ID A0A384DPX9_URSMA Unreviewed; 285 AA. AC A0A384DPX9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-AUG-2022, entry version 19. DE RecName: Full=CCR4-NOT transcription complex subunit 7 {ECO:0000256|ARBA:ARBA00014176}; DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161}; DE AltName: Full=CCR4-associated factor 1 {ECO:0000256|ARBA:ARBA00032531}; GN Name=CNOT7 {ECO:0000313|Ensembl:ENSUMAP00000028376, GN ECO:0000313|RefSeq:XP_008709117.1, ECO:0000313|RefSeq:XP_040499248.1}; OS Ursus maritimus (Polar bear) (Thalarctos maritimus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus. OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008709117.1}; RN [1] {ECO:0000313|Ensembl:ENSUMAP00000028376} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2019) to UniProtKB. RN [2] {ECO:0000313|RefSeq:XP_008709117.1, ECO:0000313|RefSeq:XP_040499248.1} RP IDENTIFICATION. RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008709117.1, RC ECO:0000313|RefSeq:XP_040499248.1}; RG RefSeq; RL Submitted (APR-2022) 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=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|ARBA:ARBA00001941}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the CAF1 family. CC {ECO:0000256|ARBA:ARBA00008372}. 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 RefSeq; XP_008709117.1; XM_008710895.1. DR RefSeq; XP_008709117.1; XM_008710895.2. DR RefSeq; XP_040499248.1; XM_040643314.1. DR STRING; 29073.XP_008709117.1; -. DR Ensembl; ENSUMAT00000033570.1; ENSUMAP00000028376.1; ENSUMAG00000020629.1. DR GeneID; 103681341; -. DR KEGG; umr:103681341; -. DR CTD; 29883; -. DR GeneTree; ENSGT00390000000080; -. DR OMA; DTKWISF; -. DR Proteomes; UP000261680; Unplaced. DR GO; GO:0030014; C:CCR4-NOT complex; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0000932; C:P-body; IEA:Ensembl. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:Ensembl. DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl. DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IEA:Ensembl. DR GO; GO:0031047; P:gene silencing by RNA; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl. DR GO; GO:0033962; P:P-body assembly; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl. DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl. DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl. 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 3: Inferred from homology; KW Reference proteome {ECO:0000313|Proteomes:UP000261680}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. SQ SEQUENCE 285 AA; 32745 MW; 2AF23ED27E06EFDB 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 ANKQS //