CNOT7_MOUSE
ID CNOT7_MOUSE Reviewed; 285 AA.
AC Q60809;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7791755; DOI=10.1128/mcb.15.7.3487;
RA Draper M.P., Salvadore C., Denis C.L.;
RT "Identification of a mouse protein whose homolog in Saccharomyces
RT cerevisiae is a component of the CCR4 transcriptional regulatory complex.";
RL Mol. Cell. Biol. 15:3487-3495(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH BTG1 AND BTG2.
RX PubMed=9712883; DOI=10.1074/jbc.273.35.22563;
RA Rouault J.P., Prevot D., Berthet C., Birot A.M., Billaud M., Magaud J.P.,
RA Corbo L.;
RT "Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the
RT murine homolog of a component of the yeast CCR4 transcriptional regulatory
RT complex.";
RL J. Biol. Chem. 273:22563-22569(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH AGO2.
RX PubMed=19716330; DOI=10.1016/j.molcel.2009.08.004;
RA Fabian M.R., Mathonnet G., Sundermeier T., Mathys H., Zipprich J.T.,
RA Svitkin Y.V., Rivas F., Jinek M., Wohlschlegel J., Doudna J.A., Chen C.Y.,
RA Shyu A.B., Yates J.R. III, Hannon G.J., Filipowicz W., Duchaine T.F.,
RA Sonenberg N.;
RT "Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-dependent
RT deadenylation.";
RL Mol. Cell 35:868-880(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS2.
RX PubMed=20133598; DOI=10.1073/pnas.0908664107;
RA Suzuki A., Igarashi K., Aisaki K., Kanno J., Saga Y.;
RT "NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to
RT suppression of specific RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3594-3599(2010).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22367759; DOI=10.1002/stem.1070;
RA Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P.,
RA Archer T.K., Jothi R., Hu G.;
RT "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit
RT extraembryonic differentiation.";
RL Stem Cells 30:910-922(2012).
RN [8]
RP INTERACTION WITH BTG4 AND EIF4E, AND MUTAGENESIS OF LYS-203.
RX PubMed=27065194; DOI=10.1038/nsmb.3204;
RA Yu C., Ji S.Y., Sha Q.Q., Dang Y., Zhou J.J., Zhang Y.L., Liu Y.,
RA Wang Z.W., Hu B., Sun Q.Y., Sun S.C., Tang F., Fan H.Y.;
RT "BTG4 is a meiotic cell cycle-coupled maternal-zygotic-transition licensing
RT factor in oocytes.";
RL Nat. Struct. Mol. Biol. 23:387-394(2016).
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. {ECO:0000269|PubMed:19716330, ECO:0000269|PubMed:22367759}.
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 (By similarity). In the complex,
CC interacts directly with CNOT1 (By similarity). Interacts with AGO2
CC (PubMed:19716330). Interacts with TOB1; recruited by TOB1 to a ternary
CC complex with CPEB3 which is required for mRNA deadenylation and decay
CC (By similarity). Interacts with BTG1 (PubMed:9712883). Interacts with
CC BTG2 (PubMed:9712883). Interacts with NANOS2 (PubMed:20133598).
CC Interacts with ZFP36, ZFP36L1 and ZFP36L2; these interactions are
CC inhibited in response to phorbol 12-myristate 13-acetate (PMA)
CC treatment in a p38 MAPK-dependent manner (By similarity). Interacts
CC with BTG4 (PubMed:27065194). Interacts with EIF4E; this interaction is
CC increased by CNOT7 interaction with BTG4 (PubMed:27065194).
CC {ECO:0000250|UniProtKB:Q9UIV1, ECO:0000269|PubMed:19716330,
CC ECO:0000269|PubMed:20133598, ECO:0000269|PubMed:27065194,
CC ECO:0000269|PubMed:9712883}.
CC -!- INTERACTION:
CC Q60809; Q04211: Btg2; NbExp=2; IntAct=EBI-2104739, EBI-7847081;
CC Q60809; O70552: Btg4; NbExp=6; IntAct=EBI-2104739, EBI-16204405;
CC Q60809; Q8VEG6: Cnot6l; NbExp=2; IntAct=EBI-2104739, EBI-2104661;
CC Q60809; P62324: BTG1; Xeno; NbExp=5; IntAct=EBI-2104739, EBI-742279;
CC Q60809; P78543: BTG2; Xeno; NbExp=5; IntAct=EBI-2104739, EBI-1047576;
CC Q60809; Q9UKZ1: CNOT11; Xeno; NbExp=3; IntAct=EBI-2104739, EBI-2562014;
CC Q60809; P06730: EIF4E; Xeno; NbExp=2; IntAct=EBI-2104739, EBI-73440;
CC Q60809; Q14106: TOB2; Xeno; NbExp=4; IntAct=EBI-2104739, EBI-2562000;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20133598}. Cytoplasm,
CC P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its
CC localization to P-body.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells.
CC {ECO:0000269|PubMed:22367759}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; U21855; AAA87455.1; -; mRNA.
DR EMBL; BC006021; AAH06021.1; -; mRNA.
DR CCDS; CCDS22253.1; -.
DR RefSeq; NP_001258471.1; NM_001271542.1.
DR RefSeq; NP_035265.1; NM_011135.5.
DR RefSeq; XP_011240485.1; XM_011242183.1.
DR AlphaFoldDB; Q60809; -.
DR SMR; Q60809; -.
DR BioGRID; 202298; 9.
DR DIP; DIP-46843N; -.
DR IntAct; Q60809; 28.
DR MINT; Q60809; -.
DR STRING; 10090.ENSMUSP00000117304; -.
DR iPTMnet; Q60809; -.
DR PhosphoSitePlus; Q60809; -.
DR EPD; Q60809; -.
DR MaxQB; Q60809; -.
DR PaxDb; Q60809; -.
DR PRIDE; Q60809; -.
DR ProteomicsDB; 283408; -.
DR Antibodypedia; 22252; 203 antibodies from 28 providers.
DR DNASU; 18983; -.
DR Ensembl; ENSMUST00000034012; ENSMUSP00000034012; ENSMUSG00000031601.
DR Ensembl; ENSMUST00000132032; ENSMUSP00000122933; ENSMUSG00000031601.
DR Ensembl; ENSMUST00000149992; ENSMUSP00000117304; ENSMUSG00000031601.
DR GeneID; 18983; -.
DR KEGG; mmu:18983; -.
DR UCSC; uc009lmq.2; mouse.
DR CTD; 29883; -.
DR MGI; MGI:1298230; Cnot7.
DR VEuPathDB; HostDB:ENSMUSG00000031601; -.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q60809; -.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q60809; -.
DR TreeFam; TF314185; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR BioGRID-ORCS; 18983; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cnot7; mouse.
DR PRO; PR:Q60809; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60809; protein.
DR Bgee; ENSMUSG00000031601; Expressed in superior cervical ganglion and 285 other tissues.
DR ExpressionAtlas; Q60809; baseline and differential.
DR Genevisible; Q60809; MM.
DR GO; GO:0030014; C:CCR4-NOT complex; IPI:MGI.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IMP:MGI.
DR GO; GO:0033962; P:P-body assembly; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISO:MGI.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
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_0000212845"
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"
FT MUTAGEN 203
FT /note="K->A: Severe decrease of interaction with BTG4."
FT /evidence="ECO:0000269|PubMed:27065194"
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
