CNOT7_CAEEL
ID CNOT7_CAEEL Reviewed; 310 AA.
AC Q17345;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=CCR4-NOT transcription complex subunit 7;
DE EC=3.1.13.4 {ECO:0000305|PubMed:23843623};
DE AltName: Full=CCR4-associated factor 1;
DE Short=CAF1;
GN Name=ccf-1 {ECO:0000312|WormBase:Y56A3A.20};
GN ORFNames=Y56A3A.20 {ECO:0000312|WormBase:Y56A3A.20};
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 [MRNA].
RX PubMed=7791755; DOI=10.1128/mcb.15.7.3487;
RA Draper M.P., Salvadore C., Denis C.L.;
RT "Identification of a mouse protein whose homolog in Saccharomyces
RT cerevisiae is a component of the CCR4 transcriptional regulatory complex.";
RL Mol. Cell. Biol. 15:3487-3495(1995).
RN [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]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE CCR4-NOT COMPLEX,
RP INTERACTION WITH LET-711, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23843623; DOI=10.1242/jcs.132936;
RA Nousch M., Techritz N., Hampel D., Millonigg S., Eckmann C.R.;
RT "The Ccr4-Not deadenylase complex constitutes the main poly(A) removal
RT activity in C. elegans.";
RL J. Cell Sci. 126:4274-4285(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28204614; DOI=10.1093/nar/gkw872;
RA Wu E., Vashisht A.A., Chapat C., Flamand M.N., Cohen E., Sarov M.,
RA Tabach Y., Sonenberg N., Wohlschlegel J., Duchaine T.F.;
RT "A continuum of mRNP complexes in embryonic microRNA-mediated silencing.";
RL Nucleic Acids Res. 45:2081-2098(2017).
CC -!- FUNCTION: Catalytic component of the CCR4-NOT complex which is one of
CC the major cellular mRNA deadenylases and is linked to various cellular
CC processes including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation (PubMed:23843623, PubMed:28204614). Within the
CC complex, plays a role in miRNA-mediated deadenylation in embryos
CC (PubMed:28204614). Within the complex promotes germ cell development
CC and fertility in hermaphrodites (PubMed:23843623). Additional complex
CC functions may be a consequence of its influence on mRNA expression.
CC {ECO:0000269|PubMed:23843623, ECO:0000269|PubMed:28204614}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000305|PubMed:23843623};
CC -!- SUBUNIT: Component of the CCR4-NOT complex at least composed of ccf-1,
CC ccr-4 and let-711, which is required for germ cell development in
CC hermaphrodites (PubMed:23843623). Within the complex interacts with
CC let-711 (PubMed:23843623). {ECO:0000269|PubMed:23843623}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the germline (PubMed:23843623).
CC In particular, highly expressed in germ cells that enter meiosis and
CC progress through the pachytene stage (PubMed:23843623).
CC {ECO:0000269|PubMed:23843623}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages in males and
CC hermaphrodites (PubMed:23843623). Expressed at low levels in embryos
CC and L1 stage larvae (PubMed:23843623). {ECO:0000269|PubMed:23843623}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown either results in
CC sterility or a reduced brood size (PubMed:23843623). RNAi-mediated
CC knockdown disrupts the arrangement, differentiation and maturation of
CC oocytes in the proximal region and as a result small oocyte-like cells
CC arrange in several rows in the germline (PubMed:23843623). RNAi-
CC mediated knockdown reduces miRNA-mediated deadenylation
CC (PubMed:28204614). RNAi-mediated knockdown reduces ccr-4 and ntl-1
CC protein levels (PubMed:28204614). In another study, RNAi-mediated
CC knockdown does not alter the levels of let-711 or ccr-4
CC (PubMed:23843623). RNAi-mediated knockdown results in reduced global
CC poly(A) tail deadenylation (PubMed:23843623).
CC {ECO:0000269|PubMed:23843623, ECO:0000269|PubMed:28204614}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; U21854; AAA87454.1; -; mRNA.
DR EMBL; BX284603; CAB60501.1; -; Genomic_DNA.
DR RefSeq; NP_499553.1; NM_067152.6.
DR AlphaFoldDB; Q17345; -.
DR SMR; Q17345; -.
DR BioGRID; 41805; 20.
DR ComplexPortal; CPX-634; Ccr4-Not complex.
DR DIP; DIP-29083N; -.
DR IntAct; Q17345; 4.
DR STRING; 6239.Y56A3A.20; -.
DR EPD; Q17345; -.
DR PaxDb; Q17345; -.
DR PeptideAtlas; Q17345; -.
DR EnsemblMetazoa; Y56A3A.20.1; Y56A3A.20.1; WBGene00000369.
DR GeneID; 176625; -.
DR KEGG; cel:CELE_Y56A3A.20; -.
DR UCSC; Y56A3A.20.1; c. elegans.
DR CTD; 176625; -.
DR WormBase; Y56A3A.20; CE22588; WBGene00000369; ccf-1.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q17345; -.
DR OMA; RTPNCAS; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q17345; -.
DR SignaLink; Q17345; -.
DR PRO; PR:Q17345; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000369; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:WormBase.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:0000932; C:P-body; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10797; PTHR10797; 1.
DR Pfam; PF04857; CAF1; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Translation regulation.
FT CHAIN 1..310
FT /note="CCR4-NOT transcription complex subunit 7"
FT /id="PRO_0000212848"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 33838 MW; AC07E23BFFD1E5B0 CRC64;
MASSSSGGAG GAGGASGAPE VKIHNVYMSN VEEEFARIRG FVEDYPYVAM DTEFPGVVAT
PLGTFRSKED FNYQQVFCNV NMLKLIQVGF AMVNDKGELP PTGDVWQFNF NFSFAEDMFS
HESVEMLRQA GIDFTLLQNN GIPTAVFGEL LTTSGLITDP RITWLTFSSG YDFGYLLKSI
TLGDLPKEES TFFMCHKTLF PTSFDIKILL RTPNCASAKL KGGLQEVADQ LDVKRQGVRH
QAGSDALLTA ATFFKIKKQF FGDNWNQIAP LICGHMFGLG SSLSLFHSSG STSRLGDETP
QGLIGVPQQA
