ID   MOS_PATPE               Reviewed;         351 AA.
AC   Q9GRC0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Serine/threonine-protein kinase mos {ECO:0000250|UniProtKB:P10741};
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P10741};
DE   AltName: Full=Oocyte maturation factor mos {ECO:0000250|UniProtKB:P10741};
GN   Name=mos {ECO:0000312|EMBL:BAB13700.1};
OS   Patiria pectinifera (Starfish) (Asterina pectinifera).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Asterinidae; Patiria.
OX   NCBI_TaxID=7594;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB13700.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:11121036};
RX   PubMed=11121036; DOI=10.1073/pnas.97.26.14301;
RA   Tachibana K., Tanaka D., Isobe T., Kishimoto T.;
RT   "c-Mos forces the mitotic cell cycle to undergo meiosis II to produce
RT   haploid gametes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14301-14306(2000).
CC   -!- FUNCTION: Suppresses the mitotic cell cycle in oocytes, forcing them to
CC       undergo meiosis II to produce haploid gametes. Acts as a MAPK kinase
CC       kinase (MAP3K) that acts upstream of MAP kinase in oocytes.
CC       {ECO:0000269|PubMed:11121036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000250|UniProtKB:P10741};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P10741};
CC   -!- DEVELOPMENTAL STAGE: Expression is first detected in immature oocytes
CC       just after germinal vesicle breakdown (GVBD). Expression remains
CC       throughout both meiotic cycles, unless fertilization occurs, and
CC       disappears after fertilization (at protein level).
CC       {ECO:0000269|PubMed:11121036}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AB040102; BAB13700.1; -; mRNA.
DR   AlphaFoldDB; Q9GRC0; -.
DR   SMR; Q9GRC0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0007292; P:female gamete generation; IDA:UniProtKB.
DR   GO; GO:0007147; P:female meiosis II; IDA:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="Serine/threonine-protein kinase mos"
FT                   /id="PRO_0000419763"
FT   DOMAIN          71..340
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10741,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         77..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P10741,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P10741,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   351 AA;  39155 MW;  5EE04A62A177604C CRC64;
     MPCDTADNWA RYEGQDNAIM VARRGSVNSA FVTNSSQYHQ AEDTNGNCFI NARNDNWDNR
     DCNACVGHSD FSIDGVIGSG GFGSVFLGRY CGRRVAVKSV RQCSRNKEAS RQSFQAEFNA
     LLLRHDNIVS VLATTAYEDF DSGAFIIMEY AGRNLQQIVN DPGSSLSPTR RTKYALHIIR
     ALHYTHSQGI AHLDVKPANV IVDSNTDVCR LADFGCSQRV SEGEGRDSFT SRSYLTGTFA
     YRAPELLRGR PPTTKADIYS YGVTLWQMLT RETPFAGENH HVVIFGVVAQ NLRPSLPENA
     NDAWYESLVT RCWEGRVADR PSAAEILLAL ERRTDDTENL PRDLKRRHGT T