ID   WEE1A_XENLA             Reviewed;         571 AA.
AC   Q8AYK6; B7ZQE2;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Wee1-like protein kinase 1-A;
DE            EC=2.7.10.2;
DE   AltName: Full=Zygotic wee1-like protein kinase 2;
DE            Short=XWee2;
GN   Name=wee1-a; Synonyms=wee2;
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] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12217326; DOI=10.1006/dbio.2002.0743;
RA   Leise W., Mueller P.R.;
RT   "Multiple Cdk1 inhibitory kinases regulate the cell cycle during
RT   development.";
RL   Dev. Biol. 249:156-173(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=15084456; DOI=10.1242/dev.01054;
RA   Leise W.F. III, Mueller P.R.;
RT   "Inhibition of the cell cycle is required for convergent extension of the
RT   paraxial mesoderm during Xenopus neurulation.";
RL   Development 131:1703-1715(2004).
CC   -!- FUNCTION: Acts as a zygotic negative regulator of entry into mitosis
CC       (G2 to M transition) by protecting the nucleus from cytoplasmically
CC       activated cyclin B1-complexed cdk1 before the onset of mitosis by
CC       mediating phosphorylation of cdk1 on 'Tyr-15'. Specifically
CC       phosphorylates and inactivates cyclin B1-complexed cdk1 reaching a
CC       maximum during G2 phase and a minimum as cells enter M phase.
CC       Phosphorylation of cyclin B1-cdk1 occurs exclusively on 'Tyr-15' and
CC       phosphorylation of monomeric cdk1 does not occur. Involved in
CC       convergent extension of the paraxial mesoderm during neurulation by
CC       inhibiting the cell cycle. {ECO:0000269|PubMed:12217326,
CC       ECO:0000269|PubMed:15084456}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8AYK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8AYK6-2; Sequence=VSP_041323, VSP_041324;
CC   -!- TISSUE SPECIFICITY: Zygotically expressed. Expressed in regions of the
CC       embryo that are devoid of mitotic cells, such as the involuting
CC       mesoderm. {ECO:0000269|PubMed:12217326}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- CAUTION: Was initially assigned as wee2 (PubMed:12217326). However, it
CC       corresponds to the zygotic protein WEE1 in mammals.
CC       {ECO:0000305|PubMed:12217326}.
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DR   EMBL; AF358869; AAN07091.1; -; mRNA.
DR   EMBL; BC169775; AAI69775.1; -; mRNA.
DR   RefSeq; NP_001082306.1; NM_001088837.1. [Q8AYK6-1]
DR   AlphaFoldDB; Q8AYK6; -.
DR   SMR; Q8AYK6; -.
DR   PRIDE; Q8AYK6; -.
DR   GeneID; 398396; -.
DR   KEGG; xla:398396; -.
DR   CTD; 398396; -.
DR   Xenbase; XB-GENE-17338608; wee1.L.
DR   OrthoDB; 1063695at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 398396; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
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   InterPro; IPR017164; Wee1-like_protein_kinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF037281; Wee1-like_protein_kinase; 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   Alternative splicing; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW   Kinase; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..571
FT                   /note="Wee1-like protein kinase 1-A"
FT                   /id="PRO_0000409522"
FT   DOMAIN          224..494
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          500..539
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        36..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..98
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        351
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         230..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         388
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         51
FT                   /note="W -> WE (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_041323"
FT   VAR_SEQ         74..84
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_041324"
SQ   SEQUENCE   571 AA;  63607 MW;  A3E78D020B22BB28 CRC64;
     MSLQPVPHRL LFSDSDDEED GHSTGEDSAF QESDSPVSRL REKQEGPGGS WEEEEGLGSS
     PIKSPGHFFM CDSPTYRDLP PASPPGPAAS PPDCPGTPPH KTFRKLRLFD TPHTPKSLLS
     KARGIGSSAL RFRGGTLFRE AEKLPKPEFT YSTPQVNINP FTPDSLEIQS STGLCRRRKR
     ALLNDSCGED MEGSDCELED EDVRPAKRIP ITESNMKSRY ATEFHELEKI GSGEFGSVFK
     CVKRLDGCIY AIKRSKKPMA GSVDEQNALR EVYAHAVLGQ HPHVVRYYSA WAEDDHMLIQ
     NEYCNGGSLA DAISENYRTM QYFTEPELKD LLLQVARGLK YIHSMSLVHM DIKPSNIFIS
     RITVPNTGVE EGDDEDCGSG NVVYKIGDLG HVTRVSSPQV EEGDSRFLAN EVLQEDYTHL
     AKADIFALAL TVWCAAGAEP FPTNGDQWHE IRQGKLPRVP QLLSQEFVDL IKLMISPDSE
     KRPSSMALVK HSVLLSASRK NAEQLRIELN AEKFKNALLQ KELKKAQIAK AAAEERALFP
     DRIATRSTTQ SNRTTRLIGK KMNRSVSLTI Y