CNO6L_DANRE
ID CNO6L_DANRE Reviewed; 559 AA.
AC A2BHJ4; Q502N1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=CCR4-NOT transcription complex subunit 6-like;
DE EC=3.1.13.4 {ECO:0000250|UniProtKB:Q96LI5};
GN Name=cnot6l; ORFNames=si:dkey-58f10.2, zgc:111987;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000250|UniProtKB:Q96LI5};
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.
CC {ECO:0000250|UniProtKB:Q96LI5}.
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; BX640512; CAM16193.1; -; Genomic_DNA.
DR EMBL; BC095634; AAH95634.1; -; mRNA.
DR RefSeq; NP_001018474.1; NM_001020638.1.
DR RefSeq; XP_005165372.1; XM_005165315.3.
DR AlphaFoldDB; A2BHJ4; -.
DR SMR; A2BHJ4; -.
DR STRING; 7955.ENSDARP00000071278; -.
DR PaxDb; A2BHJ4; -.
DR PeptideAtlas; A2BHJ4; -.
DR Ensembl; ENSDART00000076807; ENSDARP00000071278; ENSDARG00000054597.
DR Ensembl; ENSDART00000182886; ENSDARP00000156384; ENSDARG00000054597.
DR GeneID; 553665; -.
DR KEGG; dre:553665; -.
DR CTD; 246175; -.
DR ZFIN; ZDB-GENE-050522-302; cnot6l.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000157298; -.
DR HOGENOM; CLU_016428_4_2_1; -.
DR InParanoid; A2BHJ4; -.
DR OMA; YHFPSDH; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; A2BHJ4; -.
DR TreeFam; TF323175; -.
DR Reactome; R-DRE-429947; Deadenylation of mRNA.
DR Reactome; R-DRE-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR PRO; PR:A2BHJ4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000054597; Expressed in muscle tissue and 20 other tissues.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
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 Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat; Magnesium;
KW Metal-binding; mRNA processing; Nuclease; Nucleus; Reference proteome;
KW Repeat; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..559
FT /note="CCR4-NOT transcription complex subunit 6-like"
FT /id="PRO_0000315251"
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 1..550
FT /note="Nuclease domain"
FT /evidence="ECO:0000250"
FT REGION 1..148
FT /note="Required for interaction with cnot1, cnot3 and
FT cnot7"
FT /evidence="ECO:0000250"
FT ACT_SITE 405
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 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT CONFLICT 88
FT /note="S -> G (in Ref. 2; AAH95634)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="K -> E (in Ref. 2; AAH95634)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="T -> A (in Ref. 2; AAH95634)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="P -> H (in Ref. 2; AAH95634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 63378 MW; 09F1E8775FF7DBA0 CRC64;
MPKEKYDPPD PRRLYTIMSA EEVASGKKSH WTELEISGRV RSLSSSLWTL THLTALHINN
NNLSRIPPEI AKLPHLVYLN LSSNKLRSLP AELGNMVTLR ELLLNNNCLR VLPYELGRLF
QLQTLGLKGN PLSQDILNLY QEPDGTRKLL NYMLDNLAVH PEQLPQRPWI TLRERDQMMP
TAVFTVMCYN VLCDKYATRQ LYGYCPSWAL NWEYRKKGIM EEITNCDADI ISLQEVETEQ
YYTFFLETLK DRGYDGFFCP KSRAKLVSEQ ERKHVDGCGV FFKTEKFALV QKHTVEFNQV
AMANSEGSEV MLNRVMTKDN IGVAVLLEVK KDLFATGLKP PPEKQLLLVA NAHMHWDPEY
SDVKLIQTMM FLSELKSIAE RASGSINSSS PTSETSSIPI VLCADLNSLP DSGVVEYLSN
GGVAENHKDF KELRYSDCLT NFSCNGKNGK PDGSITHSFQ LKSAYEGNLM PYTNYTYDFK
GVIDYIFFSK THMSVLGVLG PLETQWLKDN NITGCPHPHI PSDHFSLLAQ LEYHPPLPPL
NGLHLPVHST ACESKMLTE
