CNOT7_CHICK
ID CNOT7_CHICK Reviewed; 285 AA.
AC Q5ZJV9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, 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; ORFNames=RCJMB04_15f9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720325; CAG31984.1; -; mRNA.
DR RefSeq; NP_001006454.1; NM_001006454.1.
DR RefSeq; XP_015140922.1; XM_015285436.1.
DR AlphaFoldDB; Q5ZJV9; -.
DR SMR; Q5ZJV9; -.
DR STRING; 9031.ENSGALP00000022159; -.
DR PaxDb; Q5ZJV9; -.
DR Ensembl; ENSGALT00000022198; ENSGALP00000022159; ENSGALG00000013649.
DR Ensembl; ENSGALT00000072687; ENSGALP00000051058; ENSGALG00000013649.
DR GeneID; 422733; -.
DR KEGG; gga:422733; -.
DR CTD; 29883; -.
DR VEuPathDB; HostDB:geneid_422733; -.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q5ZJV9; -.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q5ZJV9; -.
DR TreeFam; TF314185; -.
DR Reactome; R-GGA-429947; Deadenylation of mRNA.
DR Reactome; R-GGA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:Q5ZJV9; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000013649; Expressed in colon and 13 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; IBA:GO_Central.
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_0000313894"
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; 32745 MW; 2AF23ED27E06EFDB 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 ANKQS
