CNOT7_HUMAN
ID CNOT7_HUMAN Reviewed; 285 AA.
AC Q9UIV1; A8MZM5; B3KMP1; B3KN35; D3DSP6; G3V108; Q7Z530;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=CCR4-NOT transcription complex subunit 7;
DE EC=3.1.13.4;
DE AltName: Full=BTG1-binding factor 1;
DE AltName: Full=CCR4-associated factor 1;
DE Short=CAF-1;
DE AltName: Full=Caf1a;
GN Name=CNOT7; Synonyms=CAF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9820826; DOI=10.1042/bj3360471;
RA Bogdan J.A., Adams-Burton C., Pedicord D.L., Sukovich D.A., Benfield P.A.,
RA Corjay M.H., Stoltenborg J.K., Dicker I.B.;
RT "Human carbon catabolite repressor protein (CCR4)-associative factor 1:
RT cloning, expression and characterization of its interaction with the B-cell
RT translocation protein BTG1.";
RL Biochem. J. 336:471-481(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wan Y.Z., Yu L., Zhang H.L., Liu Q., Chen S.Y., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homology to mouse mCAF1 protein
RT mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate, and Testis;
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 [7]
RP CATALYTIC ACTIVITY.
RX PubMed=15769875; DOI=10.1261/rna.7135305;
RA Bianchin C., Mauxion F., Sentis S., Seraphin B., Corbo L.;
RT "Conservation of the deadenylase activity of proteins of the Caf1 family in
RT human.";
RL RNA 11:487-494(2005).
RN [8]
RP IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE CCR4-NOT
RP COMPLEX.
RX PubMed=19558367; DOI=10.1042/bj20090500;
RA Lau N.C., Kolkman A., van Schaik F.M., Mulder K.W., Pijnappel W.W.,
RA Heck A.J., Timmers H.T.;
RT "Human Ccr4-Not complexes contain variable deadenylase subunits.";
RL Biochem. J. 422:443-453(2009).
RN [9]
RP FUNCTION.
RX PubMed=19605561; DOI=10.1091/mbc.e09-02-0146;
RA Aslam A., Mittal S., Koch F., Andrau J.C., Winkler G.S.;
RT "The Ccr4-NOT deadenylase subunits CNOT7 and CNOT8 have overlapping roles
RT and modulate cell proliferation.";
RL Mol. Biol. Cell 20:3840-3850(2009).
RN [10]
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).
RN [11]
RP FUNCTION.
RX PubMed=20065043; DOI=10.1128/mcb.01481-09;
RA Piao X., Zhang X., Wu L., Belasco J.G.;
RT "CCR4-NOT deadenylates mRNA associated with complexes in human cells.";
RL Mol. Cell. Biol. 30:1486-1494(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH TOB1, AND MUTAGENESIS OF ASP-161.
RX PubMed=21336257; DOI=10.1038/emboj.2011.37;
RA Hosoda N., Funakoshi Y., Hirasawa M., Yamagishi R., Asano Y., Miyagawa R.,
RA Ogami K., Tsujimoto M., Hoshino S.;
RT "Anti-proliferative protein Tob negatively regulates CPEB3 target by
RT recruiting Caf1 deadenylase.";
RL EMBO J. 30:1311-1323(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH TOB1 AND BTG2.
RX PubMed=23236473; DOI=10.1371/journal.pone.0051331;
RA Doidge R., Mittal S., Aslam A., Winkler G.S.;
RT "The anti-proliferative activity of BTG/TOB proteins is mediated via the
RT Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not
RT complex.";
RL PLoS ONE 7:E51331-E51331(2012).
RN [15]
RP INTERACTION WITH ZFP36; ZFP36L1 AND ZFP36L2.
RX PubMed=25106868; DOI=10.1093/nar/gku652;
RA Adachi S., Homoto M., Tanaka R., Hioki Y., Murakami H., Suga H.,
RA Matsumoto M., Nakayama K.I., Hatta T., Iemura S., Natsume T.;
RT "ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK-RSK pathway.";
RL Nucleic Acids Res. 42:10037-10049(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INTERACTION WITH TARDBP.
RX PubMed=30520513; DOI=10.1002/1873-3468.13310;
RA Fukushima M., Hosoda N., Chifu K., Hoshino S.I.;
RT "TDP-43 accelerates deadenylation of target mRNAs by recruiting Caf1
RT deadenylase.";
RL FEBS Lett. 593:277-287(2019).
RN [18]
RP INTERACTION WITH BTG4.
