WEE2_AILME
ID WEE2_AILME Reviewed; 565 AA.
AC D2HHP1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=PANDA_010640;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates
CC and inhibits CDK1 and acts as a key regulator of meiosis during both
CC prophase I and metaphase II. Required to maintain meiotic arrest in
CC oocytes during the germinal vesicle (GV) stage, a long period of
CC quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15',
CC leading to inhibit CDK1 activity and prevent meiotic reentry. Also
CC required for metaphase II exit during egg activation by phosphorylating
CC CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote
CC pronuclear formation (By 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 -!- PTM: Phosphorylation leads to increase its activity. {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; GL192847; EFB29558.1; -; Genomic_DNA.
DR RefSeq; XP_002921735.1; XM_002921689.3.
DR AlphaFoldDB; D2HHP1; -.
DR SMR; D2HHP1; -.
DR STRING; 9646.ENSAMEP00000015995; -.
DR GeneID; 100468598; -.
DR KEGG; aml:100468598; -.
DR CTD; 494551; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_000288_25_1_1; -.
DR InParanoid; D2HHP1; -.
DR OMA; GAAWHHI; -.
DR OrthoDB; 1063695at2759; -.
DR TreeFam; TF101088; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0007143; P:female meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0035038; P:female pronucleus assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; ISS:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0080154; P:regulation of fertilization; ISS:UniProtKB.
DR GO; GO:0060631; P:regulation of meiosis I; ISS:UniProtKB.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Meiosis; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..565
FT /note="Wee1-like protein kinase 2"
FT /id="PRO_0000409524"
FT DOMAIN 214..492
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 18..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 495..521
FT /evidence="ECO:0000255"
FT MOTIF 173..175
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 317..331
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 29..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 220..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A4PES0"
SQ SEQUENCE 565 AA; 62913 MW; E5B24F2A1D99F606 CRC64;
MDDSSINKEL KQKLNFSYCE EESESEGQEA WETRDAHSQI PDRAEGQESE AKFTPPGPPL
SSVHEVGTFQ EKTKKSPEQV LMTPVSGFRN YPETPAQPDS RSKLLDCESP FTPKGLLSQS
VISSTEKIPS RGSKHLRFTP VPFVDEMTSS ALVNINPFTP ESYRKQFLKS NGKRKTRGDF
EEAGPGEGNV EQGLPAKRCV LQETNMASRY EKEFLEVEKI GVGEFGTVYK CIKRLDGCVY
AIKRSTKPFA GLSNENLALH EVYAHAVLGH HPHVVRYYSA WAEDDHMIIQ NEYCNGGSLQ
TAISENTKSG NHFQEPKLKD ILLQISLGLK YIHSSGMVHL DIKPSNIFIC HKMQSDSPVV
PEEIENEADW FLSANVMYKI GDLGHVTSIS KPKVEEGDSR FLANEILQED YQHLPKADIF
ALGLTIAVAA GAESLPTNGA AWHHIREGKL PDIPQKLSEE FYNLLKNMIH PDPRERPSAA
ALARSRVLRP SLGKAEELQQ QLNLEKFKTA TLERELREAQ QAWFSQEERG DAGVSGTPTG
SRSTKRLVGG KSAKSSSFTW GKSSP
