ID CNO6L_HUMAN Reviewed; 555 AA. AC Q96LI5; Q9UF92; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 27-MAR-2024, entry version 173. DE RecName: Full=CCR4-NOT transcription complex subunit 6-like; DE EC=3.1.13.4 {ECO:0000269|PubMed:17452450, ECO:0000269|PubMed:18377426, ECO:0000269|PubMed:27013054}; DE AltName: Full=Carbon catabolite repressor protein 4 homolog B; GN Name=CNOT6L; Synonyms=CCR4B {ECO:0000303|PubMed:17452450}; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-555 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, RP INTERACTION WITH CNOT1; CNOT3; CNOT7; CNOT8 AND CNOT9, TISSUE SPECIFICITY, RP AND MUTAGENESIS OF ASP-410; ASP-489 AND HIS-529. RX PubMed=17452450; DOI=10.1128/mcb.02304-06; RA Morita M., Suzuki T., Nakamura T., Yokoyama K., Miyasaka T., Yamamoto T.; RT "Depletion of mammalian CCR4b deadenylase triggers elevation of the p27Kip1 RT mRNA level and impairs cell growth."; RL Mol. Cell. Biol. 27:4980-4990(2007). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TOB1, AND SUBUNIT. RX PubMed=18377426; DOI=10.1111/j.1349-7006.2008.00746.x; RA Miyasaka T., Morita M., Ito K., Suzuki T., Fukuda H., Takeda S., Inoue J., RA Semba K., Yamamoto T.; RT "Interaction of antiproliferative protein Tob with the CCR4-NOT deadenylase RT complex."; RL Cancer Sci. 99:755-761(2008). RN [6] 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 [7] 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 [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21233283; DOI=10.1091/mbc.e10-11-0898; RA Mittal S., Aslam A., Doidge R., Medica R., Winkler G.S.; RT "The Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the human RT Ccr4-Not complex contribute to the prevention of cell death and RT senescence."; RL Mol. Biol. Cell 22:748-758(2011). RN [9] {ECO:0007744|PDB:3NGN, ECO:0007744|PDB:3NGO, ECO:0007744|PDB:3NGQ} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 158-555 ALONE AND IN COMPLEX WITH RP MAGNESIUM IONS; AMP ANALOG AND POLY-A DNA, MUTAGENESIS OF GLU-240; PRO-365; RP PHE-484; ASP-489 AND HIS-529, COFACTOR, ACTIVE SITE, AND MAGNESIUM-BINDING RP SITES. RX PubMed=20628353; DOI=10.1038/emboj.2010.152; RA Wang H., Morita M., Yang X., Suzuki T., Yang W., Wang J., Ito K., Wang Q., RA Zhao C., Bartlam M., Yamamoto T., Rao Z.; RT "Crystal structure of the human CNOT6L nuclease domain reveals strict RT poly(A) substrate specificity."; RL EMBO J. 29:2566-2576(2010). RN [10] {ECO:0007744|PDB:5DV2, ECO:0007744|PDB:5DV4} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 158-555 IN COMPLEXES WITH CMP AND RP NEOMYCIN, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, MUTAGENESIS OF RP GLU-240, AND ACTIVE SITE. RX PubMed=27013054; DOI=10.1002/1873-3468.12160; RA Zhang Q., Yan D., Guo E., Ding B., Yang W., Liu R., Yamamoto T., RA Bartlam M.; RT "Structural basis for inhibition of the deadenylase activity of human RT CNOT6L."; RL FEBS Lett. 590:1270-1279(2016). RN [11] RP INTERACTION WITH ZFP36L2. RX PubMed=34611029; DOI=10.1136/jmedgenet-2021-107933; RA Zheng W., Sha Q.Q., Hu H., Meng F., Zhou Q., Chen X., Zhang S., Gu Y., RA Yan X., Zhao L., Zong Y., Hu L., Gong F., Lu G., Fan H.Y., Lin G.; RT "Biallelic variants in ZFP36L2 cause female infertility characterised by RT recurrent preimplantation embryo arrest."; RL J. Med. Genet. 59:850-857(2022). CC -!- FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic CC poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex CC which is one of the major cellular mRNA deadenylases and is linked to CC various cellular processes including bulk mRNA degradation, miRNA- CC mediated repression, translational repression during translational CC initiation and general transcription regulation. Additional complex CC functions may be a consequence of its influence on mRNA expression. May CC be involved in the deadenylation-dependent degradation of mRNAs through CC the 3'-UTR AU-rich element-mediated mechanism. Involved in CC deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA CC deadenylase activity can be inhibited by TOB1. Mediates cell CC proliferation and cell survival and prevents cellular senescence. CC {ECO:0000269|PubMed:17452450, ECO:0000269|PubMed:18377426, CC ECO:0000269|PubMed:21233283}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; CC Evidence={ECO:0000269|PubMed:17452450, ECO:0000269|PubMed:18377426, CC ECO:0000269|PubMed:27013054}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:20628353, ECO:0000269|PubMed:27013054}; CC Note=Binds 2 magnesium ions, but the ions interact each with only 1 or CC 2 residues. {ECO:0000269|PubMed:20628353, ECO:0000269|PubMed:27013054}; CC -!- ACTIVITY REGULATION: Inhibited by free AMP, and with lesser efficiency CC also by CMP, GMP, UMP, ATP and neomycin. {ECO:0000269|PubMed:27013054}. 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:17452450, PubMed:18377426, CC PubMed:19558367). Interacts with CNOT1, CNOT3, CNOT7, CNOT8 and CNOT9 CC (PubMed:17452450). Interacts with TOB1 (PubMed:18377426). Interacts CC with NANOS2 (By similarity). Interacts with ZFP36 (By similarity). CC Interacts with ZFP36L2 (PubMed:34611029). Interacts with RBM46 (By CC similarity). {ECO:0000250|UniProtKB:Q8VEG6, CC ECO:0000269|PubMed:17452450, ECO:0000269|PubMed:18377426, CC ECO:0000269|PubMed:19558367, ECO:0000269|PubMed:34611029}. CC -!- INTERACTION: CC Q96LI5; A5YKK6: CNOT1; NbExp=4; IntAct=EBI-1046635, EBI-1222758; CC Q96LI5; Q9NZN8: CNOT2; NbExp=2; IntAct=EBI-1046635, EBI-743033; CC Q96LI5; O75175: CNOT3; NbExp=2; IntAct=EBI-1046635, EBI-743073; CC Q96LI5; Q9UIV1: CNOT7; NbExp=6; IntAct=EBI-1046635, EBI-2105113; CC Q96LI5; Q9UFF9: CNOT8; NbExp=4; IntAct=EBI-1046635, EBI-742299; CC Q96LI5; Q9HCJ0: TNRC6C; NbExp=6; IntAct=EBI-1046635, EBI-6507625; CC Q96LI5; P50616: TOB1; NbExp=4; IntAct=EBI-1046635, EBI-723281; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17452450, CC ECO:0000269|PubMed:21233283}. Nucleus {ECO:0000269|PubMed:21233283}. CC Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:21233283}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96LI5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96LI5-2; Sequence=VSP_030321, VSP_030322, VSP_030323; CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, skeletal muscle, CC pancreas, testis and leukocytes. Weakly expressed in heart, spleen and CC thymus. {ECO:0000269|PubMed:17452450}. CC -!- MISCELLANEOUS: Depletion of CNOT6L causes cell growth defect. CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}. 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 EMBL; AK058188; BAB71707.1; -; mRNA. DR EMBL; AC104701; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133112; CAB61415.1; -; mRNA. DR PIR; T42705; T42705. DR RefSeq; NP_001273719.1; NM_001286790.1. [Q96LI5-1] DR RefSeq; NP_653172.2; NM_144571.2. [Q96LI5-1] DR PDB; 3NGN; X-ray; 2.40 A; A=158-555. DR PDB; 3NGO; X-ray; 2.20 A; A=158-555. DR PDB; 3NGQ; X-ray; 1.80 A; A=158-555. DR PDB; 5DV2; X-ray; 2.07 A; A=158-555. DR PDB; 5DV4; X-ray; 1.80 A; A=158-555. DR PDB; 7VOI; X-ray; 4.38 A; C=1-555. DR PDBsum; 3NGN; -. DR PDBsum; 