RX PubMed=32502391; DOI=10.1016/j.ajhg.2020.05.010;
RA Zheng W., Zhou Z., Sha Q., Niu X., Sun X., Shi J., Zhao L., Zhang S.,
RA Dai J., Cai S., Meng F., Hu L., Gong F., Li X., Fu J., Shi R., Lu G.,
RA Chen B., Fan H., Wang L., Lin G., Sang Q.;
RT "Homozygous mutations in BTG4 cause zygotic cleavage failure and female
RT infertility.";
RL Am. J. Hum. Genet. 107:24-33(2020).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 11-262 IN COMPLEX WITH TOB1,
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-40; GLU-42; ASP-161;
RP HIS-225 AND ASP-230.
RX PubMed=19276069; DOI=10.1074/jbc.m809250200;
RA Horiuchi M., Takeuchi K., Noda N., Muroya N., Suzuki T., Nakamura T.,
RA Kawamura-Tsuzuku J., Takahasi K., Yamamoto T., Inagaki F.;
RT "Structural basis for the antiproliferative activity of the Tob-hCaf1
RT complex.";
RL J. Biol. Chem. 284:13244-13255(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-285 IN COMPLEX WITH CNOT1, AND
RP MUTAGENESIS OF GLU-138; MET-141; THR-142 AND GLU-149.
RX PubMed=22977175; DOI=10.1093/nar/gks883;
RA Petit A.P., Wohlbold L., Bawankar P., Huntzinger E., Schmidt S.,
RA Izaurralde E., Weichenrieder O.;
RT "The structural basis for the interaction between the CAF1 nuclease and the
RT NOT1 scaffold of the human CCR4-NOT deadenylase complex.";
RL Nucleic Acids Res. 40:11058-11072(2012).
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 CNOT8. Catalytic component of the CCR4-NOT complex which
CC is one of the major cellular mRNA deadenylases and is linked to various
CC cellular processes including bulk mRNA degradation, miRNA-mediated
CC repression, translational repression during translational initiation
CC and general transcription regulation. During miRNA-mediated repression
CC the complex seems also to act as translational repressor during
CC translational initiation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. Associates with
CC members of the BTG family such as TOB1 and BTG2 and is required for
CC their anti-proliferative activity. {ECO:0000269|PubMed:19605561,
CC ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:20634287,
CC ECO:0000269|PubMed:23236473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:15769875, ECO:0000269|PubMed:19276069,
CC ECO:0000269|PubMed:20634287};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19276069};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19276069};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:19276069};
CC Note=Binds 2 divalent metal cations per subunit with RNAase activity
CC being higher in presence of Mn(2+) than of Mg(2+) or Co(2+).
CC {ECO:0000269|PubMed:19276069};
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 (PubMed:19558367). In the complex,
CC interacts directly with CNOT1 (PubMed:21336257). Interacts with AGO2
CC (By similarity). Interacts with TOB1; recruited by TOB1 to a ternary
CC complex with CPEB3 which is required for mRNA deadenylation and decay
CC (PubMed:21336257, PubMed:23236473, PubMed:19276069). Interacts with
CC BTG1 (By similarity). Interacts with BTG2 (PubMed:23236473). Interacts
CC with NANOS2 (By similarity). Interacts with ZFP36, ZFP36L1 and ZFP36L2;
CC these interactions are inhibited in response to phorbol 12-myristate
CC 13-acetate (PMA) treatment in a p38 MAPK-dependent manner
CC (PubMed:25106868). Interacts with TARDBP (PubMed:30520513). Interacts
CC with BTG4 (PubMed:32502391). Interacts with EIF4E; this interaction is
CC increased by CNOT7 interaction with BTG4 (By similarity).
CC {ECO:0000250|UniProtKB:Q60809, ECO:0000269|PubMed:19276069,
CC ECO:0000269|PubMed:19558367, ECO:0000269|PubMed:21336257,
CC ECO:0000269|PubMed:22977175, ECO:0000269|PubMed:23236473,
CC ECO:0000269|PubMed:25106868, ECO:0000269|PubMed:30520513,
CC ECO:0000269|PubMed:32502391}.
