MEP1_CAEEL
ID MEP1_CAEEL Reviewed; 870 AA.
AC Q21502; Q95VF1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=MOG interacting and ectopic P-granules protein 1;
DE AltName: Full=Nuclear zinc finger protein;
GN Name=mep-1 {ECO:0000312|WormBase:M04B2.1}; ORFNames=M04B2.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL27004.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MOG-1; MOG-4 AND
RP MOG-5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12088146; DOI=10.1017/s1355838202028595;
RA Belfiore M., Mathies L.D., Pugnale P., Moulder G., Barstead R., Kimble J.,
RA Puoti A.;
RT "The MEP-1 zinc-finger protein acts with MOG DEAH box proteins to control
RT gene expression via the fem-3 3' untranslated region in Caenorhabditis
RT elegans.";
RL RNA 8:725-739(2002).
RN [2] {ECO:0000312|EMBL:CAB01235.2}
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 [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH HDA-1; LET-418 AND PIE-1.
RX PubMed=12507426; DOI=10.1016/s0092-8674(02)01202-3;
RA Unhavaithaya Y., Shin T.H., Miliaras N., Lee J., Oyama T., Mello C.C.;
RT "MEP-1 and a homolog of the NURD complex component Mi-2 act together to
RT maintain germline-soma distinctions in C. elegans.";
RL Cell 111:991-1002(2002).
RN [4] {ECO:0000305}
RP INTERACTION WITH UNC-98.
RX PubMed=12808046; DOI=10.1091/mbc.e02-10-0676;
RA Mercer K.B., Flaherty D.B., Miller R.K., Qadota H., Tinley T.L.,
RA Moerman D.G., Benian G.M.;
RT "Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel
RT partner of UNC-97/PINCH in muscle adhesion complexes.";
RL Mol. Biol. Cell 14:2492-2507(2003).
RN [5] {ECO:0000305}
RP INTERACTION WITH MOG-6.
RX PubMed=15151984; DOI=10.1242/dev.01154;
RA Belfiore M., Pugnale P., Saudan Z., Puoti A.;
RT "Roles of the C. elegans cyclophilin-like protein MOG-6 in MEP-1 binding
RT and germline fates.";
RL Development 131:2935-2945(2004).
RN [6] {ECO:0000305}
RP INTERACTION WITH LIN-1.
RX PubMed=15689373; DOI=10.1242/dev.01664;
RA Leight E.R., Glossip D., Kornfeld K.;
RT "Sumoylation of LIN-1 promotes transcriptional repression and inhibition of
RT vulval cell fates.";
RL Development 132:1047-1056(2005).
CC -!- FUNCTION: Has a broad role in development, specifically in the genetic
CC pathway SynMuvB that negatively regulates specification of the vulval
CC cell fate. Required for fem-3 3'-UTR-mediated repression in the
CC regulation of the sperm/oocyte switch. Acts by regulating the
CC translation of fem-3 mRNA, by binding to its 3'-UTR.
CC {ECO:0000269|PubMed:12088146, ECO:0000269|PubMed:12507426}.
CC -!- SUBUNIT: Interacts with hda-1, let-418, lin-1, mog-1, mog-4, mog-5,
CC mog-6, pie-1 and unc-98. {ECO:0000269|PubMed:12088146,
CC ECO:0000269|PubMed:12507426, ECO:0000269|PubMed:12808046,
CC ECO:0000269|PubMed:15151984, ECO:0000269|PubMed:15689373}.
CC -!- INTERACTION:
CC Q21502; P52012: cyn-4; NbExp=3; IntAct=EBI-319858, EBI-3513766;
CC Q21502; G5EBZ4: let-418; NbExp=2; IntAct=EBI-319858, EBI-3831970;
CC Q21502; Q21502: mep-1; NbExp=3; IntAct=EBI-319858, EBI-319858;
CC Q21502; P34498: mog-1; NbExp=3; IntAct=EBI-319858, EBI-3651301;
CC Q21502; G5EBT5: mog-3; NbExp=2; IntAct=EBI-319858, EBI-2418038;
CC Q21502; O45244: mog-4; NbExp=2; IntAct=EBI-319858, EBI-326143;
CC Q21502; Q09530: mog-5; NbExp=3; IntAct=EBI-319858, EBI-329912;
CC Q21502; Q94131: pie-1; NbExp=3; IntAct=EBI-319858, EBI-300501;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12088146}. Note=Found
CC in all nuclei in the germline, including oocytes, but not those of
CC mature sperm and spermatocytes. {ECO:0000269|PubMed:12088146}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic cells of embryos, the head,
CC hypodermis and tail of larvae and the germline of adults, including
CC oocytes but not mature sperm and spermatocytes.
