MPK1_CAEEL
ID MPK1_CAEEL Reviewed; 444 AA.
AC P39745; Q9U3F3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Mitogen-activated protein kinase mpk-1;
DE EC=2.7.11.24 {ECO:0000269|PubMed:20624915};
DE AltName: Full=MAP kinase sur-1;
GN Name=mpk-1; Synonyms=sur-1; ORFNames=F43C1.2;
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 [MRNA] (ISOFORM B), AND MUTAGENESIS OF ALA-106.
RC STRAIN=Bristol N2;
RX PubMed=8299935; DOI=10.1101/gad.8.2.147;
RA Wu Y., Han M.;
RT "Suppression of activated Let-60 ras protein defines a role of
RT Caenorhabditis elegans Sur-1 MAP kinase in vulval differentiation.";
RL Genes Dev. 8:147-159(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=8299936; DOI=10.1101/gad.8.2.160;
RA Lackner M.R., Kornfeld K., Miller L.M., Horvitz H.R., Kim S.K.;
RT "A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of
RT vulval cell fates in Caenorhabditis elegans.";
RL Genes Dev. 8:160-173(1994).
RN [3]
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 [4]
RP FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=11689700; DOI=10.1128/mcb.21.23.8104-8116.2001;
RA Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
RA Stern M.J.;
RT "The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like
RT multisubstrate adaptor protein in fibroblast growth factor signal
RT transduction.";
RL Mol. Cell. Biol. 21:8104-8116(2001).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ALA-106.
RX PubMed=15268855; DOI=10.1016/j.cub.2004.07.022;
RA Nicholas H.R., Hodgkin J.;
RT "The ERK MAP kinase cascade mediates tail swelling and a protective
RT response to rectal infection in C. elegans.";
RL Curr. Biol. 14:1256-1261(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16319922; DOI=10.1038/sj.emboj.7600901;
RA Lee M.H., Hook B., Lamont L.B., Wickens M., Kimble J.;
RT "LIP-1 phosphatase controls the extent of germline proliferation in
RT Caenorhabditis elegans.";
RL EMBO J. 25:88-96(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF VAL-216.
RX PubMed=17096596; DOI=10.1371/journal.pgen.0020174;
RA Leacock S.W., Reinke V.;
RT "Expression profiling of MAP kinase-mediated meiotic progression in
RT Caenorhabditis elegans.";
RL PLoS Genet. 2:e174-e174(2006).
RN [8]
RP FUNCTION, INTERACTION WITH GCK-1, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT
RP THR-256 AND TYR-258, AND DISRUPTION PHENOTYPE.
RX PubMed=19826475; DOI=10.1371/journal.pone.0007450;
RA Schouest K.R., Kurasawa Y., Furuta T., Hisamoto N., Matsumoto K.,
RA Schumacher J.M.;
RT "The germinal center kinase GCK-1 is a negative regulator of MAP kinase
RT activation and apoptosis in the C. elegans germline.";
RL PLoS ONE 4:E7450-E7450(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION AT THR-256 AND TYR-258, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20624915; DOI=10.1074/jbc.m110.146274;
RA Okuyama T., Inoue H., Ookuma S., Satoh T., Kano K., Honjoh S., Hisamoto N.,
RA Matsumoto K., Nishida E.;
RT "The ERK-MAPK pathway regulates longevity through SKN-1 and insulin-like
RT signaling in Caenorhabditis elegans.";
RL J. Biol. Chem. 285:30274-30281(2010).
RN [10]
RP FUNCTION.
RX PubMed=21160027; DOI=10.1152/ajpcell.00343.2010;
RA Falin R.A., Miyazaki H., Strange K.;
RT "C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion channel
RT activity is regulated by WNK-independent ERK kinase signaling.";
RL Am. J. Physiol. 300:C624-635(2011).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP PHOSPHORYLATION AT THR-256 AND TYR-258, AND MUTAGENESIS OF VAL-216.
RX PubMed=21901106; DOI=10.1371/journal.pgen.1002238;
RA Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M., Keyse S.M.,
RA Gartner A.;
RT "Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell
RT apoptosis by Ras/MAPK signaling.";
RL PLoS Genet. 7:E1002238-E1002238(2011).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT
RP THR-256 AND TYR-258, AND DISRUPTION PHENOTYPE.