CC -!- INTERACTION:
CC Q9UIV1; Q9UKV8: AGO2; NbExp=2; IntAct=EBI-2105113, EBI-528269;
CC Q9UIV1; P62324: BTG1; NbExp=4; IntAct=EBI-2105113, EBI-742279;
CC Q9UIV1; P78543: BTG2; NbExp=8; IntAct=EBI-2105113, EBI-1047576;
CC Q9UIV1; A5YKK6: CNOT1; NbExp=7; IntAct=EBI-2105113, EBI-1222758;
CC Q9UIV1; Q9ULM6: CNOT6; NbExp=2; IntAct=EBI-2105113, EBI-2104530;
CC Q9UIV1; Q96LI5: CNOT6L; NbExp=6; IntAct=EBI-2105113, EBI-1046635;
CC Q9UIV1; P42858: HTT; NbExp=13; IntAct=EBI-2105113, EBI-466029;
CC Q9UIV1; Q86TB9: PATL1; NbExp=5; IntAct=EBI-2105113, EBI-2562092;
CC Q9UIV1; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-2105113, EBI-2555179;
CC Q9UIV1; Q9HCJ0: TNRC6C; NbExp=9; IntAct=EBI-2105113, EBI-6507625;
CC Q9UIV1; P50616: TOB1; NbExp=9; IntAct=EBI-2105113, EBI-723281;
CC Q9UIV1; Q14106: TOB2; NbExp=7; IntAct=EBI-2105113, EBI-2562000;
CC Q9UIV1; P22893: Zfp36; Xeno; NbExp=3; IntAct=EBI-2105113, EBI-647803;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, P-body {ECO:0000250}.
CC Note=NANOS2 promotes its localization to P-body. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UIV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIV1-2; Sequence=VSP_045497;
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01500.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L46722; AAF01500.1; ALT_FRAME; mRNA.
DR EMBL; AF086915; AAP97145.1; -; mRNA.
DR EMBL; AK021808; BAG51053.1; -; mRNA.
DR EMBL; AK023466; BAG51197.1; -; mRNA.
DR EMBL; AC091050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63820.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63821.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63822.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63823.1; -; Genomic_DNA.
DR EMBL; BC060852; AAH60852.1; -; mRNA.
DR EMBL; BC070187; AAH70187.1; -; mRNA.
DR CCDS; CCDS55202.1; -. [Q9UIV1-2]
DR CCDS; CCDS6000.2; -. [Q9UIV1-1]
DR RefSeq; NP_001309016.1; NM_001322087.1. [Q9UIV1-2]
DR RefSeq; NP_001309017.1; NM_001322088.1. [Q9UIV1-2]
DR RefSeq; NP_001309018.1; NM_001322089.1. [Q9UIV1-2]
DR RefSeq; NP_001309019.1; NM_001322090.1. [Q9UIV1-1]
DR RefSeq; NP_001309020.1; NM_001322091.1. [Q9UIV1-1]
DR RefSeq; NP_001309021.1; NM_001322092.1. [Q9UIV1-1]
DR RefSeq; NP_001309022.1; NM_001322093.1.
DR RefSeq; NP_001309023.1; NM_001322094.1.
DR RefSeq; NP_001309024.1; NM_001322095.1.
DR RefSeq; NP_001309025.1; NM_001322096.1.
DR RefSeq; NP_001309026.1; NM_001322097.1.
DR RefSeq; NP_001309027.1; NM_001322098.1.
DR RefSeq; NP_001309028.1; NM_001322099.1.
DR RefSeq; NP_001309029.1; NM_001322100.1.
DR RefSeq; NP_037486.2; NM_013354.6. [Q9UIV1-1]
DR RefSeq; NP_473367.2; NM_054026.3. [Q9UIV1-2]
DR RefSeq; XP_005273538.1; XM_005273481.2. [Q9UIV1-1]
DR PDB; 2D5R; X-ray; 2.50 A; A=11-262.
DR PDB; 4GMJ; X-ray; 2.70 A; B/D/F=1-285.
DR PDB; 7AX1; X-ray; 3.30 A; B=2-285.
DR PDBsum; 2D5R; -.
DR PDBsum; 4GMJ; -.
DR PDBsum; 7AX1; -.
DR AlphaFoldDB; Q9UIV1; -.
DR SMR; Q9UIV1; -.
DR BioGRID; 118938; 138.
DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant.
DR ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant.
DR CORUM; Q9UIV1; -.
DR DIP; DIP-41902N; -.
DR IntAct; Q9UIV1; 63.
DR MINT; Q9UIV1; -.
DR STRING; 9606.ENSP00000355279; -.
DR BindingDB; Q9UIV1; -.
DR ChEMBL; CHEMBL3616361; -.
DR iPTMnet; Q9UIV1; -.
DR PhosphoSitePlus; Q9UIV1; -.
DR BioMuta; CNOT7; -.
DR DMDM; 41713629; -.
DR EPD; Q9UIV1; -.
DR jPOST; Q9UIV1; -.
DR MassIVE; Q9UIV1; -.
DR MaxQB; Q9UIV1; -.
DR PaxDb; Q9UIV1; -.
DR PeptideAtlas; Q9UIV1; -.
DR PRIDE; Q9UIV1; -.
DR ProteomicsDB; 32220; -.
