EGG3_CAEEL
ID EGG3_CAEEL Reviewed; 555 AA.
AC Q20402;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein tyrosine phosphatase-like protein egg-3 {ECO:0000305};
DE AltName: Full=Egg sterile protein 3 {ECO:0000312|WormBase:F44F4.2};
GN Name=egg-3 {ECO:0000312|WormBase:F44F4.2};
GN ORFNames=F44F4.2 {ECO:0000312|WormBase:F44F4.2};
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, INTERACTION WITH MBK-2, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, MOTIF, AND DISRUPTION PHENOTYPE.
RX PubMed=17869113; DOI=10.1016/j.cub.2007.08.049;
RA Stitzel M.L., Cheng K.C., Seydoux G.;
RT "Regulation of MBK-2/Dyrk kinase by dynamic cortical anchoring during the
RT oocyte-to-zygote transition.";
RL Curr. Biol. 17:1545-1554(2007).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17869112; DOI=10.1016/j.cub.2007.08.011;
RA Maruyama R., Velarde N.V., Klancer R., Gordon S., Kadandale P., Parry J.M.,
RA Hang J.S., Rubin J., Stewart-Michaelis A., Schweinsberg P., Grant B.D.,
RA Piano F., Sugimoto A., Singson A.;
RT "EGG-3 regulates cell-surface and cortex rearrangements during egg
RT activation in Caenorhabditis elegans.";
RL Curr. Biol. 17:1555-1560(2007).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MBK-2; EGG-4 AND EGG-5,
RP INTERACTION WITH MBK-2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-452; GLY-455 AND GLY-460.
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 [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MBK-2 AND EGG-4, SUBCELLULAR LOCATION, AND
RP 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).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20971008; DOI=10.1016/j.cub.2010.09.059;
RA Johnston W.L., Krizus A., Dennis J.W.;
RT "Eggshell chitin and chitin-interacting proteins prevent polyspermy in C.
RT elegans.";
RL Curr. Biol. 20:1932-1937(2010).
CC -!- FUNCTION: Probable pseudophosphatase required for the oocyte-to-zygote
CC transition during which it regulates the polarized dispersal of the
CC cortical actin cytoskeleton, the synthesis of the eggshell chitin layer
CC and the formation of the polar bodies after meiosis I and II
CC (PubMed:17869112). Acts as scaffold to tether kinase mbk-2 and
CC pseudophosphatases egg-4 and egg-5 to the oocyte cortex and thus
CC restricts mbk-2 activity to the cortex during meiosis I
CC (PubMed:17869113, PubMed:17869112, PubMed:19879842, PubMed:19879147).
CC Regulates mbk-2 localization to cytoplasmic foci during meiosis II
CC (PubMed:17869113, PubMed:17869112). Also required for chitin synthase
CC chs-1 localization to the cell cortex of unfertilized oocytes and to
CC cytoplasmic foci in the fertilized embryo (PubMed:17869112).
CC {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113,
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, PubMed:19879147). Interacts (via
CC tyrosine-protein phosphatase domain) with kinase mbk-2 (via N-
CC terminus); the interaction does not affect mbk-2 kinase activity, is
CC enhanced by mbk-2 tyrosine phosphorylation status and requires prior
CC binding of mbk-2 to egg-4 and egg-5 (PubMed:17869113, PubMed:19879842,
CC PubMed:19879147). Interacts with egg-4 (PubMed:19879147).
CC {ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147,
CC ECO:0000269|PubMed:19879842}.
CC -!- INTERACTION:
CC Q20402; Q9XTF3: mbk-2; NbExp=9; IntAct=EBI-2476895, EBI-2005616;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842,
CC ECO:0000269|PubMed:20971008}. Cytoplasm {ECO:0000269|PubMed:17869112,
CC ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147,
CC ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:20971008}. Note=Co-
CC localizes with mbk-2 to the oocyte cell membrane during most of meiosis
CC I, relocalizes to subcortical foci during anaphase I which become
CC cytoplasmic during meiosis II (PubMed:17869113, PubMed:17869112,
CC PubMed:19879842). At the end of meiosis II, egg-3 is degraded releasing
CC mbk-2 in the cytoplasm (PubMed:17869113, PubMed:17869112,
CC PubMed:19879842). Co-localizes with egg-4 to the cell cortex in
CC developing oocytes and in newly fertilized embryos (PubMed:19879147).
CC Cortical localization in developing oocytes is egg-1, egg-2 and chs-1-
CC dependent (PubMed:17869112, PubMed:20971008). Co-localizes in the
CC fertilized egg with chs-1 to cytoplasmic foci (PubMed:17869112).
CC {ECO:0000269|PubMed:17869112, ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842,
CC ECO:0000269|PubMed:20971008}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes during meiosis I and II
CC followed by proteasomal degradation at the 1-cell and 2-cell embryonic
CC stages (at protein level). {ECO:0000269|PubMed:17869113,
CC ECO:0000269|PubMed:19879842}.
