WEE1_ARATH
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 03-AUG-2022, entry version 141.
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.AT1G02970.1; -.
DR PaxDb; Q8L4H0; -.
DR PRIDE; Q8L4H0; -.
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; locus:2024780; AT1G02970.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_000288_25_0_1; -.
DR InParanoid; Q8L4H0; -.
DR OMA; WFENEKL; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; Q8L4H0; -.
DR PRO; PR:Q8L4H0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L4H0; baseline and differential.
DR Genevisible; Q8L4H0; AT.
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: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:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
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 CDD; cd13997; PKc_Wee1_like; 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 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 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