RX PubMed=22820175; DOI=10.1016/j.bbamcr.2012.07.006;
RA Cha D.S., Datla U.S., Hollis S.E., Kimble J., Lee M.H.;
RT "The Ras-ERK MAPK regulatory network controls dedifferentiation in
RT Caenorhabditis elegans germline.";
RL Biochim. Biophys. Acta 1823:1847-1855(2012).
RN [13]
RP FUNCTION, MUTAGENESIS OF ALA-106, AND DISRUPTION PHENOTYPE.
RX PubMed=27525822; DOI=10.1371/journal.ppat.1005826;
RA Gravato-Nobre M.J., Vaz F., Filipe S., Chalmers R., Hodgkin J.;
RT "The invertebrate lysozyme effector ILYS-3 is systemically activated in
RT response to danger signals and confers antimicrobial protection in C.
RT elegans.";
RL PLoS Pathog. 12:E1005826-E1005826(2016).
CC -!- FUNCTION: Functions in let-60 Ras signaling pathway; acts downstream of
CC lin-45 raf kinase, but before the lin-1 gene product in controlling
CC vulval cell differentiation (PubMed:8299935, PubMed:8299936). Plays a
CC negative role in proximal germline proliferation in the mitotic zone
CC (PubMed:16319922). Required for progression of developing oocytes
CC through the pachytene stage, perhaps acting after efl-1/dpl-1-mediated
CC gene activation and before gld-1 down-regulation (PubMed:16319922,
CC PubMed:19826475, PubMed:21901106, PubMed:17096596). May play a role in
CC global X chromosome reactivation or be indirectly required for
CC progression of germ cells through meiosis to the point where X
CC reactivation occurs (PubMed:17096596). In oocytes, inhibits the
CC activity of the chloride channel clh-3, likely by activating gck-3
CC (PubMed:21160027). Plays a role in response to M.nematophilum-mediated
CC bacterial infection by promoting tail swelling and preventing
CC constipation (PubMed:15268855). Involved in fluid homeostasis
CC (PubMed:11689700). In addition, involved in the up-regulation of
CC lysozyme ilys-3 expression in the intestine in responses to
CC M.nematophilum-mediated bacterial infection (PubMed:27525822). By
CC phosphorylating transcription factor skn-1 (isoform c) may play a role
CC in increasing life span downstream of lin-45, let-60 and mek-2
CC (PubMed:20624915). By up-regulating cep-1 and down-regulating gld-1
CC expression in the late pachytene stage, plays a role in germline
CC apoptosis in response to DNA damage (PubMed:21901106). Regulates egl-1
CC expression in response to DNA damage, probably upstream of cep-1
CC (PubMed:21901106). {ECO:0000269|PubMed:11689700,
CC ECO:0000269|PubMed:15268855, ECO:0000269|PubMed:16319922,
CC ECO:0000269|PubMed:19826475, ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:21160027, ECO:0000269|PubMed:21901106,
CC ECO:0000269|PubMed:27525822, ECO:0000269|PubMed:8299935,
CC ECO:0000269|PubMed:8299936}.
CC -!- FUNCTION: [Isoform b]: Suppresses germline tumor formation by
CC preventing the dedifferentiation of secondary spermatocytes probably
CC upstream of rskn-1. {ECO:0000269|PubMed:22820175}.
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=2.7.11.24;
CC Evidence={ECO:0000269|PubMed:20624915};
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=2.7.11.24; Evidence={ECO:0000269|PubMed:20624915};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20624915};
CC -!- ACTIVITY REGULATION: Activated by dual phosphorylation at Thr-256 and
CC Tyr-258 (PubMed:20624915). May be inactivated by lip-1-mediated
CC dephosphorylation (PubMed:21901106). {ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:21901106}.
CC -!- SUBUNIT: Isoform a interacts with gck-1 (via N-terminus).
CC {ECO:0000269|PubMed:19826475}.
