CNOT7_DANRE
ID CNOT7_DANRE Reviewed; 286 AA.
AC Q08BM8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=CCR4-NOT transcription complex subunit 7;
DE EC=3.1.13.4;
DE AltName: Full=CCR4-associated factor 1;
DE Short=CAF-1;
GN Name=cnot7; Synonyms=caf1; ORFNames=zgc:153168;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic
CC poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex
CC which is one of the major cellular mRNA deadenylases and is linked to
CC various cellular processes including bulk mRNA degradation, miRNA-
CC mediated repression, translational repression during translational
CC initiation and general transcription regulation. During miRNA-mediated
CC repression the complex seems also to act as translational repressor
CC during translational initiation. Additional complex functions may be a
CC consequence of its influence on mRNA expression (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit with RNAase activity
CC being higher in presence of Mn(2+) than of Mg(2+) or Co(2+).
CC {ECO:0000250};
CC -!- SUBUNIT: Component of the CCR4-NOT complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; BC124650; AAI24651.1; -; mRNA.
DR RefSeq; NP_001070723.1; NM_001077255.1.
DR RefSeq; XP_017214517.1; XM_017359028.1.
DR AlphaFoldDB; Q08BM8; -.
DR SMR; Q08BM8; -.
DR STRING; 7955.ENSDARP00000087385; -.
DR PaxDb; Q08BM8; -.
DR PRIDE; Q08BM8; -.
DR Ensembl; ENSDART00000092953; ENSDARP00000087385; ENSDARG00000032116.
DR Ensembl; ENSDART00000180961; ENSDARP00000151775; ENSDARG00000115413.
DR Ensembl; ENSDART00000186864; ENSDARP00000156128; ENSDARG00000032116.
DR GeneID; 768119; -.
DR KEGG; dre:768119; -.
DR CTD; 29883; -.
DR ZFIN; ZDB-GENE-061013-29; cnot7.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q08BM8; -.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q08BM8; -.
DR TreeFam; TF314185; -.
DR Reactome; R-DRE-429947; Deadenylation of mRNA.
DR Reactome; R-DRE-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:Q08BM8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000032116; Expressed in mature ovarian follicle and 25 other tissues.
DR ExpressionAtlas; Q08BM8; baseline.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0004532; F:exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:ZFIN.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR039636; CNOT7.
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 PANTHER; PTHR10797:SF2; PTHR10797:SF2; 1.
DR Pfam; PF04857; CAF1; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; Repressor; RNA-binding;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..286
FT /note="CCR4-NOT transcription complex subunit 7"
FT /id="PRO_0000313895"
FT BINDING 40
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 40
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 42
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 161
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 230
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 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 32876 MW; 98916F3D24A7B539 CRC64;
MPAATVDHSQ RICEVWACNL EEEMKRIRQV TRKFNYIAMD TEFPGVVARP IGEFRSNADY
QYQLLRCNVD LLKIIQLGLT FMNEQGEYPP GTSTWQFNFK FNLTEDMYAQ DSIELLTSSG
IQFKKHEEEG IETMYFAELL MTSGVVLCEG VKWLSFHSGY DFGYLIKILS NSKLPDEEVD
FFEILRLFFP IIYDVKYLMK SCKNLKGGLQ EVAEQLELER IGPQHQAGSD SLLTGMAFFK
MREMFFEDHI DDAKYCGHLY GLGSGSSYVQ NGTGNAYEEE ANKQQS
