CNO6L_HUMAN
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 03-AUG-2022, entry version 165.
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).
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 {ECO:0000250|UniProtKB:Q8VEG6, ECO:0000269|PubMed:17452450,
CC ECO:0000269|PubMed:18377426, ECO:0000269|PubMed:19558367}.
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 CCDS; CCDS68731.1; -. [Q96LI5-1]
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 PDBsum; 3NGN; -.
DR PDBsum; 3NGO; -.
DR PDBsum; 3NGQ; -.
DR PDBsum; 5DV2; -.
DR PDBsum; 5DV4; -.
DR AlphaFoldDB; Q96LI5; -.
DR SMR; Q96LI5; -.
DR BioGRID; 128873; 93.
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 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; Q96LI5; -.
DR PeptideAtlas; Q96LI5; -.
DR PRIDE; Q96LI5; -.
DR ProteomicsDB; 77208; -. [Q96LI5-1]
DR ProteomicsDB; 77209; -. [Q96LI5-2]
DR Antibodypedia; 50898; 62 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 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; 724242at2759; -.
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 SignaLink; Q96LI5; -.
DR SIGNOR; Q96LI5; -.
DR BioGRID-ORCS; 246175; 24 hits in 1077 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 193 other tissues.
DR ExpressionAtlas; Q96LI5; baseline and differential.
DR Genevisible; Q96LI5; HS.
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:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
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:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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 CDD; cd10312; Deadenylase_CCR4b; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 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 Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 4.
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
