CNOT6_XENLA
ID CNOT6_XENLA Reviewed; 552 AA.
AC Q5BJ41;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=CCR4-NOT transcription complex subunit 6;
DE EC=3.1.13.4 {ECO:0000269|PubMed:20634287};
DE AltName: Full=Cytoplasmic deadenylase;
GN Name=cnot6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20634287; DOI=10.1074/jbc.m110.150763;
RA Cooke A., Prigge A., Wickens M.;
RT "Translational repression by deadenylases.";
RL J. Biol. Chem. 285:28506-28513(2010).
CC -!- FUNCTION: Poly(A) nuclease involved in mRNA decay. Has 3'-5' RNase
CC activity (PubMed:20634287). The CCR4-NOT complex functions as general
CC transcription regulation complex (By similarity). Enhances ligand-
CC dependent transcriptional activity of nuclear hormone receptors (By
CC similarity). {ECO:0000250|UniProtKB:Q9ULM6,
CC ECO:0000269|PubMed:20634287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:20634287};
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: Subunit of the CCR4-NOT core complex.
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}.
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DR EMBL; BC091632; AAH91632.1; -; mRNA.
DR RefSeq; NP_001184194.1; NM_001197265.1.
DR AlphaFoldDB; Q5BJ41; -.
DR SMR; Q5BJ41; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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 1: Evidence at protein 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..552
FT /note="CCR4-NOT transcription complex subunit 6"
FT /id="PRO_0000218576"
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..552
FT /note="Nuclease domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 407
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
SQ SEQUENCE 552 AA; 62776 MW; 5DC598040C453EFD CRC64;
MPKEKYEPPD PRRMYTIMSS EEAANGKKSH WAELEISGKV RSLSSSLWSL THLTALHLSD
NSLSCIPSDI AKLHNLVYLD LSHNQIQSLP AELGNMVSLR ELHLNYNQLR VLPFELGKLF
QLQTLSLKGN PLTQDILNLC LEPDGTRRLL NYLLDNLSVS TEQPPPRSWI MLQEPDRTRP
TALFSVMCYN VLCDKYATRQ LYGYCPSWAL NWDYRKKAII QEILSCNADI ISLQEVETEQ
YYSFFLVELK ERGYNGFFSP KSRARTMSEQ ERKHVDGCAI FFKTEKFTLV QKHTVEFNQL
AMANSEGSEA MLNRVMTKDN IGVAVLLELR KELIEMSSGK PHLGTEKQLI LVANAHMHWD
PEYSDVKLVQ TMMFLSEVKN IIDKASRSLK SSVLGECGTI PLVLCADLNS LPDSGVVEYL
STGGVETNHK DFKELRYNES LTNFSCNGKN GMTNGRITHG FKLKSAYENG LMPYTNYTFD
FKGIIDYIFY SKPQLNTLAI LGPLDHHWLV ENNISGCPHP LIPSDHFSLF AQLELLLPFL
PQVNGIHLPG RR
