CNOT6_RAT
ID CNOT6_RAT Reviewed; 557 AA.
AC Q6AXU9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=CCR4-NOT transcription complex subunit 6;
DE EC=3.1.13.4 {ECO:0000250|UniProtKB:Q9ULM6};
DE AltName: Full=CCR4 carbon catabolite repression 4-like;
DE AltName: Full=Carbon catabolite repressor protein 4 homolog;
DE AltName: Full=Cytoplasmic deadenylase;
GN Name=Cnot6; Synonyms=Ccr4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Poly(A) nuclease with 3'-5' RNase activity. Catalytic
CC component of the CCR4-NOT complex which is one of the major cellular
CC mRNA deadenylases and is linked to various cellular processes including
CC bulk mRNA degradation, miRNA-mediated repression, translational
CC repression during translational initiation and general transcription
CC regulation. Additional complex functions may be a consequence of its
CC influence on mRNA expression. Involved in mRNA decay mediated by the
CC major-protein-coding determinant of instability (mCRD) of the FOS gene
CC in the cytoplasm. In the presence of ZNF335, enhances ligand-dependent
CC transcriptional activity of nuclear hormone receptors. Mediates cell
CC proliferation and cell survival and prevents cellular senescence.
CC {ECO:0000250|UniProtKB:Q9ULM6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000250|UniProtKB:Q9ULM6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96LI5};
CC Note=Binds 2 magnesium ions, but the ions interact each with only 1 or
CC 2 residues. {ECO:0000250|UniProtKB:Q96LI5};
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. Interacts with CNOT7 and CNOT8.
CC Interacts with UNR. Interacts with ZFP36L1 (via N-terminus). Interacts
CC with ZNF335. {ECO:0000250|UniProtKB:Q8K3P5,
CC ECO:0000250|UniProtKB:Q9ULM6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LI5}. Nucleus
CC {ECO:0000250|UniProtKB:Q96LI5}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q96LI5}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079308; AAH79308.1; -; mRNA.
DR RefSeq; NP_001013878.1; NM_001013856.1.
DR AlphaFoldDB; Q6AXU9; -.
DR SMR; Q6AXU9; -.
DR STRING; 10116.ENSRNOP00000003752; -.
DR PhosphoSitePlus; Q6AXU9; -.
DR PaxDb; Q6AXU9; -.
DR Ensembl; ENSRNOT00000084509; ENSRNOP00000074431; ENSRNOG00000054891.
DR GeneID; 287249; -.
DR KEGG; rno:287249; -.
DR UCSC; RGD:1310783; rat.
DR CTD; 57472; -.
DR RGD; 1310783; Cnot6.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000158978; -.
DR InParanoid; Q6AXU9; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; Q6AXU9; -.
DR Reactome; R-RNO-429947; Deadenylation of mRNA.
DR Reactome; R-RNO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:Q6AXU9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004532; F:exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; ISS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; ISO:RGD.
DR CDD; cd10313; Deadenylase_CCR4a; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR034966; Cnot6.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 4.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..557
FT /note="CCR4-NOT transcription complex subunit 6"
FT /id="PRO_0000218575"
FT REPEAT 52..73
FT /note="LRR 1"
FT REPEAT 75..96
FT /note="LRR 2"
FT REPEAT 98..120
FT /note="LRR 3"
FT REPEAT 121..143
FT /note="LRR 4"
FT REGION 153..557
FT /note="Nuclease domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
SQ SEQUENCE 557 AA; 63304 MW; E2780FC2D56EF3F7 CRC64;
MPKEKYEPPD PRRMYTIMSS EEAANGKKSH WAELEISGKV RSLSSSLWSL THLTALHLSD
NSLSCIPSDI AKLHNLVYLD LSHNQIQSLP AELGNMVSLR ELHLNYNQLR VLPFELGKLF
QLQTLSLKGN PLTQDILNLC LEPDGTRRLL NYLLDNLSGT AKRISTEQPP PRSWIMLQEP
DRTRPTALFS VMCYNVLCDK YATRQLYGYC PSWALNWDYR KKAIIQEILS CNADIISLQE
VETEQYYSFF LVELKERGYN GFFSPKSRAR TMSEQERKHV DGCAIFFKTE KFTLVQKHTV
EFNQLAMANS EGSEAMLNRV MTKDNIGVAV LLELRKELIE MSSGKPHLGT EKQLILVANA
HMHWDPEYSD VKLVQTMMFL SEVKNIIDKA SRSLKSSVLG ECGTIPLVLC ADLNSLPDSG
VVEYLSTGGV ETNHKDFKEL RYNESLTNFS CNGKNGMTNG RITHGFKLKS AYENGLMPYT
NYTFDFKGII DYIFYSKPQL NTLAILGPLD HHWLVENNIS GCPHPLIPSD HFSLFAQLEL
LLPFLPQVNG IHLPGRR
