PMY13_CAEEL
ID PMY13_CAEEL Reviewed; 677 AA.
AC O18209;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase wee-1.3;
DE EC=2.7.11.1;
DE AltName: Full=Lethal protein 37;
DE AltName: Full=Myt1 kinase;
GN Name=wee-1.3; Synonyms=let-37, myt-1, spe-37; ORFNames=Y53C12A.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11702779; DOI=10.1016/s1534-5807(01)00026-0;
RA Detwiler M.R., Reuben M., Li X., Rogers E., Lin R.;
RT "Two zinc finger proteins, OMA-1 and OMA-2, are redundantly required for
RT oocyte maturation in C. elegans.";
RL Dev. Cell 1:187-199(2001).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PHE-103; ILE-160;
RP HIS-163; GLY-245; GLY-558; GLY-560 AND ASP-561.
RX PubMed=12397109; DOI=10.1242/dev.129.21.5009;
RA Lamitina S.T., L'Hernault S.W.;
RT "Dominant mutations in the Caenorhabditis elegans Myt1 ortholog wee-1.3
RT reveal a novel domain that controls M-phase entry during spermatogenesis.";
RL Development 129:5009-5018(2002).
RN [4]
RP FUNCTION.
RX PubMed=16338136; DOI=10.1016/j.cub.2005.11.063;
RA Stitzel M.L., Pellettieri J., Seydoux G.;
RT "The C. elegans DYRK Kinase MBK-2 marks oocyte proteins for degradation in
RT response to meiotic maturation.";
RL Curr. Biol. 16:56-62(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16421191; DOI=10.1242/dev.02241;
RA Burrows A.E., Sceurman B.K., Kosinski M.E., Richie C.T., Sadler P.L.,
RA Schumacher J.M., Golden A.;
RT "The C. elegans Myt1 ortholog is required for the proper timing of oocyte
RT maturation.";
RL Development 133:697-709(2006).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16466390; DOI=10.1111/j.1440-169x.2006.00841.x;
RA Inoue T., Hirata K., Kuwana Y., Fujita M., Miwa J., Roy R., Yamaguchi Y.;
RT "Cell cycle control by daf-21/Hsp90 at the first meiotic prophase/metaphase
RT boundary during oogenesis in Caenorhabditis elegans.";
RL Dev. Growth Differ. 48:25-32(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27104746; DOI=10.1080/15384101.2016.1146839;
RA Lee Y.U., Son M., Kim J., Shim Y.H., Kawasaki I.;
RT "CDC-25.2, a C. elegans ortholog of cdc25, is essential for the progression
RT of intestinal divisions.";
RL Cell Cycle 15:654-666(2016).
CC -!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M
CC transition) by phosphorylation of the CDK1 kinase during oocyte
CC maturation (PubMed:16338136, PubMed:16421191, PubMed:16466390).
CC Required for oocyte maturation, embryonic development, germline
CC proliferation and initiation of meiosis during spermatogenesis
CC (PubMed:11702779, PubMed:12397109, PubMed:27104746). Required for
CC chromosome structure during mitosis and negative regulation of nuclear
CC envelope breakdown (PubMed:16421191). {ECO:0000269|PubMed:11702779,
CC ECO:0000269|PubMed:12397109, ECO:0000269|PubMed:16338136,
CC ECO:0000269|PubMed:16421191, ECO:0000269|PubMed:16466390,
CC ECO:0000269|PubMed:27104746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:16466390}.
CC -!- DEVELOPMENTAL STAGE: Expressed during both germline and early embryonic
CC development. In larvae, it is expressed in the distal region, germline,
CC and in some neurons and hypodermal cells. Not expressed in distal
CC region of the adult. {ECO:0000269|PubMed:12397109}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit oocytes that mature prematurely
CC (also known as the Emo phenotype) and chromosomes that appear condensed
CC (PubMed:16421191). Subcellular defects include irregular perinuclear
CC foci in oocytes (PubMed:16421191). RNAi-mediated knockdown results in
CC an accumulation of damaged, compressed, polyploid oocytes in the uterus
CC (PubMed:11702779). RNAi-mediated knockdown in a double oma-1 and oma-2
CC knockout background allows for the progression of meiosis beyond the
CC prophase stage and oocyte maturation, but these oocytes cannot be
CC fertilized (PubMed:11702779). RNAi-mediated knockdown in a cdc-25.2
CC mutant background suppresses the defect in intestinal cell divisions in
CC the cdc-25.2 single mutant (PubMed:27104746).
