MEX5_CAEEL
ID MEX5_CAEEL Reviewed; 468 AA.
AC Q9XUB2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Zinc finger protein mex-5;
GN Name=mex-5 {ECO:0000312|WormBase:W02A2.7};
GN ORFNames=W02A2.7 {ECO:0000312|WormBase:W02A2.7};
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.
RX PubMed=10882103; DOI=10.1016/s1097-2765(00)80246-4;
RA Schubert C.M., Lin R., de Vries C.J., Plasterk R.H., Priess J.R.;
RT "MEX-5 and MEX-6 function to establish soma/germline asymmetry in early C.
RT elegans embryos.";
RL Mol. Cell 5:671-682(2000).
RN [3]
RP FUNCTION, INTERACTION WITH PLK-1 AND PLK-2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION AT THR-186, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF THR-186.
RX PubMed=18199581; DOI=10.1242/dev.013425;
RA Nishi Y., Rogers E., Robertson S.M., Lin R.;
RT "Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-
RT primed MEX-5 and MEX-6.";
RL Development 135:687-697(2008).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT
RP SER-458, AND MUTAGENESIS OF SER-458.
RX PubMed=18842813; DOI=10.1242/dev.027060;
RA Tenlen J.R., Molk J.N., London N., Page B.D., Priess J.R.;
RT "MEX-5 asymmetry in one-cell C. elegans embryos requires PAR-4- and PAR-1-
RT dependent phosphorylation.";
RL Development 135:3665-3675(2008).
RN [5]
RP FUNCTION.
RX PubMed=27594427; DOI=10.1016/j.cell.2016.08.006;
RA Saha S., Weber C.A., Nousch M., Adame-Arana O., Hoege C., Hein M.Y.,
RA Osborne-Nishimura E., Mahamid J., Jahnel M., Jawerth L., Pozniakovski A.,
RA Eckmann C.R., Juelicher F., Hyman A.A.;
RT "Polar positioning of phase-separated liquid compartments in cells
RT regulated by an mRNA competition mechanism.";
RL Cell 166:1572-1584(2016).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30279189; DOI=10.1534/g3.118.200744;
RA Gauvin T.J., Han B., Sun M.J., Griffin E.E.;
RT "PIE-1 Translation in the Germline Lineage Contributes to PIE-1 Asymmetry
RT in the Early Caenorhabditis elegans Embryo.";
RL G3 (Bethesda) 8:3791-3801(2018).
CC -!- FUNCTION: Functions with mex-6 to affect embryonic viability, establish
CC soma germline asymmetry in embryos and establish plk-1, pie-1, mex-1,
CC and pos-1 asymmetry in embryos (PubMed:10882103, PubMed:18199581,
CC PubMed:18842813, PubMed:30279189). Also affects formation of intestinal
CC cells (PubMed:10882103). Binds to mRNA in vitro, and inhibits pgl-3-
CC mediated P-granule formation, probably by competing with pgl-3 for
CC binding to mRNA (PubMed:27594427). {ECO:0000269|PubMed:10882103,
CC ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18842813,
CC ECO:0000269|PubMed:27594427, ECO:0000269|PubMed:30279189}.
CC -!- SUBUNIT: Interacts (when phosphorylated on Thr-186) with plk-1 (via
CC POLO box domain) and plk-2 (via POLO box domain).
CC {ECO:0000269|PubMed:18199581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:18842813}.
CC -!- TISSUE SPECIFICITY: Asymmetrically localized to the anterior of the
CC zygote before mitotic division, then differentially distributed to the
CC somatic blastomere precursor cells. {ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:18842813}.
CC -!- PTM: Phosphorylation on Ser-458 by par-1 promotes localization of the
CC protein to the anterior cytoplasm of the zygote (PubMed:18842813).
CC Phosphorylation by mbk-1 appears to be required for subsequent
CC phosphorylation by plk-1 (PubMed:18199581).
CC {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18842813}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces the expression of
CC pie-1 in P2 blastomeres (PubMed:30279189). RNAi-mediated knockdown in
CC mex-6 pk440 mutant background causes a loss in plk-1 asymmetric
CC distribution during the first embryonic cell divisions.
