ID   WEE1_ARATH              Reviewed;         500 AA.
AC   Q8L4H0; Q9SRY9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Wee1-like protein kinase;
DE            EC=2.7.10.2;
DE   AltName: Full=Wee1-At;
GN   Name=WEE1; OrderedLocusNames=At1g02970; ORFNames=F22D16.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=12111237; DOI=10.1007/s00425-002-0815-4;
RA   Sorrell D.A., Marchbank A., McMahon K., Dickinson J.R., Rogers H.J.,
RA   Francis D.;
RT   "A WEE1 homologue from Arabidopsis thaliana.";
RL   Planta 215:518-522(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=16856985; DOI=10.1111/j.1365-313x.2006.02820.x;
RA   Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C.,
RA   Uchimiya H., Umeda M.;
RT   "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-
RT   activating kinases in Arabidopsis.";
RL   Plant J. 47:701-710(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION, AND
RP   INTERACTION WITH CDKA-1.
RX   PubMed=17209125; DOI=10.1105/tpc.106.045047;
RA   de Schutter K., Joubes J., Cools T., Verkest A., Corellou F., Babiychuk E.,
RA   van der Schueren E., Beeckman T., Kushnir S., Inze D., de Veylder L.;
RT   "Arabidopsis WEE1 kinase controls cell cycle arrest in response to
RT   activation of the DNA integrity checkpoint.";
RL   Plant Cell 19:211-225(2007).
CC   -!- FUNCTION: Cell cycle regulatory kinase that is not rate-limiting for
CC       cycle progression under normal growth conditions. Transcriptionally
CC       activated upon DNA stress or damage in an ATR- or ATM-dependent manner.
CC       Once activated, inhibits plant growth by arresting dividing cells in
CC       the G2 phase before proceeding into mitosis. Down-regulates CDKA-1 and
CC       CDKD-2 by tyrosine phosphorylation. May target principally CDKA-1.
CC       {ECO:0000269|PubMed:12111237, ECO:0000269|PubMed:16856985,
CC       ECO:0000269|PubMed:17209125}.
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   -!- SUBUNIT: Interacts with CDKA-1, but not with CDKB1-1.
CC       {ECO:0000269|PubMed:17209125}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16856985}.
CC   -!- TISSUE SPECIFICITY: Expressed in shoot apex, vasculatures tissues of
CC       roots and leaves, and developing flowers. {ECO:0000269|PubMed:12111237,
CC       ECO:0000269|PubMed:17209125}.
CC   -!- INDUCTION: By replication blocking agents (hydroxyurea and
CC       aphidicolin). {ECO:0000269|PubMed:17209125}.
CC   -!- DISRUPTION PHENOTYPE: Plants show no obvious cell division or
CC       endoreduplication phenotype when grown under nonstress conditions, but
CC       are hypersensitive to agents that impair DNA replication.
CC       {ECO:0000269|PubMed:17209125}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF02869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB077385; BAC11716.1; -; mRNA.
DR   EMBL; AJ439593; CAD28679.1; -; mRNA.
DR   EMBL; AC009525; AAF02869.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27508.1; -; Genomic_DNA.
DR   PIR; C86160; C86160.
DR   RefSeq; NP_171796.1; NM_100178.3.
DR   AlphaFoldDB; Q8L4H0; -.
DR   SMR; Q8L4H0; -.
DR   BioGRID; 24688; 9.
DR   IntAct; Q8L4H0; 8.
DR   STRING; 3702.Q8L4H0; -.
DR   PaxDb; 3702-AT1G02970-1; -.
DR   ProteomicsDB; 243078; -.
DR   EnsemblPlants; AT1G02970.1; AT1G02970.1; AT1G02970.
DR   GeneID; 839453; -.
DR   Gramene; AT1G02970.1; AT1G02970.1; AT1G02970.
DR   KEGG; ath:AT1G02970; -.
DR   Araport; AT1G02970; -.
DR   TAIR; AT1G02970; WEE1.
DR   eggNOG; KOG0601; Eukaryota.
DR   HOGENOM; CLU_000288_25_0_1; -.
DR   InParanoid; Q8L4H0; -.
DR   OMA; WFENEKL; -.
DR   OrthoDB; 928649at2759; -.
DR   PhylomeDB; Q8L4H0; -.
DR   PRO; PR:Q8L4H0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L4H0; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:InterPro.
DR   GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; IMP:TAIR.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13997; PKc_Wee1_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR045067; PKc_Wee1-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR   PANTHER; PTHR11042:SF185; WEE1-LIKE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q8L4H0; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Magnesium; Metal-binding;
KW   Mitosis; Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..500
FT                   /note="Wee1-like protein kinase"
FT                   /id="PRO_0000295672"
FT   DOMAIN          249..495
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          141..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         255..263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  56530 MW;  7E7C32697B9A9E44 CRC64;
     MFEKNGRTLL AKRKTQGTIK TRASKKIRKM EGTLERHSLL QFGQLSKISF ENRPSSNVAS
     SAFQGLLDSD SSELRNQLGS ADSDANCGEK DFILSQDFFC TPDYITPDNQ NLMSGLDISK
     DHSPCPRSPV KLNTVKSKRC RQESFTGNHS NSTWSSKHRV DEQENDDIDT DEVMGDKLQA
     NQTERTGYVS QAAVALRCRA MPPPCLKNPY VLNQSETATD PFGHQRSKCA SFLPVSTSGD
     GLSRYLTDFH EIRQIGAGHF SRVFKVLKRM DGCLYAVKHS TRKLYLDSER RKAMMEVQAL
     AALGFHENIV GYYSSWFENE QLYIQLELCD HSLSALPKKS SLKVSEREIL VIMHQIAKAL
     HFVHEKGIAH LDVKPDNIYI KNGVCKLGDF GCATRLDKSL PVEEGDARYM PQEILNEDYE
     HLDKVDIFSL GVTVYELIKG SPLTESRNQS LNIKEGKLPL LPGHSLQLQQ LLKTMMDRDP
     KRRPSARELL DHPMFDRIRG
//