ID   MOS_XENLA               Reviewed;         359 AA.
AC   P12965;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Serine/threonine-protein kinase mos;
DE            EC=2.7.11.1;
DE   AltName: Full=pp39-mos;
GN   Name=mos;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2527365; DOI=10.1073/pnas.86.15.5805;
RA   Freeman R.S., Pickham K.M., Kanki J.P., Lee B.A., Pena S.V., Donoghue D.J.;
RT   "Xenopus homolog of the mos protooncogene transforms mammalian fibroblasts
RT   and induces maturation of Xenopus oocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5805-5809(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2971141; DOI=10.1038/335519a0;
RA   Sagata N., Oskarsson M., Copeland T., Brumbaugh J., Vande Woude G.F.;
RT   "Function of c-mos proto-oncogene product in meiotic maturation in Xenopus
RT   oocytes.";
RL   Nature 335:519-525(1988).
CC   -!- FUNCTION: Serine/threonine kinase involved in the regulation of MAPK
CC       signaling. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00540}.
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; M25366; AAA49677.1; -; mRNA.
DR   EMBL; X13311; CAA31689.1; -; mRNA.
DR   PIR; S06433; TVXLMS.
DR   RefSeq; NP_001081563.1; NM_001088094.1.
DR   AlphaFoldDB; P12965; -.
DR   SMR; P12965; -.
DR   BioGRID; 99260; 3.
DR   iPTMnet; P12965; -.
DR   GeneID; 397924; -.
DR   KEGG; xla:397924; -.
DR   AGR; Xenbase:XB-GENE-1011507; -.
DR   CTD; 397924; -.
DR   Xenbase; XB-GENE-1011507; mos.L.
DR   OrthoDB; 54134at2759; -.
DR   BRENDA; 2.7.10.2; 6725.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 397924; Expressed in blastula and 19 other cell types or tissues.
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:0000165; P:MAPK cascade; IDA:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
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..359
FT                   /note="Serine/threonine-protein kinase mos"
FT                   /id="PRO_0000086358"
FT   DOMAIN          63..336
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         69..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        46
FT                   /note="P -> R (in Ref. 2; CAA31689)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  39162 MW;  6442F2A056738B57 CRC64;
     MPSPIPVERF LPRDLSPSID LRPCSSPLEL SHRKLPGGLP ACSGRPRLLP PRLAWCSIDW
     EQVLLLEPLG SGGFGSVYRA TYRGETVALK KVKRSTKNSL ASRQSFWAEL NAARLRHPHV
     VRVVAASASC PGDPGCPGTI IMEYTGTGTL HQRIYGRSPP LGAEICMRYA RHVADGLRFL
     HRDGVVHLDL KPANVLLAPG DLCKIGDFGC SQRLREGDEA AGGEPCCTQL RHVGGTYTHR
     APELLKGEPV TAKADIYSFA ITLWQMVSRE LPYTGDRQCV LYAVVAYDLR PEMGPLFSHT
     EEGRAARTIV QSCWAARPQE RPNAEQLLER LEQECAMCTG GPPSCSPESN APPPLGTGL
//