CC -!- INTERACTION:
CC P39745; O02289: gla-3; NbExp=3; IntAct=EBI-321013, EBI-317795;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P39745-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P39745-2; Sequence=VSP_004848;
CC -!- TISSUE SPECIFICITY: Expressed in cells lining the rectum
CC (PubMed:15268855, PubMed:20624915). Isoform a is expressed in nervous
CC system, body wall muscles and posterior intestine (PubMed:20624915).
CC Isoform b expression may be restricted to germline (PubMed:22820175).
CC {ECO:0000269|PubMed:15268855, ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:22820175}.
CC -!- DEVELOPMENTAL STAGE: The phosphorylated form is present in early to mid
CC pachytene, is absent in late pachytene and diplotene/diakinesis stages
CC and is again present in oocytes when they reach the spermatheca
CC (PubMed:19826475, PubMed:21901106, PubMed:22820175). The phosphorylated
CC form is also present in sperm (PubMed:22820175).
CC {ECO:0000269|PubMed:19826475, ECO:0000269|PubMed:21901106,
CC ECO:0000269|PubMed:22820175}.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Isoform a is phosphorylated at the pachytene stage during
CC oogenesis and is negatively regulated by gck-1. Isoform b is
CC phosphorylated in proximal oocytes. {ECO:0000269|PubMed:19826475}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an increase in the
CC number of germline cells in the mitotic zone, a lack of transition zone
CC and a defect in pachytene progression resulting in a proximal gonad
CC devoid of nuclei (PubMed:19826475, PubMed:16319922). Causes sterility
CC (PubMed:19826475). RNAi-mediated knockdown in adults decreases lifespan
CC (PubMed:20624915). RNAi-mediated knockdown of isoform b in lip-1 and
CC puf-8 double mutant causes a decrease in number of germline tumors
CC (PubMed:22820175). RNAi-mediated knockdown causes a reduction in
CC intestinal ilys-3 expression in response to M.nematophilum-mediated
CC bacterial infection (PubMed:27525822). {ECO:0000269|PubMed:16319922,
CC ECO:0000269|PubMed:19826475, ECO:0000269|PubMed:20624915,
CC ECO:0000269|PubMed:22820175, ECO:0000269|PubMed:27525822}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; U03879; AAA18956.1; -; mRNA.
DR EMBL; U27124; AAA73482.1; -; mRNA.
DR EMBL; Z46937; CAA87057.1; -; Genomic_DNA.
DR EMBL; Z46937; CAB60996.1; -; Genomic_DNA.
DR PIR; A36977; A36977.
DR PIR; A36978; A36978.
DR RefSeq; NP_001022583.1; NM_001027412.3.
DR RefSeq; NP_001022584.1; NM_001027413.2. [P39745-1]
DR AlphaFoldDB; P39745; -.
DR SMR; P39745; -.
DR BioGRID; 40782; 96.
DR DIP; DIP-26227N; -.
DR IntAct; P39745; 52.
DR MINT; P39745; -.
DR STRING; 6239.F43C1.2b; -.
DR iPTMnet; P39745; -.
DR EPD; P39745; -.
DR PaxDb; P39745; -.
DR PeptideAtlas; P39745; -.
DR EnsemblMetazoa; F43C1.2a.1; F43C1.2a.1; WBGene00003401. [P39745-2]
DR EnsemblMetazoa; F43C1.2a.2; F43C1.2a.2; WBGene00003401. [P39745-2]
DR EnsemblMetazoa; F43C1.2b.1; F43C1.2b.1; WBGene00003401. [P39745-1]
DR GeneID; 175545; -.
DR KEGG; cel:CELE_F43C1.2; -.
DR UCSC; F43C1.2a.1; c. elegans. [P39745-1]
DR CTD; 175545; -.
DR WormBase; F43C1.2a; CE01583; WBGene00003401; mpk-1. [P39745-2]
DR WormBase; F43C1.2b; CE24971; WBGene00003401; mpk-1. [P39745-1]
DR eggNOG; KOG0660; Eukaryota.
DR GeneTree; ENSGT00940000156771; -.
DR InParanoid; P39745; -.
DR OMA; FINNHPY; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; P39745; -.
DR BRENDA; 2.7.11.24; 1045.
