WEE2_DANRE
ID WEE2_DANRE Reviewed; 532 AA.
AC Q1LX51; A4IFZ5; Q1LX50; Q32PP5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Wee1-like protein kinase 2;
DE EC=2.7.10.2;
DE AltName: Full=Wee1-like protein kinase 1B;
DE AltName: Full=Wee1B kinase;
GN Name=wee2; Synonyms=wee1b; ORFNames=si:ch211-238n5.5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Egg, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates
CC and inhibits cdk1 and acts as a key regulator of meiosis. Required to
CC maintain meiotic arrest in oocytes by phosphorylating cdk1 at 'Tyr-15',
CC leading to inhibit cdk1 activity and prevent meiotic reentry (By
CC similarity). {ECO:0000250}.
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=Q1LX51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1LX51-2; Sequence=VSP_041325;
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; BX470166; CAK04661.1; -; Genomic_DNA.
DR EMBL; BX470166; CAK04662.1; -; Genomic_DNA.
DR EMBL; BC108038; AAI08039.1; -; mRNA.
DR EMBL; BC134853; AAI34854.1; -; mRNA.
DR RefSeq; NP_001032299.2; NM_001037222.2. [Q1LX51-2]
DR RefSeq; NP_001038367.1; NM_001044902.1. [Q1LX51-1]
DR RefSeq; XP_017207393.1; XM_017351904.1.
DR AlphaFoldDB; Q1LX51; -.
DR SMR; Q1LX51; -.
DR STRING; 7955.ENSDARP00000109848; -.
DR PaxDb; Q1LX51; -.
DR Ensembl; ENSDART00000040074; ENSDARP00000040073; ENSDARG00000012718. [Q1LX51-2]
DR Ensembl; ENSDART00000121699; ENSDARP00000109848; ENSDARG00000012718. [Q1LX51-1]
DR Ensembl; ENSDART00000136710; ENSDARP00000121512; ENSDARG00000012718. [Q1LX51-2]
DR GeneID; 327471; -.
DR KEGG; dre:327471; -.
DR CTD; 494551; -.
DR ZFIN; ZDB-GENE-030131-5682; wee2.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000158803; -.
DR InParanoid; Q1LX51; -.
DR OMA; GAAWHHI; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; Q1LX51; -.
DR TreeFam; TF101088; -.
DR PRO; PR:Q1LX51; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000012718; Expressed in mature ovarian follicle and 19 other tissues.
DR ExpressionAtlas; Q1LX51; baseline.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0060631; P:regulation of meiosis I; 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 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; Coiled coil; Kinase; Magnesium; Meiosis;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..532
FT /note="Wee1-like protein kinase 2"
FT /id="PRO_0000409528"
FT DOMAIN 188..465
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 123..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..495
FT /evidence="ECO:0000255"
FT COMPBIAS 132..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 194..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..5
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041325"
FT CONFLICT 17
FT /note="N -> S (in Ref. 2; AAI08039)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="K -> R (in Ref. 2; AAI34854)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="T -> P (in Ref. 2; AAI08039/AAI34854)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="N -> S (in Ref. 2; AAI08039/AAI34854)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="C -> R (in Ref. 2; AAI08039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 532 AA; 59774 MW; 2192E4A0F6113D3C CRC64;
MKWSEMASVN ATQQHLNFSS SWEEDSSDNS FDEWTHKSVP LRSPCRTPRI QRHRNRSITV
SPSVPTSPIP YAAWKKLRLC DSPSTPKSLL SKSTMPCSSS KTCRSQRFLR LSTAFERVPS
VNINPFTPDT VRRNSEHYKR KSQRSDDDED YGPRSKEIQN SSEDESFFLP SKRPAVSARM
LSRYESEFLE LACIGVGEFG SVYRCVKRLD GCMYAIKRSR RPIAGSANEQ LALKEVYAHA
VLGHHPHVVR YYSAWAEDDH MIIQNEYCDG GSLHDAITEK REQGEFFSVP ELRDLLLQVS
MGLKYIHNSG LVHLDIKPSN IFICRRSTLS AGGEGDSEEE DESHSSGVVY KIGDLGHVTS
ISSPQVEEGD SRFLAYEVLR EDYTHLPKAD IFALGLTVLL AAGASPLPQN GDDWHRLRQG
ELPNLPHELP ALFKDLLKSL LDPDPTARPS ATALCRHDVL CKERAGKLAT QLRKELNVEK
FRTAMLEREL KEARLAATSP QQSCQPGSLP KAKRKLVGRN VARSVSFGFP GY