DR ProteomicsDB; 84569; -. [Q9UIV1-1]
DR Antibodypedia; 22252; 203 antibodies from 28 providers.
DR DNASU; 29883; -.
DR Ensembl; ENST00000361272.9; ENSP00000355279.4; ENSG00000198791.12. [Q9UIV1-1]
DR Ensembl; ENST00000523917.5; ENSP00000429093.1; ENSG00000198791.12. [Q9UIV1-2]
DR GeneID; 29883; -.
DR KEGG; hsa:29883; -.
DR MANE-Select; ENST00000361272.9; ENSP00000355279.4; NM_013354.7; NP_037486.2.
DR UCSC; uc003wxg.2; human. [Q9UIV1-1]
DR CTD; 29883; -.
DR DisGeNET; 29883; -.
DR GeneCards; CNOT7; -.
DR HGNC; HGNC:14101; CNOT7.
DR HPA; ENSG00000198791; Low tissue specificity.
DR MIM; 604913; gene.
DR neXtProt; NX_Q9UIV1; -.
DR OpenTargets; ENSG00000198791; -.
DR PharmGKB; PA26678; -.
DR VEuPathDB; HostDB:ENSG00000198791; -.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_027974_0_1_1; -.
DR InParanoid; Q9UIV1; -.
DR OMA; DTKWISF; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q9UIV1; -.
DR TreeFam; TF314185; -.
DR BRENDA; 3.1.13.4; 2681.
DR PathwayCommons; Q9UIV1; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR SignaLink; Q9UIV1; -.
DR SIGNOR; Q9UIV1; -.
DR BioGRID-ORCS; 29883; 204 hits in 1085 CRISPR screens.
DR ChiTaRS; CNOT7; human.
DR EvolutionaryTrace; Q9UIV1; -.
DR GeneWiki; CNOT7; -.
DR GenomeRNAi; 29883; -.
DR Pharos; Q9UIV1; Tchem.
DR PRO; PR:Q9UIV1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UIV1; protein.
DR Bgee; ENSG00000198791; Expressed in oocyte and 207 other tissues.
DR ExpressionAtlas; Q9UIV1; baseline and differential.
DR Genevisible; Q9UIV1; HS.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0004532; F:exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; TAS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IC:ComplexPortal.
DR GO; GO:0033962; P:P-body assembly; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR IDEAL; IID00504; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Repressor;
KW RNA-binding; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..285
FT /note="CCR4-NOT transcription complex subunit 7"
FT /id="PRO_0000212844"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
FT BINDING 278
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT VAR_SEQ 244..285
FT /note="MFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS -> V (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045497"
FT MUTAGEN 40
FT /note="D->N: Abolishes RNA deadenylase activity."
FT /evidence="ECO:0000269|PubMed:19276069"
FT MUTAGEN 42
FT /note="E->Q: Abolishes RNA deadenylase activity."
FT /evidence="ECO:0000269|PubMed:19276069"
FT MUTAGEN 138
FT /note="E->K: Abolishes interaction with CNOT1; when
FT associated with Y-142 and K-149."
FT /evidence="ECO:0000269|PubMed:22977175"
FT MUTAGEN 141
FT /note="M->R: Abolishes interaction with CNOT1."
FT /evidence="ECO:0000269|PubMed:22977175"
FT MUTAGEN 142
FT /note="T->Y: Abolishes interaction with CNOT1; when
FT associated with K-138 and K-149."
FT /evidence="ECO:0000269|PubMed:22977175"
FT MUTAGEN 149
FT /note="E->K: Abolishes interaction with CNOT1; when
FT associated with K-138 and Y-142."
FT /evidence="ECO:0000269|PubMed:22977175"
FT MUTAGEN 161
FT /note="D->N: Abolishes RNA deadenylase activity.
FT Drastically reduces the rate of deadenylation and decay of
FT CBEP3-tethered mRNA."
FT /evidence="ECO:0000269|PubMed:19276069,
FT ECO:0000269|PubMed:21336257"
FT MUTAGEN 203
FT /note="K->A: Abolishes interaction with TOB1."
FT MUTAGEN 225
FT /note="H->A: Abolishes RNA deadenylase activity."
FT /evidence="ECO:0000269|PubMed:19276069"
FT MUTAGEN 230
FT /note="D->N: Abolishes RNA deadenylase activity."
FT /evidence="ECO:0000269|PubMed:19276069"
FT CONFLICT 4..5
FT /note="AT -> EL (in Ref. 3; AAP97145)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="M -> V (in Ref. 4; BAG51197)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:7AX1"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2D5R"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:2D5R"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2D5R"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:7AX1"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:2D5R"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:2D5R"
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
