALPQTLMG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044548"
FT VARIANT 54
FT /note="R -> C (in PMDS2; dbSNP:rs534999427)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015525"
FT VARIANT 142
FT /note="G -> V (in PMDS2)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015526"
FT VARIANT 282
FT /note="H -> Q (in PMDS2; dbSNP:rs539695176)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015527"
FT VARIANT 319
FT /note="R -> H (in dbSNP:rs144236183)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_069048"
FT VARIANT 406
FT /note="R -> Q (in PMDS2; dbSNP:rs137853104)"
FT /evidence="ECO:0000269|PubMed:11549681"
FT /id="VAR_015528"
FT VARIANT 426
FT /note="D -> G (in PMDS2)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015529"
FT VARIANT 445..453
FT /note="Missing (in PMDS2)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_031057"
FT VARIANT 458
FT /note="V -> A (in PMDS2; dbSNP:rs775889926)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015530"
FT VARIANT 491
FT /note="D -> H (in PMDS2; dbSNP:rs780680518)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015531"
FT VARIANT 504
FT /note="R -> C (in PMDS2; dbSNP:rs772294564)"
FT /evidence="ECO:0000269|PubMed:8872466"
FT /id="VAR_015532"
FT CONFLICT 121
FT /note="S -> N (in Ref. 4; AAU21221)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="L -> V (in Ref. 2; CAA62593)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="V -> A (in Ref. 4; AAU21221)"
FT /evidence="ECO:0000305"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7L0J"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:7L0J"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:7L0J"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:7L0J"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:7L0J"
SQ SEQUENCE 573 AA; 62750 MW; 1347C10C2942FDBA CRC64;
MLGSLGLWAL LPTAVEAPPN RRTCVFFEAP GVRGSTKTLG ELLDTGTELP RAIRCLYSRC
CFGIWNLTQD RAQVEMQGCR DSDEPGCESL HCDPSPRAHP SPGSTLFTCS CGTDFCNANY
SHLPPPGSPG TPGSQGPQAA PGESIWMALV LLGLFLLLLL LLGSIILALL QRKNYRVRGE
PVPEPRPDSG RDWSVELQEL PELCFSQVIR EGGHAVVWAG QLQGKLVAIK AFPPRSVAQF
QAERALYELP GLQHDHIVRF ITASRGGPGR LLSGPLLVLE LHPKGSLCHY LTQYTSDWGS
SLRMALSLAQ GLAFLHEERW QNGQYKPGIA HRDLSSQNVL IREDGSCAIG DLGLALVLPG
LTQPPAWTPT QPQGPAAIME AGTQRYMAPE LLDKTLDLQD WGMALRRADI YSLALLLWEI
LSRCPDLRPD SSPPPFQLAY EAELGNTPTS DELWALAVQE RRRPYIPSTW RCFATDPDGL
RELLEDCWDA DPEARLTAEC VQQRLAALAH PQESHPFPES CPRGCPPLCP EDCTSIPAPT
ILPCRPQRSA CHFSVQQGPC SRNPQPACTL SPV