CC {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:30279189}.
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DR EMBL; BX284604; CAB05310.1; -; Genomic_DNA.
DR PIR; T26081; T26081.
DR RefSeq; NP_502566.1; NM_070165.4.
DR PDB; 6PMG; NMR; -; X=312-346.
DR PDBsum; 6PMG; -.
DR AlphaFoldDB; Q9XUB2; -.
DR BMRB; Q9XUB2; -.
DR SMR; Q9XUB2; -.
DR BioGRID; 43384; 23.
DR IntAct; Q9XUB2; 3.
DR STRING; 6239.W02A2.7; -.
DR BindingDB; Q9XUB2; -.
DR ChEMBL; CHEMBL1293319; -.
DR DrugCentral; Q9XUB2; -.
DR iPTMnet; Q9XUB2; -.
DR EPD; Q9XUB2; -.
DR PaxDb; Q9XUB2; -.
DR PeptideAtlas; Q9XUB2; -.
DR EnsemblMetazoa; W02A2.7.1; W02A2.7.1; WBGene00003230.
DR GeneID; 178296; -.
DR KEGG; cel:CELE_W02A2.7; -.
DR UCSC; W02A2.7; c. elegans.
DR CTD; 178296; -.
DR WormBase; W02A2.7; CE21237; WBGene00003230; mex-5.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00970000196404; -.
DR HOGENOM; CLU_584274_0_0_1; -.
DR InParanoid; Q9XUB2; -.
DR OMA; YHRVMEH; -.
DR OrthoDB; 1028924at2759; -.
DR PRO; PR:Q9XUB2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003230; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:WormBase.
DR GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:WormBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:WormBase.
DR InterPro; IPR045877; ZFP36-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12547; PTHR12547; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="Zinc finger protein mex-5"
FT /id="PRO_0000089183"
FT ZN_FING 270..299
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 314..344
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphothreonine; by mbk-2"
FT /evidence="ECO:0000269|PubMed:18199581"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18842813"
FT MUTAGEN 186
FT /note="T->A: Abolishes phosphorylation. Reduced embryo
FT viability and, pie-1 and mex-5 degradation in embryonic
FT somatic cells. Severe reduction in binding to plk-1 and
FT plk-2. Prevent subsequent phosphorylation by plk-1."
FT /evidence="ECO:0000269|PubMed:18199581"
FT MUTAGEN 186
FT /note="T->D,E: Phosphomimetic mutant which severely
FT abolishes interaction with plk-1 and plk-2."
FT /evidence="ECO:0000269|PubMed:18199581"
FT MUTAGEN 458
FT /note="S->A: Loss of phosphorylation and zygotic
FT asymmetry."
FT /evidence="ECO:0000269|PubMed:18842813"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6PMG"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:6PMG"
SQ SEQUENCE 468 AA; 52820 MW; 6B0E6FC4971CF5CD CRC64;
MKAASNSVSS AGGSVSPTTT QPPLPPGQSS HPQIYDQQMQ YYFAAAMPNQ PMATYAAQNG
SSQQYAPAAP YYQDANGQYV QVPANGSMAP QQHMMVSGQP YLYMAQPQQG AQQVMQSGQP
QLIYYQQSMA PQAAPMYFHP MQAAPMLPEQ MGVMPHTQPA IPPQQQPRQV GVEISSTRTA
PLTSSTPLPT SLEYETVQRD NRNRNIQFRY HRVMEHDELP IDEISKITLD NHNDDTMSAE
KENHFHEHRG EKFGRRGFPI PETDSQQPPN YKTRLCMMHA SGIKPCDMGA RCKFAHGLKE
LRATDAPARY PNNKYKTKLC KNFARGGTGF CPYGLRCEFV HPTDKEFQNI PPYQRMSHDD
QDYDQDVIPE DYVVARHQPR FMRTGGRATT PTKVMLKHRN VAGSMMCLSN AGRDLQAGGD
YNQPESNEDD LPPHLRRNRR ENPPMNKRRT SLSTKWTSEE NLGLRGHY