3NGO; -. DR PDBsum; 3NGQ; -. DR PDBsum; 5DV2; -. DR PDBsum; 5DV4; -. DR PDBsum; 7VOI; -. DR AlphaFoldDB; Q96LI5; -. DR SMR; Q96LI5; -. DR BioGRID; 128873; 97. DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant. DR ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant. DR CORUM; Q96LI5; -. DR DIP; DIP-46837N; -. DR IntAct; Q96LI5; 37. DR STRING; 9606.ENSP00000424896; -. DR ChEMBL; CHEMBL4105957; -. DR GlyCosmos; Q96LI5; 1 site, 2 glycans. DR GlyGen; Q96LI5; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; Q96LI5; -. DR PhosphoSitePlus; Q96LI5; -. DR BioMuta; CNOT6L; -. DR DMDM; 166216089; -. DR EPD; Q96LI5; -. DR jPOST; Q96LI5; -. DR MassIVE; Q96LI5; -. DR MaxQB; Q96LI5; -. DR PaxDb; 9606-ENSP00000424896; -. DR PeptideAtlas; Q96LI5; -. DR ProteomicsDB; 77208; -. [Q96LI5-1] DR ProteomicsDB; 77209; -. [Q96LI5-2] DR Pumba; Q96LI5; -. DR Antibodypedia; 50898; 64 antibodies from 15 providers. DR DNASU; 246175; -. DR Ensembl; ENST00000504123.7; ENSP00000424896.1; ENSG00000138767.14. [Q96LI5-1] DR GeneID; 246175; -. DR KEGG; hsa:246175; -. DR MANE-Select; ENST00000504123.7; ENSP00000424896.1; NM_144571.3; NP_653172.2. DR UCSC; uc011ccd.4; human. [Q96LI5-1] DR AGR; HGNC:18042; -. DR CTD; 246175; -. DR DisGeNET; 246175; -. DR GeneCards; CNOT6L; -. DR HGNC; HGNC:18042; CNOT6L. DR HPA; ENSG00000138767; Low tissue specificity. DR MIM; 618069; gene. DR neXtProt; NX_Q96LI5; -. DR OpenTargets; ENSG00000138767; -. DR PharmGKB; PA38480; -. DR VEuPathDB; HostDB:ENSG00000138767; -. DR eggNOG; KOG0620; Eukaryota. DR GeneTree; ENSGT00940000157298; -. DR InParanoid; Q96LI5; -. DR OrthoDB; 37764at2759; -. DR PhylomeDB; Q96LI5; -. DR TreeFam; TF323175; -. DR BRENDA; 3.1.13.4; 2681. DR PathwayCommons; Q96LI5; -. 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 Reactome; R-HSA-9820841; M-decay: degradation of maternal mRNAs by maternally stored factors. DR SignaLink; Q96LI5; -. DR SIGNOR; Q96LI5; -. DR BioGRID-ORCS; 246175; 25 hits in 1157 CRISPR screens. DR ChiTaRS; CNOT6L; human. DR EvolutionaryTrace; Q96LI5; -. DR GenomeRNAi; 246175; -. DR Pharos; Q96LI5; Tbio. DR PRO; PR:Q96LI5; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q96LI5; Protein. DR Bgee; ENSG00000138767; Expressed in secondary oocyte and 195 other cell types or tissues. DR ExpressionAtlas; Q96LI5; baseline and differential. DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 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:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; 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; 4. DR Genevisible; Q96LI5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; KW Leucine-rich repeat; Magnesium; Metal-binding; mRNA processing; Nuclease; KW Nucleus; Reference proteome; Repeat; RNA-mediated gene silencing; KW Transcription; Transcription regulation; Translation regulation. FT CHAIN 1..555 FT /note="CCR4-NOT transcription complex subunit 6-like" FT /id="PRO_0000314587" FT REPEAT 57..78 FT /note="LRR 1" FT REPEAT 80..101 FT /note="LRR 2" FT REPEAT 103..125 FT /note="LRR 3" FT REPEAT 126..148 FT /note="LRR 4" FT REGION 1..152 FT /note="Required for interaction with CNOT1, CNOT3 and FT CNOT7" FT /evidence="ECO:0000269|PubMed:17452450" FT REGION 158..555 FT /note="Nuclease domain" FT ACT_SITE 410 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:20628353, FT ECO:0000305|PubMed:27013054" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0007744|PDB:3NGO" FT BINDING 240 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054, ECO:0007744|PDB:3NGN, FT