ID TNKS1_HUMAN Reviewed; 1327 AA. AC O95271; O95272; Q4G0F2; Q59FX0; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 27-MAR-2024, entry version 220. DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase-1 {ECO:0000305}; DE EC=2.4.2.30 {ECO:0000269|PubMed:19759537}; DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 5 {ECO:0000303|PubMed:20106667}; DE Short=ARTD5 {ECO:0000303|PubMed:20106667}; DE AltName: Full=Poly [ADP-ribose] polymerase 5A {ECO:0000303|PubMed:20106667}; DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase-1 {ECO:0000305}; DE EC=2.4.2.- {ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:25043379}; DE AltName: Full=TNKS-1; DE AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase; DE AltName: Full=Tankyrase I; DE AltName: Full=Tankyrase-1 {ECO:0000303|PubMed:9822378}; DE Short=TANK1 {ECO:0000303|PubMed:9822378}; GN Name=TNKS {ECO:0000312|HGNC:HGNC:11941}; GN Synonyms=PARP5A {ECO:0000303|PubMed:9822378}, PARPL, TIN1, TINF1, GN TNKS1; 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] (ISOFORMS 1 AND 2). RC TISSUE=Testis; RX PubMed=9822378; DOI=10.1126/science.282.5393.1484; RA Smith S., Giriat I., Schmitt A., de Lange T.; RT "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres."; RL Science 282:1484-1487(1998). RN [2] 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 [3] {ECO:0000312|EMBL:BAD92576.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-1327. RC TISSUE=Brain {ECO:0000312|EMBL:BAD92576.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 [5] RP SUBCELLULAR LOCATION. RX PubMed=10523501; DOI=10.1242/jcs.112.21.3649; RA Smith S., de Lange T.; RT "Cell cycle dependent localization of the telomeric PARP, tankyrase, to RT nuclear pore complexes and centrosomes."; RL J. Cell Sci. 112:3649-3656(1999). RN [6] RP FUNCTION, AND PHOSPHORYLATION. RX PubMed=10988299; DOI=10.1074/jbc.m007635200; RA Chi N.-W., Lodish H.F.; RT "Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate RT that interacts with IRAP in GLUT4 vesicles."; RL J. Biol. Chem. 275:38437-38444(2000). RN [7] RP INTERACTION WITH NUMA1. RX PubMed=12080061; DOI=10.1074/jbc.m203916200; RA Sbodio J.I., Chi N.W.; RT "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and RT human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a RT novel tankyrase partner."; RL J. Biol. Chem. 277:31887-31892(2002). RN [8] RP FUNCTION, AND MUTAGENESIS OF HIS-1184 AND GLU-1291. RX PubMed=11739745; DOI=10.1128/mcb.22.1.332-342.2002; RA Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.; RT "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at RT human telomeres."; RL Mol. Cell. Biol. 22:332-342(2002). RN [9] RP IDENTIFICATION IN A COMPLEX WITH POT1; TERF1 AND TINF2. RX PubMed=12768206; DOI=10.1038/nature01688; RA Loayza D., De Lange T.; RT "POT1 as a terminal transducer of TRF1 telomere length control."; RL Nature 423:1013-1018(2003). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16076287; DOI=10.1042/bj20050885; RA Chang W., Dynek J.N., Smith S.; RT "NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in RT mitosis."; RL Biochem. J. 391:177-184(2005). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH RP AXIN1 AND AXIN2. RX PubMed=19759537; DOI=10.1038/nature08356; RA Huang S.M., Mishina Y.M., Liu S., Cheung A., Stegmeier F., Michaud G.A., RA Charlat O., Wiellette E., Zhang Y., Wiessner S., Hild M., Shi X., RA Wilson C.J., Mickanin C., Myer V., Fazal A., Tomlinson R., Serluca F., RA Shao W., Cheng H., Shultz M., Rau C., Schirle M., Schlegl J., Ghidelli S., RA Fawell S., Lu C., Curtis D., Kirschner M.W., Lengauer C., Finan P.M., RA Tallarico J.A., Bouwmeester T., Porter J.A., Bauer A., Cong F.; RT "Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling."; RL Nature 461:614-620(2009). RN [12] RP NOMENCLATURE. RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003; RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.; RT "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."; RL Trends Biochem. Sci. 35:208-219(2010). RN [13] RP FUNCTION, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, AND RP UBIQUITINATION. RX PubMed=21478859; DOI=10.1038/ncb2222; RA Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., RA Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., RA Huang S.M., Cong F.; RT "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin RT degradation and Wnt signalling."; RL Nat. Cell Biol. 13:623-629(2011). RN [14] RP INTERACTION WITH AXIN1, AND SUBCELLULAR LOCATION. RX PubMed=21799911; DOI=10.1371/journal.pone.0022595; RA Callow M.G., Tran H., Phu L., Lau T., Lee J., Sandoval W.N., Liu P.S., RA Bheddah S., Tao J., Lill J.R., Hongo J.A., Davis D., Kirkpatrick D.S., RA Polakis P., Costa M.; RT "Ubiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt RT signaling."; RL PLoS ONE 6:E22595-E22595(2011). