ZNF2_CAEEL
ID ZNF2_CAEEL Reviewed; 422 AA.
AC Q20082;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc finger protein zfp-2 {ECO:0000312|WormBase:F35H8.3};
GN Name=zfp-2 {ECO:0000312|WormBase:F35H8.3};
GN ORFNames=F35H8.3 {ECO:0000312|WormBase:F35H8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17417969; DOI=10.1186/1471-213x-7-30;
RA Ceron J., Rual J.F., Chandra A., Dupuy D., Vidal M., van den Heuvel S.;
RT "Large-scale RNAi screens identify novel genes that interact with the C.
RT elegans retinoblastoma pathway as well as splicing-related components with
RT synMuv B activity.";
RL BMC Dev. Biol. 7:30-30(2007).
CC -!- FUNCTION: Probable zinc finger transcription factor that acts as a
CC transcriptional repressor. Acts redundantly with the transcriptional
CC repressor lin-35 to control the development of somatic gonad lineages.
CC May, in addition, suppress sensitivity to RNAi.
CC {ECO:0000269|PubMed:17417969}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17417969}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval cells and all somatic gonad
CC structures such as spermatheca, sheath cells, uterine cells and distal
CC tip cells. {ECO:0000269|PubMed:17417969}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Double knockout with lin-35
CC results in sterility, defects in gonad migration and vulval morphology.
CC {ECO:0000269|PubMed:17417969}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284602; CAA85325.1; -; Genomic_DNA.
DR PIR; T21820; T21820.
DR RefSeq; NP_496055.1; NM_063654.4.
DR AlphaFoldDB; Q20082; -.
DR SMR; Q20082; -.
DR STRING; 6239.F35H8.3; -.
DR EPD; Q20082; -.
DR PaxDb; Q20082; -.
DR EnsemblMetazoa; F35H8.3.1; F35H8.3.1; WBGene00009448.
DR GeneID; 174505; -.
DR KEGG; cel:CELE_F35H8.3; -.
DR UCSC; F35H8.3; c. elegans.
DR CTD; 174505; -.
DR WormBase; F35H8.3; CE00981; WBGene00009448; zfp-2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000171158; -.
DR HOGENOM; CLU_652527_0_0_1; -.
DR InParanoid; Q20082; -.
DR OMA; QIVEMDG; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q20082; -.
DR PRO; PR:Q20082; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009448; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..422
FT /note="Zinc finger protein zfp-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441015"
FT ZN_FING 171..194
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 255..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..379
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 95..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 48607 MW; CB3BF05E74B00E56 CRC64;
MEEMMMNDPS AMVIYEEEVT TAPNLPCSLI QQRSWDEEKP IGYELTNTKC YKTPNGVQKT
ATIQREQLST SKDFGEQQIV EMDGEFSIEG TDMHAIPCTS SSMQPSTSSN PSSGEHQPVP
LRRMAIKIGQ RVLRFKVISA EEAPEAPLDT QDSWINDPKP VTTPKALAGL YRCTNCKTYF
GNKEVYQRHI QEVHGDARPF RCFNCGMRFA NKTSMTHHLK DHSLLKPMFS CDYCPRIFSK
LESKTRHHKM HFTRSTCQTC MRFFTTEDAL RHHQSTAHPA TFDSGPPPED LLPNGKSARY
SCSYCNLRFH FKKDMLVHER IHTGEKPYSC GYCMKSFAQS QALTAHIRTH TKELPYGCGK
CDKRFRDNSC LRKHELAAHT DEPIVRPISV AYSNQVQKQM QRQRENRRKQ ELLIAERHPY
RI