ID   MOS_RAT                 Reviewed;         339 AA.
AC   P00539;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Proto-oncogene serine/threonine-protein kinase mos {ECO:0000305};
DE            EC=2.7.11.1;
DE   AltName: Full=Oocyte maturation factor mos;
DE   AltName: Full=Proto-oncogene c-Mos;
GN   Name=Mos {ECO:0000312|RGD:3103};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6322135; DOI=10.1093/nar/12.4.2147;
RA   van der Hoorn F.A., Firzlaff J.;
RT   "Complete c-mos (rat) nucleotide sequence: presence of conserved domains in
RT   c-mos proteins.";
RL   Nucleic Acids Res. 12:2147-2156(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Skeletal muscle;
RX   PubMed=1697408;
RA   Leibovitch S.A., Lenormand J.-L., Leibovitch M.-P., Guiller M., Mallard L.,
RA   Harel J.;
RT   "Rat myogenic c-mos cDNA: cloning sequence analysis and regulation during
RT   muscle development.";
RL   Oncogene 5:1149-1157(1990).
CC   -!- FUNCTION: Serine/threonine kinase involved in the regulation of MAPK
CC       signaling. Is an activator of the ERK1/2 signaling cascade playing an
CC       essential role in the stimulation of oocyte maturation.
CC       {ECO:0000250|UniProtKB:P00540}.
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   -!- 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;
CC   -!- SUBUNIT: Interacts with MAP2K1/MEK1. {ECO:0000250|UniProtKB:P00540}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in gonadal tissues, and cardiac
CC       and skeletal muscles. {ECO:0000269|PubMed:1697408}.
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; X00422; CAA25123.1; -; Genomic_DNA.
DR   EMBL; X52952; CAA37128.1; -; mRNA.
DR   PIR; A00648; TVRTM.
DR   AlphaFoldDB; P00539; -.
DR   SMR; P00539; -.
DR   STRING; 10116.ENSRNOP00000064243; -.
DR   PhosphoSitePlus; P00539; -.
DR   PaxDb; 10116-ENSRNOP00000064243; -.
DR   UCSC; RGD:3103; rat.
DR   AGR; RGD:3103; -.
DR   RGD; 3103; Mos.
DR   eggNOG; KOG0192; Eukaryota.
DR   InParanoid; P00539; -.
DR   PhylomeDB; P00539; -.
DR   BRENDA; 2.7.10.2; 5301.
DR   PRO; PR:P00539; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR   GO; GO:0051296; P:establishment of meiotic spindle orientation; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR   GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0000212; P:meiotic spindle organization; ISS:UniProtKB.
DR   GO; GO:1902103; P:negative regulation of metaphase/anaphase transition of meiotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0001556; P:oocyte maturation; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; NAS:RGD.
DR   CDD; cd13979; STKc_Mos; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR23257:SF706; PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE MOS; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Proto-oncogene;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..339
FT                   /note="Proto-oncogene serine/threonine-protein kinase mos"
FT                   /id="PRO_0000086347"
FT   DOMAIN          61..335
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         67..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        47
FT                   /note="L -> V (in Ref. 2; CAA37128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="R -> A (in Ref. 2; CAA37128)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   339 AA;  37621 MW;  A074246A5E471278 CRC64;
     MPSPLILCRY LPRELSPTVD SRSCSSPLVA SRAGKFLGAT PPRAPRLSRR LAWCFIDWGQ
     VCLLHRLGSG GFGSVYKATY HGVPVAIKQV NKCTRTLRAS QRNFWAELNI ARLHHDNIIR
     VVAASTRTPE GSNSLGTIIM EFGGNVTLHQ VIYGATRSPE PLSCREQLSL GKCLKYSLDI
     VNGLLFLHSQ SILHLDLKPA NILISEKDVC KISDFGCSQK LQDLRCRPSL HHIGGTYTHQ
     APELLKGEIA TPKADIYSFG ITLWQMTTRE VPYSGEPQYV QYAVVAYNLR PHWQAVFTAS
     LTGKTLQNNV QSCWEARALQ RPGAELLQKD LKAFRGALG
//