CNOT8_MOUSE
ID CNOT8_MOUSE Reviewed; 292 AA.
AC Q9D8X5; Q3U532;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=CCR4-NOT transcription complex subunit 8;
DE EC=3.1.13.4;
DE AltName: Full=CCR4-associated factor 8;
GN Name=Cnot8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Pancreas, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22367759; DOI=10.1002/stem.1070;
RA Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P.,
RA Archer T.K., Jothi R., Hu G.;
RT "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit
RT extraembryonic differentiation.";
RL Stem Cells 30:910-922(2012).
RN [4]
RP INTERACTION WITH BTG4.
RX PubMed=27065194; DOI=10.1038/nsmb.3204;
RA Yu C., Ji S.Y., Sha Q.Q., Dang Y., Zhou J.J., Zhang Y.L., Liu Y.,
RA Wang Z.W., Hu B., Sun Q.Y., Sun S.C., Tang F., Fan H.Y.;
RT "BTG4 is a meiotic cell cycle-coupled maternal-zygotic-transition licensing
RT factor in oocytes.";
RL Nat. Struct. Mol. Biol. 23:387-394(2016).
CC -!- FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic
CC poly(A) RNA substrate. Its function seems to be partially redundant
CC with that of CNOT7. Catalytic component of the CCR4-NOT complex which
CC is linked to various cellular processes including bulk mRNA
CC degradation, miRNA-mediated repression, translational repression during
CC translational initiation and general transcription regulation. During
CC miRNA-mediated repression the complex seems also to act as
CC translational repressor during translational initiation. Additional
CC complex functions may be a consequence of its influence on mRNA
CC expression. Associates with members of the BTG family such as TOB1 and
CC BTG2 and is required for their anti-proliferative activity.
CC {ECO:0000269|PubMed:22367759}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
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. In the complex interacts directly
CC with CNOT1. Interacts with BTG1, BTG2 and TOB1 (By similarity).
CC Interacts with BTG4 (PubMed:27065194). {ECO:0000250|UniProtKB:Q9UFF9,
CC ECO:0000269|PubMed:27065194}.
CC -!- INTERACTION:
CC Q9D8X5; Q04211: Btg2; NbExp=3; IntAct=EBI-16204625, EBI-7847081;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells.
CC {ECO:0000269|PubMed:22367759}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; AK007581; BAB25119.1; -; mRNA.
DR EMBL; AK075727; BAC35913.1; -; mRNA.
DR EMBL; AK150757; BAE29826.1; -; mRNA.
DR EMBL; AK153907; BAE32248.1; -; mRNA.
DR EMBL; BC004040; AAH04040.1; -; mRNA.
DR CCDS; CCDS24722.1; -.
DR RefSeq; NP_081225.1; NM_026949.3.
DR RefSeq; XP_006534165.1; XM_006534102.1.
DR RefSeq; XP_006534166.1; XM_006534103.3.
DR RefSeq; XP_006534167.1; XM_006534104.1.
DR RefSeq; XP_006534168.1; XM_006534105.1.
DR RefSeq; XP_006534169.1; XM_006534106.3.
DR AlphaFoldDB; Q9D8X5; -.
DR SMR; Q9D8X5; -.
DR BioGRID; 213244; 4.
DR DIP; DIP-61988N; -.
DR IntAct; Q9D8X5; 4.
DR STRING; 10090.ENSMUSP00000104471; -.
DR iPTMnet; Q9D8X5; -.
DR PhosphoSitePlus; Q9D8X5; -.
DR EPD; Q9D8X5; -.
DR MaxQB; Q9D8X5; -.
DR PaxDb; Q9D8X5; -.
DR PeptideAtlas; Q9D8X5; -.
DR PRIDE; Q9D8X5; -.
DR ProteomicsDB; 283654; -.
DR Antibodypedia; 28328; 281 antibodies from 28 providers.
DR DNASU; 69125; -.
DR Ensembl; ENSMUST00000020822; ENSMUSP00000020822; ENSMUSG00000020515.
DR Ensembl; ENSMUST00000108843; ENSMUSP00000104471; ENSMUSG00000020515.
DR GeneID; 69125; -.
DR KEGG; mmu:69125; -.
DR UCSC; uc007jaj.1; mouse.
DR CTD; 9337; -.
DR MGI; MGI:1916375; Cnot8.
DR VEuPathDB; HostDB:ENSMUSG00000020515; -.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q9D8X5; -.
DR OMA; HIREVWS; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q9D8X5; -.
DR TreeFam; TF314185; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR BioGRID-ORCS; 69125; 13 hits in 76 CRISPR screens.
DR ChiTaRS; Cnot8; mouse.
DR PRO; PR:Q9D8X5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D8X5; protein.
DR Bgee; ENSMUSG00000020515; Expressed in secondary oocyte and 269 other tissues.
DR ExpressionAtlas; Q9D8X5; baseline and differential.
DR Genevisible; Q9D8X5; MM.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR InterPro; IPR027212; Cnot8.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10797; PTHR10797; 1.
DR PANTHER; PTHR10797:SF1; PTHR10797:SF1; 1.
DR Pfam; PF04857; CAF1; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW Reference proteome; Repressor; RNA-binding; RNA-mediated gene silencing;
KW Transcription; Transcription regulation; Translation regulation.
FT CHAIN 1..292
FT /note="CCR4-NOT transcription complex subunit 8"
FT /id="PRO_0000212847"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33574 MW; 9CB57A966E51A91B CRC64;
MPAALVENSQ VICEVWASNL EEEMRKIREI VLSYSYIAMD TEFPGVVVRP IGEFRSSIDY
QYQLLRCNVD LLKIIQLGLT FTNEKGEYPS GINTWQFNFK FNLTEDMYSQ DSIDLLANSG
LQFQKHEEEG IDTLHFAELL MTSGVVLCDN VKWLSFHSGY DFGYMVKLLT DSRLPEEEHE
FFHILNLFFP SIYDVKYLMK SCKNLKGGLQ EVADQLDLQR IGRQHQAGSD SLLTGMAFFR
MKELFFEDSI DDAKYCGRLY GLGTGVAQKQ NEDVDCAQEK MSILAMINNM QQ
