DPFF1_CAEEL
ID DPFF1_CAEEL Reviewed; 372 AA.
AC Q09477; A8WFG1; H2KZ28; Q09247;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein dpff-1 {ECO:0000250|UniProtKB:Q92784};
GN Name=dpff-1 {ECO:0000312|WormBase:C28H8.9a};
GN ORFNames=C28H8.9 {ECO:0000312|WormBase:C28H8.9a};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28940692; DOI=10.1002/dvg.23072;
RA Villanueva-Chimal E., Salinas L.S., Fernandez-Cardenas L.P.,
RA Huelgas-Morales G., Cabrera-Wrooman A., Navarro R.E.;
RT "DPFF-1 transcription factor deficiency causes the aberrant activation of
RT MPK-1 and meiotic defects in the Caenorhabditis elegans germline.";
RL Genesis 55:0-0(2017).
CC -!- FUNCTION: Probable transcription factor, involved in meiosis and stress
CC protection. {ECO:0000269|PubMed:28940692}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28940692}. Cytoplasm
CC {ECO:0000269|PubMed:28940692}. Note=Expressed at higher level in
CC nuclei. {ECO:0000269|PubMed:28940692}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:C28H8.9a};
CC IsoId=Q09477-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C28H8.9b};
CC IsoId=Q09477-2; Sequence=VSP_057652, VSP_057653;
CC Name=c {ECO:0000312|WormBase:C28H8.9c};
CC IsoId=Q09477-3; Sequence=VSP_057651, VSP_057652, VSP_057653;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout all embryonic and post-
CC embryonic stages. {ECO:0000269|PubMed:28940692}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces expression of
CC sod-3 (PubMed:28940692). RNAi-mediated knockdown on a cep-1 mutant
CC background increases germ cell apoptosis (PubMed:28940692).
CC {ECO:0000269|PubMed:28940692}.
CC -!- SIMILARITY: Belongs to the requiem/DPF family. {ECO:0000305}.
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DR EMBL; FO080703; CCD65970.1; -; Genomic_DNA.
DR EMBL; FO080703; CCD65971.1; -; Genomic_DNA.
DR EMBL; FO080703; CCD65978.1; -; Genomic_DNA.
DR PIR; F88469; F88469.
DR RefSeq; NP_001122678.1; NM_001129206.2. [Q09477-3]
DR RefSeq; NP_498281.2; NM_065880.5. [Q09477-1]
DR RefSeq; NP_871638.1; NM_181909.3.
DR AlphaFoldDB; Q09477; -.
DR SMR; Q09477; -.
DR BioGRID; 41054; 17.
DR ComplexPortal; CPX-1031; PBAF chromatin remodeling complex.
DR IntAct; Q09477; 12.
DR STRING; 6239.C28H8.9a; -.
DR EPD; Q09477; -.
DR PaxDb; Q09477; -.
DR PeptideAtlas; Q09477; -.
DR EnsemblMetazoa; C28H8.9a.1; C28H8.9a.1; WBGene00016200. [Q09477-1]
DR EnsemblMetazoa; C28H8.9b.1; C28H8.9b.1; WBGene00016200. [Q09477-2]
DR EnsemblMetazoa; C28H8.9c.1; C28H8.9c.1; WBGene00016200. [Q09477-3]
DR GeneID; 175832; -.
DR KEGG; cel:CELE_C28H8.9; -.
DR UCSC; C28H8.9c; c. elegans.
DR CTD; 175832; -.
DR WormBase; C28H8.9a; CE06896; WBGene00016200; dpff-1. [Q09477-1]
DR WormBase; C28H8.9b; CE32813; WBGene00016200; dpff-1. [Q09477-2]
DR WormBase; C28H8.9c; CE41615; WBGene00016200; dpff-1. [Q09477-3]
DR eggNOG; KOG1244; Eukaryota.
DR GeneTree; ENSGT00940000170234; -.
DR HOGENOM; CLU_038980_0_1_1; -.
DR InParanoid; Q09477; -.
DR OMA; TYGSRRW; -.
DR OrthoDB; 708781at2759; -.
DR PhylomeDB; Q09477; -.
DR SignaLink; Q09477; -.
DR PRO; PR:Q09477; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016200; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR025750; DPF1-3_N.
DR InterPro; IPR038047; DPF3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615:SF120; PTHR10615:SF120; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF14051; Requiem_N; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..372
FT /note="Zinc finger protein dpff-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000168157"
FT ZN_FING 212..235
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 256..314
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 316..361
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 108..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 112
FT /note="T -> TVRFA (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057651"
FT VAR_SEQ 182..192
FT /note="VPTTRSSVSRL -> NAARNTKASRV (in isoform b and isoform
FT c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057652"
FT VAR_SEQ 193..372
FT /note="Missing (in isoform b and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057653"
SQ SEQUENCE 372 AA; 42418 MW; 2A6DA04EDDC619B2 CRC64;
MISENGYMDL MRNCIKWNSR QMEDRKKRLR FPYYEHQTAT AQRESRFTTR NVDHMYPSND
PNTVVQFATE RWKKSKSQPP SDAVEMSMFL RENPSIQVAI DHLTPQVVGP TTESVSDSSN
DSTTIRPSRQ TQIKEEYRDD YVLDDELSPD EFGSDEDDWS SRKRRKGNLG PVQKATSSRK
KVPTTRSSVS RLTPSRSIVK ETKYEEPEEK TYPCDKCSAK YKSLAGLSYH QSYLHDQKSS
QPLVKLLSPS IEISTSCDFC SGTAFMNKNT KLPEDLVSCH DCGRSGHPSC LNFNQNVTKI
IKRSGWQCLE CKSCTICGTS ENDDKLLFCD DCDRGYHLYC LTPALEKAPD DEYSCRLCQV
EFGDKASAPA KK
