PMY11_CAEEL
ID PMY11_CAEEL Reviewed; 468 AA.
AC Q20085;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.1;
DE EC=2.7.11.1;
DE AltName: Full=Myt1 kinase;
GN Name=wee-1.1; ORFNames=F35H8.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10209262; DOI=10.1016/s0167-4781(99)00027-5;
RA Wilson M.A., Hoch R.V., Ashcroft N.R., Kosinski M.E., Golden A.;
RT "A Caenorhabditis elegans wee1 homolog is expressed in a temporally and
RT spatially restricted pattern during embryonic development.";
RL Biochim. Biophys. Acta 1445:99-109(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M
CC transition) by phosphorylation of the CDK1 kinase. {ECO:0000250}.
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: Nucleus {ECO:0000269|PubMed:10209262}.
CC Note=Observed in the nucleus during prophase and metaphase.
CC -!- TISSUE SPECIFICITY: In the 12-13-cell embryo, expressed in the E
CC blastomere. In the 16-cell embryo, expressed in the eight AB cells.
CC {ECO:0000269|PubMed:10209262}.
CC -!- DEVELOPMENTAL STAGE: Expression is first seen in the 12-13-cell embryo
CC and is last observed in the 16-cell embryo before division.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; Z36752; CAA85329.1; -; Genomic_DNA.
DR PIR; T21824; T21824.
DR RefSeq; NP_496058.1; NM_063657.1.
DR AlphaFoldDB; Q20085; -.
DR SMR; Q20085; -.
DR STRING; 6239.F35H8.7; -.
DR PaxDb; Q20085; -.
DR EnsemblMetazoa; F35H8.7.1; F35H8.7.1; WBGene00006938.
DR GeneID; 192085; -.
DR KEGG; cel:CELE_F35H8.7; -.
DR UCSC; F35H8.7; c. elegans.
DR CTD; 192085; -.
DR WormBase; F35H8.7; CE09940; WBGene00006938; wee-1.1.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000159427; -.
DR HOGENOM; CLU_584270_0_0_1; -.
DR InParanoid; Q20085; -.
DR OMA; EERCIRY; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; Q20085; -.
DR PRO; PR:Q20085; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006938; Expressed in embryonic cell and 11 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; TAS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; 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; Cell cycle; Developmental protein; Differentiation; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..468
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase wee-1.1"
FT /id="PRO_0000086837"
FT DOMAIN 106..357
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 25..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 112..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 54046 MW; CB69A21E2C3C8FD2 CRC64;
MNSVLSNIEK LDTYILRRNE YVAESKDEPN KLNTSRKLEV TTKKNQSNNK KRPPPINKAR
KSLPSIFRRA EENKDSAQII TPTGSKIIGS PLYKRSKSDS FFDHAFNFDK NLGKGSFGEV
VAATCRSTSK KFAIKKIPFS KLSKDQYREA YGHMNIPCHP NIVRFHQAWI DKQILHIQLE
MCDKSLAAYC HGIDWLEDKE LWNVFLDILQ GLGHLHNNFM LHNDIKPDNI FMTKNKVCKL
GDFGLISDMR SEPINNSSNK HYQSEGDGKY CSKEAINGTL SIFSDIFSFG ISILEVGTNI
HLPSYGTGWE PIRKWEIPEE ILEPMSDELR ELVKQMMDKA PTRRPTCSEL MKNHVVKEKL
RIRKQEVEHI PSESQFQPIS YLTTESPLGS RESSCSSIDF LDHFENAEKK TPFVSKLNFD
LEDDEDEYEV FSPPRTPVKK SRYQQTMPEV SPPRKIQKLF QRKNLFDE
