MEX6_CAEEL
ID MEX6_CAEEL Reviewed; 467 AA.
AC Q09436;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Zinc finger protein mex-6;
GN Name=mex-6; ORFNames=AH6.5;
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, PHOSPHORYLATION AT THR-190,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-190.
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).
CC -!- FUNCTION: Functions with mex-5 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). Also
CC affects formation of intestinal cells (PubMed:10882103).
CC {ECO:0000269|PubMed:10882103, ECO:0000269|PubMed:18199581}.
CC -!- SUBUNIT: Interacts (probably when phosphorylated on Thr-190) with plk-1
CC (via POLO box domain) and plk-2 (via POLO box domain).
CC {ECO:0000269|PubMed:18199581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9XUB2}.
CC -!- PTM: Phosphorylation on Ser-457 by par-1 promotes localization of the
CC protein to the anterior cytoplasm of the zygote.
CC {ECO:0000250|UniProtKB:Q9XUB2}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in mex-5 zu199 mutant
CC background causes a loss in plk-1 asymmetric distribution during the
CC first embryonic cell divisions. {ECO:0000269|PubMed:18199581}.
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DR EMBL; Z48009; CAA88088.2; -; Genomic_DNA.
DR PIR; T18624; T18624.
DR RefSeq; NP_496043.1; NM_063642.5.
DR AlphaFoldDB; Q09436; -.
DR BioGRID; 39827; 24.
DR DIP; DIP-26165N; -.
DR IntAct; Q09436; 15.
DR STRING; 6239.AH6.5; -.
DR iPTMnet; Q09436; -.
DR EPD; Q09436; -.
DR PaxDb; Q09436; -.
DR PeptideAtlas; Q09436; -.
DR EnsemblMetazoa; AH6.5.1; AH6.5.1; WBGene00003231.
DR GeneID; 174504; -.
DR KEGG; cel:CELE_AH6.5; -.
DR UCSC; AH6.5; c. elegans.
DR CTD; 174504; -.
DR WormBase; AH6.5; CE26846; WBGene00003231; mex-6.
DR eggNOG; KOG1677; Eukaryota.
DR GeneTree; ENSGT00970000196404; -.
DR HOGENOM; CLU_584274_0_0_1; -.
DR InParanoid; Q09436; -.
DR OrthoDB; 954544at2759; -.
DR PRO; PR:Q09436; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003231; Expressed in germ line (C elegans) and 3 other tissues.
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: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; IGI: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; 2.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; DNA-binding; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Zinc finger protein mex-6"
FT /id="PRO_0000089184"
FT ZN_FING 273..302
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 317..347
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000303|PubMed:18199581"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XUB2"
FT MUTAGEN 190
FT /note="T->A: Abolishes phosphorylation. Severe reduction in
FT binding to plk-1 and plk-2."
FT /evidence="ECO:0000269|PubMed:18199581"
FT MUTAGEN 190
FT /note="T->E: Phosphomimetic mutant which severely abolishes
FT interaction with plk-1 and plk-2."
FT /evidence="ECO:0000269|PubMed:18199581"
SQ SEQUENCE 467 AA; 52393 MW; EEC1A76ABEF5E4B1 CRC64;
MTATSNSAPL AGGSLSSSAT AQPPQPPPGH QQQHPLPQIY DSQMQYYYGS SMPNQPIPTY
TAQNGAPQQF GTPPYYQDAN GQFGQVPAQQ QMMTAGHPYF YMAQPQQGGQ HVAQSGQPQI
FYYQQPLGQM AQQAAPMYFH PMQAASTPML SEQMSMMPQI QSTNPQQSEQ LRKSGAQIST
TRTVPLTSST PLPTSREYET VQRDRNRNSQ SRYQCPIEHD DLPIDEISKI TIDNHNDDTM
SAEKENRFNK NRVEKLGRRG FAKPEVDSQL PHNFKTRLCM THAAGINPCA LGARCKFAHG
LKELRASDIP TRYPNNKYKT KLCKNFARGG SGVCPYGLRC EFVHPSDTEF QNIPPYQRKM
VEEHDSIPED YVVARYQPRF MHTSGKATTP TKVTLKQRNV AGSMMCLSNT GRDLEAGGDF
NHPEINENDL PPHLRRIRRG NPPVTRSRPS FSTKWTSVEN LGLRGHY
