PMY13_CAEBR
ID PMY13_CAEBR Reviewed; 656 AA.
AC Q626B1; A8WP04;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.3;
DE EC=2.7.11.1;
GN Name=wee-1.3 {ECO:0000250|UniProtKB:O18209}; ORFNames=CBG01053;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M
CC transition) by phosphorylation of the CDK1 kinase during oocyte
CC maturation. Required for embryonic development, germline proliferation
CC and initiation of meiosis during spermatogenesis. Required for
CC chromosome structure during mitosis and negative regulation of nuclear
CC envelope breakdown (By similarity). {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 Evidence={ECO:0000250|UniProtKB:O18209};
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; Evidence={ECO:0000250|UniProtKB:O18209};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cytoplasm
CC {ECO:0000250|UniProtKB:O18209}.
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; HE600951; CAP22210.1; -; Genomic_DNA.
DR RefSeq; XP_002629809.1; XM_002629763.1.
DR AlphaFoldDB; Q626B1; -.
DR SMR; Q626B1; -.
DR STRING; 6238.CBG01053; -.
DR EnsemblMetazoa; CBG01053a.1; CBG01053a.1; WBGene00024344.
DR GeneID; 8573224; -.
DR KEGG; cbr:CBG_01053; -.
DR CTD; 8573224; -.
DR WormBase; CBG01053a; CBP13925; WBGene00024344; Cbr-wee-1.3.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_406103_0_0_1; -.
DR InParanoid; Q626B1; -.
DR OMA; ESHMIIP; -.
DR OrthoDB; 1063695at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cytoplasm; Developmental protein; Differentiation;
KW Golgi apparatus; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Oogenesis; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase.
FT CHAIN 1..656
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase wee-1.3"
FT /id="PRO_0000282348"
FT DOMAIN 107..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 656 AA; 75018 MW; F27A3C9B85EE1CFD CRC64;
MDETENNTSI DSVEVGPSSP RVVATPRIPI PVMMRETPLS TKRERQALTP RFRRPAPRMI
KTVPQTRSIW SVRKDTTPQL VTPHGPQELE SPHYDRANTQ TFFEQVFQID EIIGRGSFGE
VFAARCREDS RLYAVKVSIA PMRQHSMSKY REAESHMIIP PHKNLVKFYR AWEETDRLYI
QTELCEQSLQ QYCSVQHALP ENEIWNIFVD LLEAVHHLHS NDMIHDDIKP ENIFLTKHKI
CKLGDFGLVI NLKNPNDVKS AEEGDSKYLA PEVLNGKPTF ASDIFSLGVT ILEAATDLDV
PSNGDAWHQI RNGQIPERFF VGISSDLRVL IEQMINKEPM KRPTSDALRK HLSIRTRLDS
RRRYILSMDM RDGFCNLMSS ILVWCMAFLS VVFHPVTRFH EAINNRRSEL CAQFVNNQQH
TPIQTPETSK VYSESLTGVA LRQASQISPF DFSDDENPPH SQRRLFTGPV SRRLNFDDEM
EDEEQATCSS SNSSAIETAE DSLSSPKKPV IPVTRQGTPK SARRLIPSYR NRSGSRDPTH
HAGAGDSMNS SILDQERTDR YLRMRLAEQQ LDWNDHSNMI DEAPPPMSCP PRIRRSLRDM
PRMPVLNFNL LDEPIKKGKE KPVVEPAELR QRPMRNGLKS LRSRMASFQG SSGDEN