CC {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:16421191,
CC ECO:0000269|PubMed:27104746}.
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; Z99277; CAB16484.1; -; Genomic_DNA.
DR PIR; T27127; T27127.
DR RefSeq; NP_496095.1; NM_063694.4.
DR AlphaFoldDB; O18209; -.
DR SMR; O18209; -.
DR BioGRID; 39853; 10.
DR DIP; DIP-24649N; -.
DR IntAct; O18209; 1.
DR STRING; 6239.Y53C12A.1; -.
DR EPD; O18209; -.
DR PaxDb; O18209; -.
DR EnsemblMetazoa; Y53C12A.1.1; Y53C12A.1.1; WBGene00006940.
DR GeneID; 174531; -.
DR KEGG; cel:CELE_Y53C12A.1; -.
DR UCSC; Y53C12A.1; c. elegans.
DR CTD; 174531; -.
DR WormBase; Y53C12A.1; CE14884; WBGene00006940; wee-1.3.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000159427; -.
DR HOGENOM; CLU_406103_0_0_1; -.
DR InParanoid; O18209; -.
DR OMA; ESHMIIP; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; O18209; -.
DR Reactome; R-CEL-156711; Polo-like kinase mediated events.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-CEL-69478; G2/M DNA replication checkpoint.
DR PRO; PR:O18209; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006940; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; TAS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IGI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0051078; P:meiotic nuclear membrane disassembly; IMP:UniProtKB.
DR GO; GO:1904145; P:negative regulation of meiotic cell cycle process involved in oocyte maturation; IMP:UniProtKB.
DR GO; GO:0060280; P:negative regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 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; Cytoplasm; Developmental protein; Differentiation;
KW Golgi apparatus; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Oogenesis; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Transferase.
FT CHAIN 1..677
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase wee-1.3"
FT /id="PRO_0000086576"
FT DOMAIN 108..355
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 114..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 103
FT /note="F->I: In eb94; viable but induces male sterility due
FT to abnormal sperm."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 160
FT /note="I->N: In eb62; viable but induces male sterility due
FT to abnormal sperm."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 163
FT /note="H->P: In eb90; induces inviable embryos and larvae."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 245
FT /note="G->E: In eb88; induces inviable embryos and larvae."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 558
FT /note="G->R: In eb95; induces defects in spermatogenesis."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 560
FT /note="G->E: In hc144; induces defects in spermatogenesis."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 560
FT /note="G->R: In q89; dominant allele that induces an arrest
FT of spermatogenesis at early stages."
FT /evidence="ECO:0000269|PubMed:12397109"
FT MUTAGEN 561
FT /note="D->N: In hc145; induces defects in spermatogenesis."
FT /evidence="ECO:0000269|PubMed:12397109"
SQ SEQUENCE 677 AA; 76967 MW; D1F35F551E30CEA9 CRC64;
MDDTEGNSSM DSIRNGQSSP LPQVTPRLPQ IPMMMRETPL STKRERQAIT PRFRRPAPKM
IKTMPPTRSI WSVRKESVPL LVTPQGPKPL ESPKYDHTNA QSFFEQVFQI DEIIGRGSFG
EVFAARCRED SQLYAVKVSL APIRQHSISK YREAESHMII PPHKNLVKFY RAWEETGRLY
IQTELCDQSL LKYCTEKHAL PEDEIWNIFV DLLQAVHHLH SNDMIHDDIK PENIFLTKDM
ICKLGDFGLV INLKNPNDVK SAEEGDSKYL APEVLNGRPT KSSDIFSLGM TILEATTDLD
VPSNGDSWHQ IRNGQIPDRF FAGISTDLRS LIALMLDSDP RIRPTSRDLL DHPVIKKKLM
KRGTYVKCIS ILNGFFYAFS AVLVWVMAFF SVLFHPIVRF HAAIKDRQSE ICAQFVNNQQ
HTPIQTPETS KVYLESLTGV AVRQASQIVS PFDFSDDENP PNAQRRLFTG AVPCRLNFDN
DQDDDEEQAT CSSSNSSAIE PQLDEPESPP RMNDVIDKLG KRGTPRSARR NLTFNRHRQV
AASVAPKSSL NHYNHHTGSG DGFSNNSLIP ISDQERTEKY LRMRLTEQQL DWADQNNVID
EAPPPMSCPP RIRRSIRDLP RMPVLNFNVL DEPSNKPTVD HHTILEQSES PRRRLNRGAK
PVPRNRMMSF GSSGDEV
