MOS_XENLA
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 03-AUG-2022, entry version 117.
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 -!- 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 -!- 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 CTD; 397924; -.
DR Xenbase; XB-GENE-1011507; mos.L.
DR OrthoDB; 993493at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397924; Expressed in blastula and 19 other 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 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..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