CC {ECO:0000269|PubMed:12088146}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in all developmental stages; highest in embryos, decreasing
CC during early larval development (L1-L3) until the fourth larval stage
CC (L4) where it increases. Expression in hermaphrodite adults is mostly
CC contained to the germline. {ECO:0000269|PubMed:12088146}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit temperature-dependent arrested
CC elongation of gonadal arms. Mutants raised at 25 degrees C show reduced
CC numbers of descendants of the gonadal precursors Z1 and Z4, while
CC mutants raised at 15 degrees C show wild type gonadal development.
CC Vulval defects are also temperature sensitive. Mutants grown at 20
CC degrees C showed protruding vulva (80%) and some had pseudovulvae
CC (15%). At 15 degrees C, fewer mutants exhibited everted (36%) or
CC additional small vulvae (7%). {ECO:0000269|PubMed:12088146}.
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DR EMBL; AF416567; AAL27004.1; -; mRNA.
DR EMBL; Z77667; CAB01235.2; -; Genomic_DNA.
DR PIR; T23697; T23697.
DR RefSeq; NP_502173.2; NM_069772.6.
DR AlphaFoldDB; Q21502; -.
DR BioGRID; 43171; 40.
DR IntAct; Q21502; 31.
DR MINT; Q21502; -.
DR STRING; 6239.M04B2.1; -.
DR EPD; Q21502; -.
DR PaxDb; Q21502; -.
DR PeptideAtlas; Q21502; -.
DR PRIDE; Q21502; -.
DR EnsemblMetazoa; M04B2.1.1; M04B2.1.1; WBGene00003218.
DR GeneID; 178074; -.
DR KEGG; cel:CELE_M04B2.1; -.
DR UCSC; M04B2.1; c. elegans.
DR CTD; 38327; -.
DR WormBase; M04B2.1; CE31852; WBGene00003218; mep-1.
DR eggNOG; ENOG502QQXF; Eukaryota.
DR GeneTree; ENSGT00390000000042; -.
DR HOGENOM; CLU_017465_0_0_1; -.
DR InParanoid; Q21502; -.
DR OMA; CKETDTN; -.
DR OrthoDB; 570981at2759; -.
DR PhylomeDB; Q21502; -.
DR SignaLink; Q21502; -.
DR PRO; PR:Q21502; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003218; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Gonadal differentiation;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor; RNA-binding;
KW Sexual differentiation; Zinc; Zinc-finger.
FT CHAIN 1..870
FT /note="MOG interacting and ectopic P-granules protein 1"
FT /id="PRO_0000308521"
FT ZN_FING 421..444
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 450..473
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255"
FT ZN_FING 486..508
FT /note="CCHC-type"
FT /evidence="ECO:0000255"
FT ZN_FING 713..736
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255"
FT ZN_FING 753..776
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255"
FT ZN_FING 794..815
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255"
FT ZN_FING 826..849
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97450 MW; 3BF8924F86B5A6E3 CRC64;
MVTADETVLA TTTNTTSMSV EPTDPRSAGE SSSDSEPDTI EQLKAEQREV MADAANGSEV
NGNQENGKEE AASADVEVIE IDDTEESTDP SPDGSDENGD AASTSVPIEE EARKKDEGAS
EVTVASSEIE QDDDGDVMEI TEEPNGKSED TANGTVTEEV LDEEEPEPSV NGTTEIATEK
EPEDSSMPVE QNGKGVKRPV ECIELDDDDD DEIQEISTPA PAKKAKIDDV KATSVPEEDN
NEQAQKRLLD KLEEYVKEQK DQPSSKSRKV LDTLLGAINA QVQKEPLSVR KLILDKVLVL
PNTISFPPSQ VCDLLIEHDP EMPLTKVINR MFGEERPKLS DSEKRERAQL KQHNPVPNMT
KLLVDIGQDL VQEATYCDIV HAKNLPEVPK NLETYKQVAA QLKPVWETLK RKNEPYKLKM
HRCDVCGFQT ESKLVMSTHK ENLHFTGSKF QCTMCKETDT SEQRMKDHYF ETHLVIAKSE
EKESKYPCAI CEEDFNFKGV REQHYKQCKK DYIRIRNIMM PKQDDHLYIN RWLWERPQLD
PSILQQQQQA ALQQAQQKKQ QQLLHQQQAA QAAAAAQLLR KQQLQQQQQQ QQARLREQQQ
AAQFRQVAQL LQQQSAQAQR AQQNQGNVNH NTLIAAMQAS LRRGGQQGNS LAVSQLLQKQ
MAALKSQQGA QQLQAAVNSM RSQNSQKTPT HRSSKLVTTP SHATVGSSSA PTFVCEICDA
SVQEKEKYLQ HLQTTHKQMV GKVLQDMSQG APLACSRCRD RFWTYEGLER HLVMSHGLVT
ADLLLKAQKK EDGGRCKTCG KNYAFNMLQH LVADHQVKLC SAEIMYSCDV CAFKCSSYQT
LEAHLTSNHP KGDKKTSTPA KKDDCITLDD