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22864114; DOI=10.1016/j.molcel.2012.06.033; RA Ozaki Y., Matsui H., Asou H., Nagamachi A., Aki D., Honda H., Yasunaga S., RA Takihara Y., Yamamoto T., Izumi S., Ohsugi M., Inaba T.; RT "Poly-ADP ribosylation of Miki by tankyrase-1 promotes centrosome RT maturation."; RL Mol. Cell 47:694-706(2012). RN [16] RP FUNCTION. RX PubMed=23622245; DOI=10.1016/j.cell.2013.03.040; RA Cho-Park P.F., Steller H.; RT "Proteasome regulation by ADP-ribosylation."; RL Cell 153:614-627(2013). RN [17] RP FUNCTION. RX PubMed=25043379; DOI=10.1038/ncomms5426; RA Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I., RA Chang P.; RT "Family-wide analysis of poly(ADP-ribose) polymerase activity."; RL Nat. Commun. 5:4426-4426(2014). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1325, AND ZINC-BINDING SITES. RX PubMed=18436240; DOI=10.1016/j.jmb.2008.03.058; RA Lehtio L., Collins R., van den Berg S., Johansson A., Dahlgren L.G., RA Hammarstrom M., Helleday T., Holmberg-Schiavone L., Karlberg T., RA Weigelt J.; RT "Zinc binding catalytic domain of human tankyrase 1."; RL J. Mol. Biol. 379:136-145(2008). RN [19] {ECO:0007744|PDB:5GP7} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 799-957, FUNCTION, AND RP DEUBIQUITINATION BY USP25. RX PubMed=28619731; DOI=10.1101/gad.300889.117; RA Xu D., Liu J., Fu T., Shan B., Qian L., Pan L., Yuan J.; RT "USP25 regulates Wnt signaling by controlling the stability of RT tankyrases."; RL Genes Dev. 31:1024-1035(2017). RN [20] {ECO:0007744|PDB:7KKM, ECO:0007744|PDB:7KKN} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1104-1314 IN COMPLEX WITH RP TALAZOPARIB INHIBITOR; OLAPARIB; NIRAPARIB AND VELIPARIB. RX PubMed=33361107; DOI=10.1074/jbc.ra120.016573; RA Ryan K., Bolanos B., Smith M., Palde P.B., Cuenca P.D., VanArsdale T.L., RA Niessen S., Zhang L., Behenna D., Ornelas M.A., Tran K.T., Kaiser S., RA Lum L., Stewart A., Gajiwala K.S.; RT "Dissecting the molecular determinants of clinical PARP1 inhibitor RT selectivity for tankyrase1."; RL J. Biol. Chem. 296:100251-100251(2021). CC -!- FUNCTION: Poly-ADP-ribosyltransferase involved in various processes CC such as Wnt signaling pathway, telomere length and vesicle trafficking CC (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, CC PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379, CC PubMed:28619731). Acts as an activator of the Wnt signaling pathway by CC mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key CC components of the beta-catenin destruction complex: poly-ADP- CC ribosylated target proteins are recognized by RNF146, which mediates CC their ubiquitination and subsequent degradation (PubMed:19759537, CC PubMed:21478859). Also mediates PARsylation of BLZF1 and CASC3, CC followed by recruitment of RNF146 and subsequent ubiquitination CC (PubMed:21478859). Mediates PARsylation of TERF1, thereby contributing CC to the regulation of telomere length (PubMed:11739745). Involved in CC centrosome maturation during prometaphase by mediating PARsylation of CC HEPACAM2/MIKI (PubMed:22864114). May also regulate vesicle trafficking CC and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles CC (PubMed:10988299). May be involved in spindle pole assembly through CC PARsylation of NUMA1 (PubMed:16076287). Stimulates 26S proteasome CC activity (PubMed:23622245). {ECO:0000269|PubMed:10988299, CC ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:16076287, CC ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, CC ECO:0000269|PubMed:22864114, ECO:0000269|PubMed:23622245, CC ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:28619731}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D- CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; CC Evidence={ECO:0000269|PubMed:19759537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L- CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA- CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; CC Evidence={ECO:0000305}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L- CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA- CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; CC Evidence={ECO:0000305}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; CC Evidence={ECO:0000305}; CC -!