ID MEP1_CAEBR Reviewed; 880 AA.
AC Q61SK8; A8X0U0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=MOG interacting and ectopic P-granules protein 1;
DE AltName: Full=Nuclear zinc finger protein;
GN Name=mep-1 {ECO:0000250|UniProtKB:Q21502}; ORFNames=CBG06138;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:Q21502}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q21502}.
CC Note=Found in all nuclei in the germline, including oocytes, but not
CC those of mature sperm and spermatocytes.
CC {ECO:0000250|UniProtKB:Q21502}.
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DR EMBL; HE600986; CAP26250.2; -; Genomic_DNA.
DR AlphaFoldDB; Q61SK8; -.
DR STRING; 6238.Q61SK8; -.
DR EnsemblMetazoa; CBG06138.1; CBG06138.1; WBGene00028458.
DR WormBase; CBG06138; CBP28353; WBGene00028458; Cbr-mep-1.
DR eggNOG; ENOG502QQXF; Eukaryota.
DR HOGENOM; CLU_017465_0_0_1; -.
DR InParanoid; Q61SK8; -.
DR OMA; ETDTNEQ; -.
DR OrthoDB; 2965251at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0002119; P:nematode larval development; ISS:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IEA:EnsemblMetazoa.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24406; TRANSCRIPTIONAL REPRESSOR CTCFL-RELATED; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE 3: Inferred from homology;
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..880
FT /note="MOG interacting and ectopic P-granules protein 1"
FT /id="PRO_0000308520"
FT ZN_FING 436..459
FT /note="C2H2-type 1"
FT ZN_FING 465..488
FT /note="C2H2-type 2"
FT ZN_FING 501..523
FT /note="CCHC-type"
FT ZN_FING 728..751
FT /note="C2H2-type 3"
FT ZN_FING 768..791
FT /note="C2H2-type 4"
FT ZN_FING 809..830
FT /note="C2H2-type 5"
FT ZN_FING 841..864
FT /note="C2H2-type 6"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 99166 MW; C204123CAAB5D529 CRC64;
MVTSDETVLA TTTNKTSITT EPMEPKSSDE STDSETDKIK ILKAEQREAL TEATGSVEVN
GNEENGHVEC ATVDEVAHVE EDKVEEATNS VVDLSSNGSS ATTSVPVEEQ EEKANEDETN
DVVMETSENG ENGKEENGTA MEVAENPAVT ENGSKSDGET ETDRVAIKDS QEDDSEPVNG
SVKPEEKEEK NDTDAPMEEE DQNGKGVKRP VECIQLDDDD DDIQEVSPPV PAKKQKTEET
KQEPKQEAKA EPADDNEQAQ IRLLDKLQEY VGDQRGQPCN KTRKVLDTLL GAINAQVQKE
PLSVRKLILD KVLVLPNTIS FPPSQVCDLL IEHDPEMPLA KVINRMFGEE RPKLSDSEKR
ERQQMKQHNP VSHMTKLLVD IGQDLVQETT YCDIVHAKNL PEIPKNIETY KQVAAQLKPV
WETLKRKNEP YKLKMSRCGV CGFQTESKLA MAAHKETLHF TGSKFQCTLC KETDTNEQRM
KEHYFEAHLI IAKSEEKESK YPCAICEEDF NFKGVREQHY KQCKKDYIRI RNIMMPKQED
HLYLNRWLWE RPPVDPSIIQ QQQAAALQQA EQKKRHQQAL LREQHAQAQA AQLLRKQQLQ
QQQQAQRLRE QQAQAQYRQM AQLIQQQQQQ QNRNNANNMS NSLIQAMQAQ LRRSGTGTSP
QNLNLLQKQM AAVLKNQNPA QIQALVASMN KQTQSPKTPT TPKVAKAAAT PTLPLAMSAS
SSSPGVSFQC EICDQTVHEK DKYLSHLQVL HKQMVGKTLQ DMTQGAPLAC SRCRDRFWTY
EGLERHLVMS HGLVTADLLL KAQKKEDGGR CKTCGKQYAF NMLQHLVADH QVKLCSAEIM
YSCDVCAFKC SSYQTLEAHL SSTHPKSADK KKEELITLDD
//
