CNOT7_XENLA
ID CNOT7_XENLA Reviewed; 285 AA.
AC Q3KQ85;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20634287; DOI=10.1074/jbc.m110.150763;
RA Cooke A., Prigge A., Wickens M.;
RT "Translational repression by deadenylases.";
RL J. Biol. Chem. 285:28506-28513(2010).
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.
CC {ECO:0000269|PubMed:20634287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:20634287};
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:0000305}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; BC106339; AAI06340.1; -; mRNA.
DR RefSeq; NP_001089689.1; NM_001096220.1.
DR AlphaFoldDB; Q3KQ85; -.
DR SMR; Q3KQ85; -.
DR MaxQB; Q3KQ85; -.
DR DNASU; 734751; -.
DR GeneID; 734751; -.
DR KEGG; xla:734751; -.
DR CTD; 734751; -.
DR Xenbase; XB-GENE-969328; cnot7.S.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 734751; Expressed in testis and 19 other tissues.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein 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..285
FT /note="CCR4-NOT transcription complex subunit 7"
FT /id="PRO_0000313896"
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 285 AA; 32763 MW; 4B17A377859B0F58 CRC64;
MPAATVDHSQ RICEVWACNL DDQMKRIRQV IRKYNYVAMD TEFPGVVARP IGEFRSNADY
QYQLLRCNVD LLKIIQLGLT FMNEQGEYPP GTSTWQFNFK FNLTEDMYAQ DSIELLTSSG
IQFKKHEEEG IETQYFAELF MTSGVVLCEG VKWLSFHSGY DFGYLIKILT NSNLPEVEQD
FFEILRLFFP VIYDVKYLMK SCKNLKGGLQ EVAEQLELER IGPQHQAGSD SLLTGMAFFK
MREMFFEDHI DDAKYCGHLY GLGSGSSYVQ NGTGNAYEEE ANKQS
