MOS_RAT
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 03-AUG-2022, entry version 133.
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 -!- 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 -!- TISSUE SPECIFICITY: Expressed mainly in gonadal tissues, and cardiac
CC and skeletal muscles.
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; P00539; -.
DR PRIDE; P00539; -.
DR UCSC; RGD:3103; rat.
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:0005829; C:cytosol; IDA: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:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:RGD.
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 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 2: Evidence at transcript level;
KW ATP-binding; 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
