EGG4_CAEEL
ID EGG4_CAEEL Reviewed; 753 AA.
AC O01767;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Inactive protein-tyrosine phosphatase egg-4 {ECO:0000305};
DE AltName: Full=Egg sterile protein 4 {ECO:0000312|WormBase:T21E3.1};
DE AltName: Full=Protein-tyrosine phosphatase-like protein egg-4 {ECO:0000303|PubMed:19879147};
GN Name=egg-4 {ECO:0000312|WormBase:T21E3.1};
GN ORFNames=T21E3.1 {ECO:0000312|WormBase:T21E3.1};
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, LACK OF PHOSPHATASE ACTIVITY, IDENTIFICATION IN A COMPLEX WITH
RP MBK-2; EGG-3 AND EGG-5, INTERACTION WITH MBK-2, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF HIS-599; GLY-603 AND ARG-606.
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, INTERACTION WITH EGG-3 AND MBK-2, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, 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-5 in the
CC oocyte-to-zygote transition (PubMed:19879842, PubMed:19879147).
CC Required for the polarization of cortical actin cytoskeleton
CC rearrangement in the oocyte before and after fertilization
CC (PubMed:19879147). Together with egg-5, required for the cortical
CC localization of kinase mbk-2 and for the inhibition of mbk-2 kinase
CC activity in maturing oocyte until the end of meiosis I
CC (PubMed:19879842). Also required for kinase mbk-2, pseudophosphatase
CC egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after
CC fertilization (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 (PubMed:19879842). Interacts (via tyrosine-protein
CC phosphatase domain) with kinase mbk-2 (via 'Tyr-619' and 'Tyr-621');
CC mbk-2 tyrosine phosphorylation enhances the interaction
CC (PubMed:19879842). The interaction inhibits mbk-2 kinase activity and
CC is required for mbk-2 oocyte cortex localization (PubMed:19879842,
CC PubMed:19879147). Interacts with egg-3 (PubMed:19879147).
CC {ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19879147}. Note=Co-localizes with egg-3 to the cell
CC cortex in developing oocytes and in newly fertilized embryos; cortical
CC localization requires egg-3 and chitin synthase chs-1. At the beginning
CC of meiosis anaphase I, egg-4 moves away from the cell cortex and is
CC likely degraded. {ECO:0000269|PubMed:19879147}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing oocytes (at protein
CC level). {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-4 may lack catalytic activity. Despite the lack of
CC catalytic activity, egg-4 may retain the capacity to bind to
CC phosphorylated substrates. Does not dephosphorylate mbk-2
CC (PubMed:19879842). {ECO:0000269|PubMed:19879842, ECO:0000305}.
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DR EMBL; BX284601; CCD71367.1; -; Genomic_DNA.
DR PIR; T29763; T29763.
DR RefSeq; NP_491269.1; NM_058868.4.
DR AlphaFoldDB; O01767; -.
DR SMR; O01767; -.
DR ComplexPortal; CPX-3381; Egg-3/4/5 MBK-2 complex.
DR IntAct; O01767; 2.
DR STRING; 6239.T21E3.1; -.
DR PaxDb; O01767; -.
DR PeptideAtlas; O01767; -.
DR EnsemblMetazoa; T21E3.1.1; T21E3.1.1; WBGene00020652.
DR GeneID; 171980; -.
DR KEGG; cel:CELE_T21E3.1; -.
DR UCSC; T21E3.1; c. elegans.
DR CTD; 171980; -.
DR WormBase; T21E3.1; CE13874; WBGene00020652; egg-4.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00970000196671; -.
DR HOGENOM; CLU_370166_0_0_1; -.
DR InParanoid; O01767; -.
DR OMA; FNNVRMK; -.
DR OrthoDB; 411281at2759; -.
DR PRO; PR:O01767; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020652; Expressed in adult organism and 4 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:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA: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; IDA: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-4"
FT /id="PRO_0000443251"
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 75..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 599
FT /note="H->A: Strongly reduced interaction with mbk-2; when
FT associated with A-603 and A-606."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 603
FT /note="G->A: Strongly reduced interaction with mbk-2; when
FT associated with A-599 and A-606."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 606
FT /note="R->A: Strongly reduced interaction with mbk-2; when
FT associated with A-599 and A-603."
FT /evidence="ECO:0000269|PubMed:19879842"
SQ SEQUENCE 753 AA; 86059 MW; 68EAA7234FABC448 CRC64;
MALNSEVMFR EQINAMRSQA GRKRATSLQS FCSGNTDDSS ADSTDNMDMM VDYPQQKGVS
CMRARFNSES TLSKSFRKKV KKLAQKDRRS KERLNGNSEE DAIEVPRGAP STYAAPSKLR
KSKALDCLVS EKPKDEGRRE DSGHGADIEM AKGHFNNVRM KVFAARTAMQ VEPALVMKTR
KALEMKNAVL ENHQSPGAFS LHAAYKIAAS AESRVGSITP CNKKVTKEAM ANLIRSSYDD
TEITQELLFS SKFDTKWKGR YTDIYMRRDE NGKKPKRPVN GQGWVMPLKS ICEKFGINST
FFTNHRIDLK SARDQVLLMR LLSHDQTSTW ISDIHPEAVK NETMAEYLLR ELDASTMQKR
VQAFKANVLA DRDRVRVAGQ FYNNIRIGKR MFGAARKAKY LSTIIGGMER RFEILENSVN
HIPFTHSASD NNQEKCRNPR VHCKDSTRIA 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 GEMPNKVATV DGILSPAKSV FEF
