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Database: UniProt
Entry: A0A452DSF3_CAPHI
LinkDB: A0A452DSF3_CAPHI
Original site: A0A452DSF3_CAPHI 
ID   A0A452DSF3_CAPHI        Unreviewed;       555 AA.
AC   A0A452DSF3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=poly(A)-specific ribonuclease {ECO:0000256|ARBA:ARBA00012161};
DE            EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
GN   Name=CNOT6L {ECO:0000313|Ensembl:ENSCHIP00000002694.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000002694.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000002694.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000002694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001663};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CCR4/nocturin family.
CC       {ECO:0000256|ARBA:ARBA00010774}.
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DR   EMBL; LWLT01000006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005681862.1; XM_005681805.2.
DR   AlphaFoldDB; A0A452DSF3; -.
DR   SMR; A0A452DSF3; -.
DR   STRING; 9925.ENSCHIP00000002694; -.
DR   Ensembl; ENSCHIT00000008548.1; ENSCHIP00000002694.1; ENSCHIG00000006297.1.
DR   GeneID; 102191783; -.
DR   KEGG; chx:102191783; -.
DR   CTD; 246175; -.
DR   GeneTree; ENSGT00940000157298; -.
DR   OrthoDB; 37764at2759; -.
DR   Proteomes; UP000291000; Chromosome 6.
DR   Bgee; ENSCHIG00000006297; Expressed in thymus and 17 other cell types or tissues.
DR   GO; GO:0030014; C:CCR4-NOT complex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:Ensembl.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd10312; Deadenylase_CCR4b; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR034967; Deadenylase_CCR4b.
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   PANTHER; PTHR12121; CARBON CATABOLITE REPRESSOR PROTEIN 4; 1.
DR   PANTHER; PTHR12121:SF35; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 6-LIKE; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          193..529
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
SQ   SEQUENCE   555 AA;  63001 MW;  C6E94F1BAE222241 CRC64;
     MRLIGMPKEK YDPPDPRRIY TIMSAEEVAN GKKSHWAELE ISGRVRSLST SLWSLTHLTA
     LHLNDNYLSR IPPDIAKLHN LVYLDLSSNK LRSLPAELGN MVSLRELLLN NNLLRVLPYE
     LGRLFQLQTL GLKGNPLSQD ILNLYQDPDG TRKLLNFMLD NLAVHPEQLP PRPWITLKER
     DQILPSASFT VMCYNVLCDK YATRQLYGYC PSWALNWEYR KKGIMEEIVN CDADIISLQE
     VETEQYFTLF LPALKERGYD GFFSPKSRAK IMSEQERKHV DGCAIFFKTE KFTLVQKHTV
     EFNQVAMANS DGSEAMLNRV MTKDNIGVAV VLEVHKELFG AGMKPIHAAD KQLLIVANAH
     MHWDPEYSDV KLIQTMMFVS EVKNILEKAS SRPGSPTADP NSIPLVLCAD LNSLPDSGVV
     EYLSNGGVAD NHKDFKELRY NECLMNFSCN GKNGSSEGRI THGFQLKSAY ENNLMPYTNY
     TFDFKGVIDY IFYSKTHMNV LGVLGPLDPQ WLVENNITGC PHPHIPSDHF SLLTQLELHP
     PLLPLVNGVH LPNRR
//
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