ECO:0007744|PDB:5DV2" FT BINDING 276 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0007744|PDB:3NGN" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054, ECO:0007744|PDB:3NGN, FT ECO:0007744|PDB:5DV2" FT BINDING 365 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353" FT BINDING 410 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0007744|PDB:3NGQ" FT BINDING 412 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054, ECO:0007744|PDB:3NGN, FT ECO:0007744|PDB:5DV2" FT BINDING 479 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054, ECO:0007744|PDB:3NGN, FT ECO:0007744|PDB:5DV2" FT BINDING 484 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054, ECO:0007744|PDB:5DV2" FT VAR_SEQ 127..153 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030321" FT VAR_SEQ 486..502 FT /note="GVIDYIFYSKTHMNVLG -> VSGSLWAGVEIISDTSM (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030322" FT VAR_SEQ 503..555 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_030323" FT MUTAGEN 240 FT /note="E->A: Loss of deadenylase activity." FT /evidence="ECO:0000269|PubMed:20628353, FT ECO:0000269|PubMed:27013054" FT MUTAGEN 365 FT /note="P->A: Decreased deadenylase activity." FT /evidence="ECO:0000269|PubMed:20628353" FT MUTAGEN 410 FT /note="D->A: Loss of deadenylase activity." FT /evidence="ECO:0000269|PubMed:17452450" FT MUTAGEN 484 FT /note="F->A: Loss of deadenylase activity." FT /evidence="ECO:0000269|PubMed:20628353" FT MUTAGEN 489 FT /note="D->A: Loss of deadenylase activity." FT /evidence="ECO:0000269|PubMed:17452450, FT ECO:0000269|PubMed:20628353" FT MUTAGEN 529 FT /note="H->A: Loss of deadenylase activity." FT /evidence="ECO:0000269|PubMed:17452450, FT ECO:0000269|PubMed:20628353" FT CONFLICT 439 FT /note="R -> G (in Ref. 1; BAB71707)" FT /evidence="ECO:0000305" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:3NGQ" FT TURN 204..206 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 217..231 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 234..242 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 243..248 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 250..256 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:3NGN" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 281..288 FT /evidence="ECO:0007829|PDB:3NGQ" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 292..301 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 302..308 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 314..318 FT /evidence="ECO:0007829|PDB:3NGQ" FT TURN 319..322 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 326..334 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:3NGO" FT HELIX 368..386 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 418..425 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 433..435 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 443..447 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 459..461 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:3NGQ" FT TURN 469..473 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 474..476 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 489..494 FT /evidence="ECO:0007829|PDB:3NGQ" FT TURN 495..497 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 498..504 FT /evidence="ECO:0007829|PDB:3NGQ" FT HELIX 509..514 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:3NGN" FT STRAND 527..529 FT /evidence="ECO:0007829|PDB:3NGQ" FT STRAND 532..538 FT /evidence="ECO:0007829|PDB:3NGQ" 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 //