EGG5_CAEEL
ID EGG5_CAEEL Reviewed; 753 AA.
AC O61789;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Inactive protein-tyrosine phosphatase egg-5 {ECO:0000305};
DE AltName: Full=Egg sterile protein 5 {ECO:0000312|WormBase:R12E2.10};
DE AltName: Full=Protein-tyrosine phosphatase-like protein egg-5 {ECO:0000303|PubMed:19879147};
GN Name=egg-5 {ECO:0000312|WormBase:R12E2.10};
GN ORFNames=R12E2.10 {ECO:0000312|WormBase:R12E2.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MBK-2; EGG-3 AND EGG-4,
RP INTERACTION WITH MBK-2, AND DISRUPTION PHENOTYPE.
RX PubMed=19879842; DOI=10.1016/j.cell.2009.08.047;
RA Cheng K.C., Klancer R., Singson A., Seydoux G.;
RT "Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and
RT EGG-5 during the oocyte-to-embryo transition.";
RL Cell 139:560-572(2009).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19879147; DOI=10.1016/j.cub.2009.09.015;
RA Parry J.M., Velarde N.V., Lefkovith A.J., Zegarek M.H., Hang J.S., Ohm J.,
RA Klancer R., Maruyama R., Druzhinina M.K., Grant B.D., Piano F., Singson A.;
RT "EGG-4 and EGG-5 Link Events of the Oocyte-to-Embryo Transition with
RT Meiotic Progression in C. elegans.";
RL Curr. Biol. 19:1752-1757(2009).
CC -!- FUNCTION: Inactive phosphatase which acts redundantly with egg-4 in the
CC oocyte-to-zygote transition (PubMed:19879842, PubMed:19879147).
CC Required for polarized cortical actin cytoskeleton rearrangement in the
CC oocyte before and after fertilization (PubMed:19879147). Together with
CC egg-4, required for the cortical localization of kinase mbk-2 in
CC maturing oocyte until the end of meiosis I (PubMed:19879842). Also
CC required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase
CC chs-1 localization to cytoplasmic foci after fertilization
CC (PubMed:19879147). {ECO:0000269|PubMed:19879147,
CC ECO:0000269|PubMed:19879842}.
CC -!- SUBUNIT: Part of a complex, consisting of pseudophosphatases egg-3,
CC egg-4, egg-5 and kinase mbk-2; this complex is required for the oocyte-
CC to-zygote transition. Interacts (via tyrosine-protein phosphatase
CC domain) with kinase mbk-2 (via 'Tyr-619' and 'Tyr-621'); mbk-2 tyrosine
CC phosphorylation enhances the interaction.
CC {ECO:0000269|PubMed:19879842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19879147}. Note=Localizes to the cell cortex in
CC developing oocytes and in newly fertilized embryos.
CC {ECO:0000269|PubMed:19879147}.
CC -!- DISRUPTION PHENOTYPE: Severe reduction in the number of hatched larvae
CC (PubMed:19879147). Simultaneous RNAi-mediated knockdown of egg-5
CC results in no viable progeny and causes endomitosis in the uterus,
CC generation of polyspermic embryos and defects in meiosis completion,
CC polar body formation and eggshell chitin layer formation
CC (PubMed:19879147). In addition, posterior formation of F-actin cap at
CC the cortex oocyte and its polarized dispersal after fertilization are
CC impaired (PubMed:19879147). Prevents mbk-2 localization to the
CC unfertilized oocyte cortex without affecting egg-3 cortical
CC localization (PubMed:19879842, PubMed:19879147). Prevents mbk-2, egg-3
CC and chs-1 re-localization to cytoplasmic foci at meiosis anaphase I
CC (PubMed:19879147). Simultaneous RNAi-mediated knockdown of egg-5 and
CC mel-26 causes premature phosphorylation of mei-1, a mbk-1 substrate,
CC during oocyte maturation (PubMed:19879842).
CC {ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: The active site Cys-600 is replaced by a Asp residue
CC suggesting that egg-5 may lack catalytic activity. Despite the lack of
CC catalytic activity, egg-5 may retain the capacity to bind to
CC phosphorylated substrates. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284601; CCD65177.1; -; Genomic_DNA.
DR PIR; T33093; T33093.
DR RefSeq; NP_491316.1; NM_058915.6.
DR AlphaFoldDB; O61789; -.
DR SMR; O61789; -.
DR ComplexPortal; CPX-3381; Egg-3/4/5 MBK-2 complex.
DR IntAct; O61789; 1.
DR STRING; 6239.R12E2.10; -.
DR EPD; O61789; -.
DR PaxDb; O61789; -.
DR PeptideAtlas; O61789; -.
DR EnsemblMetazoa; R12E2.10.1; R12E2.10.1; WBGene00020035.
DR GeneID; 172007; -.
DR KEGG; cel:CELE_R12E2.10; -.
DR UCSC; R12E2.10; c. elegans.
DR CTD; 172007; -.
DR WormBase; R12E2.10; CE18142; WBGene00020035; egg-5.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00970000196671; -.
DR HOGENOM; CLU_370166_0_0_1; -.
DR InParanoid; O61789; -.
DR OrthoDB; 411281at2759; -.
DR PRO; PR:O61789; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020035; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IGI:UniProtKB.
DR GO; GO:0030703; P:eggshell formation; IGI:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IGI:WormBase.
DR GO; GO:0001556; P:oocyte maturation; IC:ComplexPortal.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IGI:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IGI:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Reference proteome.
FT CHAIN 1..753
FT /note="Inactive protein-tyrosine phosphatase egg-5"
FT /id="PRO_0000443252"
FT DOMAIN 408..661
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 85957 MW; DB71183AB91FD14F CRC64;
MALNSEVMFR EQINAMRSQA GRKRATSLQS FCSGNTDDSS ADSTDNMDMM VDYPQQKGVS
CMRARFNSES TLSKSFRKKV KKLAQKDRRS KERLNGNSEE DAIEVPRGAP STYAAPSKLR
KSKALDCLVS EKPKDEGRSE DSGHGADIEM AKGHFNDVRM KVFAARTAMQ VEPALVMKTR
KALEMKNAVL ENHQSPGAFS LHAAYKIAAS AESRVGSITP CNKKVTKEAM ANLIRSSYDD
TEITQELLFS SKFDSKWKGR YTDIYMRRDE NGKKPKRPVN GQGWVMPLKS ICEKFGINST
FFTNHRIDLK SARDQVLLMR LLSHDQTSTW ISDIHPEAVK NETLAEYLLR ELDASTMQKR
VQAFKANVLA DRDRVRVAGQ FYNNIRIGKR MFGAARKAKY LSTIIGGMER RFEILENSVN
HIPFTHSASD NNQEKCRNPR VHCRDSTRIA LQFPRGQYLG DFIHANRISG KPLFNEFIMT
QAPMKNTVDD FWRMVWQEEV PYIVMLTSRK EPERCEYYWP KSPSDPAVTV PGGLRIENFG
VYQAPDPLFR VTHLRLIGPD REERHVEHWQ GDVNNSSNMY SPLNILRLLR NASKPVVIHD
HLGVSRAACL VAAEIAICSL LRGPTYKYPV QRAVQFLRQR RPFSIETPMQ YIFVHRLVAF
FFRDVIGSAK ELDVDYERWL QERSERMFLD DLAAPIPGYR LLSPRADPDI VRMVGRPERP
NYRREAPDCV GEMPNKVAAV DGILSPAKSV FEF
