CNOT7_BOVIN
ID CNOT7_BOVIN Reviewed; 285 AA.
AC Q3ZC01;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic
CC poly(A) RNA substrate. Its function seems to be partially redundant
CC with that of CNOT8. Catalytic component of the CCR4-NOT complex which
CC is one of the major cellular mRNA deadenylases and is linked to various
CC cellular processes including bulk mRNA degradation, miRNA-mediated
CC repression, translational repression during translational initiation
CC and general transcription regulation. During miRNA-mediated repression
CC the complex seems also to act as translational repressor during
CC translational initiation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. Required for miRNA-
CC mediated mRNA deadenylation. Associates with members of the BTG family
CC such as TOB1 and BTG2 and is required for their anti-proliferative
CC activity (By similarity). {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; distinct complexes seem to
CC exist that differ in the participation of probably mutually exclusive
CC catalytic subunits; the complex contains two deadenylase subunits,
CC CNOT6 or CNOT6L, and CNOT7 or CNOT8. In the complex, interacts directly
CC with CNOT1. Interacts with AGO2. Interacts with TOB1; recruited by TOB1
CC to a ternary complex with CPEB3 which is required for mRNA
CC deadenylation and decay. Interacts with BTG1. Interacts with BTG2.
CC Interacts with NANOS2. Interacts with ZFP36, ZFP36L1 and ZFP36L2; these
CC interactions are inhibited in response to phorbol 12-myristate 13-
CC acetate (PMA) treatment in a p38 MAPK-dependent manner. Interacts with
CC BTG4 (By similarity). Interacts with EIF4E; this interaction is
CC increased by CNOT7 interaction with BTG4 (By similarity).
CC {ECO:0000250|UniProtKB:Q60809, ECO:0000250|UniProtKB:Q9UIV1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, P-body
CC {ECO:0000250}. Note=NANOS2 promotes its localization to P-body.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; BC103000; AAI03001.1; -; mRNA.
DR RefSeq; NP_001029484.1; NM_001034312.1.
DR RefSeq; XP_010818548.1; XM_010820246.1.
DR AlphaFoldDB; Q3ZC01; -.
DR SMR; Q3ZC01; -.
DR STRING; 9913.ENSBTAP00000024009; -.
DR PaxDb; Q3ZC01; -.
DR PRIDE; Q3ZC01; -.
DR Ensembl; ENSBTAT00000024009; ENSBTAP00000024009; ENSBTAG00000018036.
DR GeneID; 508055; -.
DR KEGG; bta:508055; -.
DR CTD; 29883; -.
DR VEuPathDB; HostDB:ENSBTAG00000018036; -.
DR VGNC; VGNC:27522; CNOT7.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q3ZC01; -.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR TreeFam; TF314185; -.
DR Reactome; R-BTA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000018036; Expressed in oocyte and 106 other tissues.
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:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
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:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
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:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl.
DR GO; GO:0033962; P:P-body assembly; IEA:Ensembl.
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 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
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..285
FT /note="CCR4-NOT transcription complex subunit 7"
FT /id="PRO_0000313893"
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:0000255"
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:0000255"
SQ SEQUENCE 285 AA; 32718 MW; 2AF23EC38E06EFDB CRC64;
MPAATVDHSQ RICEVWACNL DEEMKKIRQV IRKYNYVAMD TEFPGVVARP IGEFRSNADY
QYQLLRCNVD LLKIIQLGLT FMNEQGEYPP GTSTWQFNFK FNLTEDMYAQ DSIELLTTSG
IQFKKHEEEG IETQYFAELL MTSGVVLCEG VKWLSFHSGY DFGYLIKILT NSNLPEEELD
FFEILRLFFP VIYDVKYLMK SCKNLKGGLQ EVAEQLELER IGPQHQAGSD SLLTGMAFFK
MREMFFEDHI DDAKYCGHLY GLGSGSSYVQ NGTGNAYEEE ASKQS
