WEE2_PIG
ID WEE2_PIG Reviewed; 565 AA.
AC A4PES0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 97.
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;
DE Short=pWee1B;
DE Short=pigWee1B;
GN Name=WEE2; Synonyms=WEE1B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19633431; DOI=10.4161/cc.8.15.9073;
RA Shimaoka T., Nishimura T., Kano K., Naito K.;
RT "Critical effect of pigWee1B on the regulation of meiotic resumption in
RT porcine immature oocytes.";
RL Cell Cycle 8:2375-2384(2009).
RN [2]
RP INVOLVEMENT IN SMALL OOCYTES.
RX PubMed=19550110; DOI=10.1262/jrd.09-072a;
RA Nishimura T., Shimaoka T., Kano K., Naito K.;
RT "Insufficient amount of Cdc2 and continuous activation of Wee1 B are the
RT cause of meiotic failure in porcine growing oocytes.";
RL J. Reprod. Dev. 55:553-557(2009).
RN [3]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF SER-77;
RP SER-118; SER-133; SER-149 AND 174-ARG-LYS-175.
RX PubMed=21123961; DOI=10.1262/jrd.10-122h;
RA Shimaoka T., Nishimura T., Kano K., Naito K.;
RT "Analyses of the regulatory mechanism of porcine WEE1B: the phosphorylation
RT sites of porcine WEE1B and mouse WEE1B are different.";
RL J. Reprod. Dev. 57:223-228(2011).
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. {ECO:0000269|PubMed:19633431}.
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:0000269|PubMed:21123961}.
CC -!- TISSUE SPECIFICITY: Ovary-specific. {ECO:0000269|PubMed:19633431}.
CC -!- DEVELOPMENTAL STAGE: Detected only in the oocytes throughout oocyte
CC maturation period. {ECO:0000269|PubMed:19633431}.
CC -!- PTM: Phosphorylation leads to increase its activity.
CC {ECO:0000269|PubMed:21123961}.
CC -!- MISCELLANEOUS: Continuous activation of WEE2 is a cause of meiotic
CC failure of small oocytes. In mammals, oocytes with a diameter less than
CC 80% of that of full-grown oocytes cannot start meiotic maturation
CC (PubMed:19550110). {ECO:0000305|PubMed:19550110}.
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=BAF56108.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB276373; BAF56108.1; ALT_INIT; mRNA.
DR RefSeq; NP_001090976.2; NM_001097507.2.
DR RefSeq; XP_005673170.1; XM_005673113.2.
DR AlphaFoldDB; A4PES0; -.
DR SMR; A4PES0; -.
DR STRING; 9823.ENSSSCP00000017471; -.
DR iPTMnet; A4PES0; -.
DR PaxDb; A4PES0; -.
DR PRIDE; A4PES0; -.
DR Ensembl; ENSSSCT00025041339; ENSSSCP00025017581; ENSSSCG00025030428.
DR Ensembl; ENSSSCT00070043086; ENSSSCP00070036248; ENSSSCG00070021693.
DR GeneID; 100048934; -.
DR KEGG; ssc:100048934; -.
DR CTD; 494551; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_000288_25_1_1; -.
DR InParanoid; A4PES0; -.
DR TreeFam; TF101088; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 18.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0004713; F:protein tyrosine kinase activity; TAS:UniProtKB.
DR GO; GO:0007143; P:female meiotic nuclear division; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:1904145; P:negative regulation of meiotic cell cycle process involved in oocyte maturation; IMP:AgBase.
DR GO; GO:0060283; P:negative regulation of oocyte development; IDA: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; IDA: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 1: Evidence at protein level;
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_0000409526"
FT DOMAIN 214..492
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..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 MOTIF 317..331
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..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 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21123961"
FT MUTAGEN 77
FT /note="S->A: Abolishes phosphorylation and ability to
FT maintain meiotic arrest in oocytes during the germinal
FT vesicle (GV) stage."
FT /evidence="ECO:0000269|PubMed:21123961"
FT MUTAGEN 118
FT /note="S->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:21123961"
FT MUTAGEN 133
FT /note="S->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:21123961"
FT MUTAGEN 149
FT /note="S->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:21123961"
FT MUTAGEN 174..175
FT /note="RK->TT: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:21123961"
SQ SEQUENCE 565 AA; 62928 MW; 2855273D6B1548BC CRC64;
MGDNGDNKEL KQKLNFSYSE EEQEDEGQKE AQESKKVQYH TPERCGHQDS EAKFTPPRTP
LNHVCELSTP QVKDRASPDQ GLRTPVSRPH TRPETPAPPD KSKPPPHCES PFTPRGHSSQ
SVISTGKLPS RGSKHLRLTP GPLTDEMTSL ALVNINPFTP ESYRRQFLKS NGKRKTRRDL
EEAGPEEGKV EKGLPAKRCV LRETNMACRY EKEFLEVEKI GVGEFGTVYK CIKRLDGCVY
AIKRSTKPVS GLSDENLAMH EVYAHSVLGH HPHVVRYYSS WAEDDHMMIQ NEYCNGGSLQ
AAISENAKSG NHFQEPKLKD ILLQISLGLK YIHNYGMVHM DIKPSNIFIC HKIPSDSPVV
PEEAENEADW FLSANVTYKI GDLGHVTSIS EPQVEEGDSR FLAKEILQEN YQHLPKADIF
ALGLTIAVAA GAEALPTNGT SWHHIREGQL PNIPQDLSKE FYNLLKDMID PDPVARPSAA
ALTRSRVLCP SLGRTEELQQ QLNLEKFKTA TLERELKEVQ RAQSSKEGQS SPGVTGTHTG
SRSTRRLVGG KSAKSSSFTW GQSSP
