MOS_MOUSE
ID MOS_MOUSE Reviewed; 343 AA.
AC P00536; E9PV67; F6UHW1; Q61886; Q61887; Q78EH5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 3.
DT 03-AUG-2022, entry version 162.
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|MGI:MGI:97052};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6173134; DOI=10.1016/0092-8674(81)90364-0;
RA van Beveren C., van Straaten F., Galleshaw J.A., Verma I.M.;
RT "Nucleotide sequence of the genome of a murine sarcoma virus.";
RL Cell 27:97-108(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30; 46-131 AND 261-343.
RX PubMed=6256659; DOI=10.1038/289258a0;
RA Van Beveren C., Galleshaw J.A., Jonas V., Berns A.J., Doolittle R.F.,
RA Donoghue D.J., Verma I.M.;
RT "Nucleotide sequence and formation of the transforming gene of a mouse
RT sarcoma virus.";
RL Nature 289:258-262(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
RC STRAIN=BALB/cJ;
RX PubMed=6292737; DOI=10.1038/300607a0;
RA Rechavi G., Givol D., Canaani E.;
RT "Activation of a cellular oncogene by DNA rearrangement: possible
RT involvement of an IS-like element.";
RL Nature 300:607-611(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 335-343.
RX PubMed=6300424; DOI=10.1128/jvi.45.2.607-617.1983;
RA Donoghue D.J., Hunter T.;
RT "Recombinational junctions of variants of Moloney murine sarcoma virus:
RT generation and divergence of a mammalian transforming gene.";
RL J. Virol. 45:607-617(1983).
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 specifically in testis during
CC spermatogenesis.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J00372; AAB59724.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J00372; AAB59725.1; -; Genomic_DNA.
DR EMBL; AL807387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137690; AAI37691.1; -; mRNA.
DR CCDS; CCDS38685.1; -.
DR PIR; A00645; TVMSM.
DR RefSeq; NP_064405.2; NM_020021.2.
DR AlphaFoldDB; P00536; -.
DR SMR; P00536; -.
DR IntAct; P00536; 1.
DR STRING; 10090.ENSMUSP00000100789; -.
DR iPTMnet; P00536; -.
DR PhosphoSitePlus; P00536; -.
DR PaxDb; P00536; -.
DR PRIDE; P00536; -.
DR Antibodypedia; 24550; 297 antibodies from 27 providers.
DR DNASU; 17451; -.
DR Ensembl; ENSMUST00000105158; ENSMUSP00000100789; ENSMUSG00000078365.
DR GeneID; 17451; -.
DR KEGG; mmu:17451; -.
DR UCSC; uc008rwo.1; mouse.
DR CTD; 4342; -.
DR MGI; MGI:97052; Mos.
DR VEuPathDB; HostDB:ENSMUSG00000078365; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000160233; -.
DR InParanoid; P00536; -.
DR OMA; CKFASGR; -.
DR OrthoDB; 993493at2759; -.
DR BRENDA; 2.7.10.2; 3474.
DR BioGRID-ORCS; 17451; 2 hits in 61 CRISPR screens.
DR ChiTaRS; Mocos; mouse.
DR PRO; PR:P00536; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P00536; protein.
DR Bgee; ENSMUSG00000078365; Expressed in primary oocyte and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0051296; P:establishment of meiotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
DR GO; GO:1902103; P:negative regulation of metaphase/anaphase transition of meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..343
FT /note="Proto-oncogene serine/threonine-protein kinase mos"
FT /id="PRO_0000086345"
FT DOMAIN 63..339
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 198
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 225
FT /note="D -> V (in Ref. 1; AAB59724/AAB59725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37886 MW; 099D3995F2179437 CRC64;
MPSPLSLCRY LPRELSPSVD SRSCSIPLVA PRKAGKLFLG TTPPRAPGLP RRLAWFSIDW
EQVCLMHRLG SGGFGSVYKA TYHGVPVAIK QVNKCTKDLR ASQRSFWAEL NIARLRHDNI
VRVVAASTRT PEDSNSLGTI IMEFGGNVTL HQVIYGATRS PEPLSCREQL SLGKCLKYSL
DVVNGLLFLH SQSILHLDLK PANILISEQD VCKISDFGCS QKLQDLRCRQ ASPHHIGGTY
THQAPEILKG EIATPKADIY SFGITLWQMT TREVPYSGEP QYVQYAVVAY NLRPSLAGAV
FTASLTGKTL QNIIQSCWEA RALQRPGAEL LQRDLKAFRG ALG
