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CNOT7_XENTR
ID   CNOT7_XENTR             Reviewed;         285 AA.
AC   A4II96;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR   EMBL; BC135920; AAI35921.1; -; mRNA.
DR   RefSeq; NP_001096375.1; NM_001102905.1.
DR   RefSeq; XP_017949366.1; XM_018093877.1.
DR   AlphaFoldDB; A4II96; -.
DR   SMR; A4II96; -.
DR   STRING; 8364.ENSXETP00000001564; -.
DR   PaxDb; A4II96; -.
DR   DNASU; 100124970; -.
DR   Ensembl; ENSXETT00000001564; ENSXETP00000001564; ENSXETG00000000701.
DR   GeneID; 100124970; -.
DR   KEGG; xtr:100124970; -.
DR   CTD; 29883; -.
DR   Xenbase; XB-GENE-969324; cnot7.
DR   eggNOG; KOG0304; Eukaryota.
DR   InParanoid; A4II96; -.
DR   OrthoDB; 931256at2759; -.
DR   Reactome; R-XTR-429947; Deadenylation of mRNA.
DR   Reactome; R-XTR-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000701; Expressed in skeletal muscle tissue and 13 other tissues.
DR   ExpressionAtlas; A4II96; baseline and differential.
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: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..285
FT                   /note="CCR4-NOT transcription complex subunit 7"
FT                   /id="PRO_0000313897"
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;  32691 MW;  C7E66DED7CB3696D CRC64;
     MPAATVDLSQ RICEVWACNL DDQMKRIRQV IRKYNYVAMD TEFPGVVARP IGEFRSNADY
     QYQLLRCNVD LLKIIQLGLT FVNEQGEYPP GTSTWQFNFK FNLTEDMYAQ DSIELLTSSG
     IQFKKHEEEG IETQYFAELF MTSGVVLCEG VKWLSFHSGY DFGYLIKILT NSNLPEVELD
     FFEILRLFFP VIYDVKYLMK SCKNLKGGLQ EVAEQLELKR IGPQHQAGSD SLLTGMAFFK
     MREMFFEDHI DDAKYCGHLY GLGSGSSYVQ NGTGNAYEEE ANKQS
 
 
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