WEE2_XENTR
ID WEE2_XENTR Reviewed; 562 AA.
AC A4QNA8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Wee1-like protein kinase 2;
DE EC=2.7.10.2;
GN Name=wee2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) 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 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 -!- 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; BC135215; AAI35216.1; -; mRNA.
DR RefSeq; NP_001096499.1; NM_001103029.1.
DR RefSeq; XP_012814794.1; XM_012959340.2.
DR AlphaFoldDB; A4QNA8; -.
DR SMR; A4QNA8; -.
DR STRING; 8364.ENSXETP00000060361; -.
DR PaxDb; A4QNA8; -.
DR PRIDE; A4QNA8; -.
DR GeneID; 100125126; -.
DR KEGG; xtr:100125126; -.
DR CTD; 494551; -.
DR Xenbase; XB-GENE-5560750; wee2.
DR eggNOG; KOG0601; Eukaryota.
DR InParanoid; A4QNA8; -.
DR OrthoDB; 1063695at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000031988; Expressed in 2-cell stage embryo and 9 other tissues.
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 ATP-binding; Coiled coil; Kinase; Magnesium; Meiosis; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..562
FT /note="Wee1-like protein kinase 2"
FT /id="PRO_0000409531"
FT DOMAIN 217..491
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 494..520
FT /evidence="ECO:0000255"
FT COMPBIAS 31..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 223..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 62352 MW; A3196C6BDB9CC54F CRC64;
MRTAMSCGGG LAQRLDFSSS DEEDGMSPGL EEGSHSNQRG SPVNSWRANN CPFPITPQRN
ERGLSPSQEE LSPCSDYSPV PSDKGVGGEC PGTPLHYSTW KKLKLCDTPY TPKSLLYKTL
PSPGSRVQCR GQRLLRFVAG TGAELDDPAL VNVNPFTPES YRQANFHPNG KRKERPEDDC
SAEPQMKYAE KEHPAVFQSK RFVLRETNMV SRYKTEFLEI EKIGAGEFGS VFKCVKRLDG
CFYAIKRSKK PLAGSTDEQL ALREVYAHAV LGHHPHVVRY YSAWAEDDHM IIQNEYCNGG
SLQDLIMENK KEGRFVPEQE LKEILLQVSM GLKYIHSSGL VHMDIKPSNI FICRKQTEVG
QDESDGEDDL SSASVLYKIG DLGHVTSILN PQVEEGDSRF LANEILQEDY RQLPKADIFA
LGLTITLAAG AGPLPCNEDS WHHIRKGNLP HIPQPLTPAF LALLKLLVHP DPVMRPPAVS
LAKNSLLRRC VGKAAQLQKQ LNVEKFKTAM LERELKAAKL AHGSGKDECS DLPPMSDFSC
RGRKRLVGAK NARSLSFTCG GY