CC -!- DOMAIN: The N-terminal destruction box (D-box) motifs 1 and 2 act as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000269|PubMed:17869113}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hermaphrodite
CC sterility characterized by the production of oocytes lacking an
CC eggshell (PubMed:17869112). Prevents the polarized dispersal of
CC cortical F-actin following oocyte fertilization without affecting the
CC formation of the F-actin cap (PubMed:17869112). Impairs egg-4 and egg-5
CC cortical localization in oocytes (PubMed:19879147). Causes a loss of
CC kinase mbk-2 cortical localization in oocyte in meiosis I
CC (PubMed:17869113, PubMed:19879842, PubMed:19879147). RNAi-mediated
CC knockdown in a mat-1 (ax227) mutant background, restores mbk-2
CC cytoplasmic relocalization and mbk-2-mediated degradation of pos-1 and
CC mei-1 (PubMed:17869113). Simultaneous RNAi-mediated knockdown of mat-1
CC causes polyspermy and a failure to internalize egg-1 after oocyte
CC fertilization (PubMed:20971008). {ECO:0000269|PubMed:17869112,
CC ECO:0000269|PubMed:17869113, ECO:0000269|PubMed:19879147,
CC ECO:0000269|PubMed:19879842, ECO:0000269|PubMed:20971008}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although the active site Cys-452 is conserved, another
CC important catalytic site, 'Arg-458', is replaced by a Lys residue
CC suggesting that egg-3 may lack catalytic activity. Despite the lack of
CC catalytic activity, egg-3 may retain the capacity to bind to
CC phosphorylated substrates. {ECO:0000305}.
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DR EMBL; BX284602; CAA85453.1; -; Genomic_DNA.
DR PIR; T22184; T22184.
DR RefSeq; NP_496341.1; NM_063940.4.
DR AlphaFoldDB; Q20402; -.
DR SMR; Q20402; -.
DR ComplexPortal; CPX-3381; Egg-3/4/5 MBK-2 complex.
DR IntAct; Q20402; 2.
DR STRING; 6239.F44F4.2.1; -.
DR EPD; Q20402; -.
DR PaxDb; Q20402; -.
DR PeptideAtlas; Q20402; -.
DR EnsemblMetazoa; F44F4.2.1; F44F4.2.1; WBGene00009701.
DR GeneID; 174677; -.
DR UCSC; F44F4.2.1; c. elegans.
DR CTD; 174677; -.
DR WormBase; F44F4.2; CE00998; WBGene00009701; egg-3.
DR eggNOG; KOG0106; Eukaryota.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000171629; -.
DR HOGENOM; CLU_039673_1_0_1; -.
DR InParanoid; Q20402; -.
DR OMA; LFECADI; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q20402; -.
DR PRO; PR:Q20402; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009701; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030703; P:eggshell formation; IMP:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IC:ComplexPortal.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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 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; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Reference proteome; Repeat.
FT CHAIN 1..555
FT /note="Protein tyrosine phosphatase-like protein egg-3"
FT /id="PRO_0000443421"
FT DOMAIN 207..514
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOTIF 96..99
FT /note="D-box 1"
FT /evidence="ECO:0000269|PubMed:17869113"
FT MOTIF 130..133
FT /note="D-box 2"
FT /evidence="ECO:0000269|PubMed:17869113"
FT MOTIF 253..256
FT /note="RXXL motif; required for cortical localization"
FT /evidence="ECO:0000269|PubMed:17869113"
FT MOTIF 266..269
FT /note="RXXL motif"
FT /evidence="ECO:0000303|PubMed:17869113"
FT MOTIF 509..512
FT /note="RXXL motif; required for cortical localization"
FT /evidence="ECO:0000269|PubMed:17869113"
FT MOTIF 525..528
FT /note="RXXL motif; required for cortical localization"
FT /evidence="ECO:0000269|PubMed:17869113"
FT MUTAGEN 452
FT /note="C->A: No effect on the interaction with mbk-2; when
FT associated with A-455 and A-460."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 455
FT /note="G->A: No effect on the interaction with mbk-2; when
FT associated with A-452 and A-460."
FT /evidence="ECO:0000269|PubMed:19879842"
FT MUTAGEN 460
FT /note="G->A: No effect on the interaction with mbk-2; when
FT associated with A-452 and A-455."
FT /evidence="ECO:0000269|PubMed:19879842"
SQ SEQUENCE 555 AA; 64151 MW; 587DA01F0CC92E94 CRC64;
MRTSDSHLPL SNLARSDSIE FKDAVINEKW VHSANRRKGH LTPKAPEKKS GWFGGQKSEE
ELLMERVEQH ELEELQTFIA QKLFRVDGII CDEETRILLV EKLMNAKEYP TINHDELAHR
YGSSMAGWLR DRLVPSMSDC SSVLQRAAAE FYQNKMSDPL CNWGQLNPEH VSMVAARIAK
FSEEMSSKVK WSLLVEPGKF SCHLTEFVQE FNRLDRMFVS NELSDEESLQ TAFNANYLTK
ARSKMVPCAE FSRVKLNDGL GRLDDRNELR NGMFSDEHEF LQEEGYTAKS TYGTTDFIHA
NYVKGGPLLN TFICAQAPLK NTQEDFWRMV FQEKCQFIVM LNSAVDSSTL GPLDSANRNH
CPYYWPRAEN ESLRFGSFHI TCMKVDSKAD PLFTITKLKV QKVGGNLLDA EFDEELFLEH
WQWDWQYLGD VHWPFRVLRK ARQLSTPTIV QCIDGCSKSG TLVSIETALM HFIRGSPITK
SLILQSCVFV RLQRRLSVSS VLLYLFIYRV ILRWIEPYVN KWYHRAALGL RFKSIGFIQK
YNAMIQEFSR ITPAY