DR Reactome; R-CEL-110056; MAPK3 (ERK1) activation.
DR Reactome; R-CEL-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-CEL-112411; MAPK1 (ERK2) activation.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-1181150; Signaling by NODAL.
DR Reactome; R-CEL-1502540; Signaling by Activin.
DR Reactome; R-CEL-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-CEL-170968; Frs2-mediated activation.
DR Reactome; R-CEL-198753; ERK/MAPK targets.
DR Reactome; R-CEL-202670; ERKs are inactivated.
DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-CEL-437239; Recycling pathway of L1.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-450341; Activation of the AP-1 family of transcription factors.
DR Reactome; R-CEL-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-CEL-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-CEL-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-CEL-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-CEL-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR SignaLink; P39745; -.
DR PRO; PR:P39745; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003401; Expressed in germ line (C elegans) and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001556; P:oocyte maturation; IMP:WormBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:WormBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008349; MAPK_ERK1/2.
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 PRINTS; PR01770; ERK1ERK2MAPK.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 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 Alternative splicing; ATP-binding; Cell cycle; Differentiation; Kinase;
KW Magnesium; Meiosis; Metal-binding; Nucleotide-binding; Oogenesis;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..444
FT /note="Mitogen-activated protein kinase mpk-1"
FT /id="PRO_0000186306"
FT DOMAIN 96..384
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..258
FT /note="TXY"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 102..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 256
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19826475,
FT ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:21901106,
FT ECO:0000269|PubMed:22820175"
FT MOD_RES 258
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19826475,
FT ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:21901106,
FT ECO:0000269|PubMed:22820175"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:8299936"
FT /id="VSP_004848"
FT MUTAGEN 106
FT /note="A->V: In ku1; loss of function and ATP-binding. Lack
FT of tail swelling, severe constipation and loss of ilys-3
FT expression up-regulation following M.nematophilium
FT infection."
FT /evidence="ECO:0000269|PubMed:15268855,
FT ECO:0000269|PubMed:27525822, ECO:0000269|PubMed:8299935"
FT MUTAGEN 216
FT /note="V->G: In ga111; at the restrictive temperature of 25
FT degrees Celsius, causes an increase in gld-1 expression and
FT a loss of cep-1 expression in late pachytene germ cells.
FT Loss of egl-1 mRNA expression in response to gamma
FT irradiation. 70 percent of mutants have germ cells arrested
FT at the pachytene stage; phenotype is reversible and meiosis
FT can resume. At the somewhat permissive temperature of 20
FT degrees Celsius has reduced live brood size; brood size
FT further decreased in pzf-1 mutant background. At the
FT restrictive temperature of 26 degrees Celsius, are
FT completely sterile. Partial phosphorylation at Thr-256 and
FT Tyr-258."
FT /evidence="ECO:0000269|PubMed:17096596,
FT ECO:0000269|PubMed:21901106"
FT CONFLICT 9..10
FT /note="LC -> FF (in Ref. 2; AAA18956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50663 MW; 11BA27D17641980D CRC64;
MPTWIPNNLC AQPTTRNAKP PSNGHPQATQ QQSAPGSLAY RNSSNIPNGA TNHVRQQKWQ
YTRSGHRKMA DGEAVISTVN NVEEVHGQLF EVAPRYVNLS YIGEGAYGMV ASALDTITRD
RVAIKKISPF EHQTFCQRTL REIKILNRFK HENIINIQEI IRSETVDSLK DIYIVQCLME
TDLYKLLKTQ KLSNDHVCYF LYQILRGLKY IHSANVLHRD LKPSNLLLNT TCDLKICDFG
LARVTDPQTD HTGFLTEYVA TRWYRAPEIM LNSKGYTKSI DVWSVGCILA EMLSNRPLFP
GKHYLDQLNL ILAVVGSPSN ADLQCIINDK ARSYLISLPH KPKQPWARLY PGADPRALDL
LDKMLTFNPH NRIDIEQALA HPYLEQYYDP GDEPVCEEPF TLEMEFDDLP KEKLKELIWE
EAEAHHRRME AEAAARNNGG QNPV