- ACTIVITY REGULATION: Specifically inhibited by XAV939, a small CC molecule, leading to inhibit the Wnt signaling pathway by stabilizing CC AXIN1 and AXIN2 (PubMed:19759537). Inhibited by talazoparib CC (PubMed:33361107). Not inhibited by olaparib, niraparib and veliparib CC (PubMed:33361107). {ECO:0000269|PubMed:19759537, CC ECO:0000269|PubMed:33361107}. CC -!- SUBUNIT: Oligomerizes and associates with TNKS2. Interacts with the CC cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to CC the N-terminus of telomeric TERF1 via the ANK repeats. Found in a CC complex with POT1; TERF1 and TINF2 (PubMed:12768206). Interacts with CC AXIN1 (PubMed:19759537, PubMed:21478859, PubMed:21799911). Interacts CC with AXIN2 (PubMed:19759537, PubMed:21478859). Interacts with BLZF1 and CC CASC3 (PubMed:21478859). Interacts with NUMA1 (PubMed:12080061). CC {ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12768206, CC ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, CC ECO:0000269|PubMed:21799911}. CC -!- INTERACTION: CC O95271; Q9NX46: ADPRS; NbExp=3; IntAct=EBI-1105254, EBI-718580; CC O95271; Q9HC77: CENPJ; NbExp=4; IntAct=EBI-1105254, EBI-946194; CC O95271; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-1105254, EBI-6255981; CC O95271; Q96RU3: FNBP1; NbExp=4; IntAct=EBI-1105254, EBI-1111248; CC O95271; Q9NWT6: HIF1AN; NbExp=5; IntAct=EBI-1105254, EBI-745632; CC O95271; O75367-2: MACROH2A1; NbExp=6; IntAct=EBI-1105254, EBI-6249599; CC O95271; Q9Y530: OARD1; NbExp=3; IntAct=EBI-1105254, EBI-8502288; CC O95271; Q9NTX7: RNF146; NbExp=6; IntAct=EBI-1105254, EBI-722397; CC O95271; O00560: SDCBP; NbExp=5; IntAct=EBI-1105254, EBI-727004; CC O95271; P56279: TCL1A; NbExp=3; IntAct=EBI-1105254, EBI-749995; CC O95271; P54274: TERF1; NbExp=6; IntAct=EBI-1105254, EBI-710997; CC O95271; Q9C0C2: TNKS1BP1; NbExp=2; IntAct=EBI-1105254, EBI-2104458; CC O95271; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-1105254, EBI-1380492; CC O95271; O35625: Axin1; Xeno; NbExp=4; IntAct=EBI-1105254, EBI-2365912; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10523501, CC ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:22864114}. Golgi CC apparatus membrane {ECO:0000269|PubMed:22864114}; Peripheral membrane CC protein {ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome {ECO:0000269|PubMed:10523501, CC ECO:0000269|PubMed:21799911}. Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:10523501}. Chromosome, telomere CC {ECO:0000305|PubMed:9822378}. Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000269|PubMed:16076287}. Note=Associated with the Golgi and with CC juxtanuclear SLC2A4/GLUT4-vesicles (PubMed:22864114). A minor CC proportion is also found at nuclear pore complexes and around the CC pericentriolar matrix of mitotic centromeres (PubMed:10523501). During CC interphase, a small fraction of TNKS is found in the nucleus, CC associated with TERF1 (PubMed:12768206). Localizes to spindle poles at CC mitosis onset via interaction with NUMA1 (PubMed:12080061). CC {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:12080061, CC ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:22864114}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95271-1; Sequence=Displayed; CC Name=2; CC IsoId=O95271-2; Sequence=VSP_004538, VSP_004539; CC -!- TISSUE SPECIFICITY: Ubiquitous; highest levels in testis. CC -!- PTM: Phosphorylated on serine residues by MAPK kinases upon insulin CC stimulation. Phosphorylated during mitosis. CC {ECO:0000269|PubMed:10988299}. CC -!- PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to CC its degradation. Deubiquitinated by USP25; leading to stabilization CC (PubMed:28619731). {ECO:0000269|PubMed:21478859, CC ECO:0000269|PubMed:28619731}. CC -!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is CC recognized by RNF146, followed by ubiquitination. CC {ECO:0000269|PubMed:21478859}. CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43534/TNKS"; 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; AF082556; AAC79841.1; -; mRNA. DR EMBL; AF082557; AAC79842.1; -; mRNA. DR EMBL; AF082558; AAC79843.1; -; mRNA. DR EMBL; AF082559; AAC79844.1; -; mRNA. DR EMBL; AC103834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC103877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104052; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC021242; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC098394; AAH98394.1; -; mRNA. DR EMBL; AB209339; BAD92576.1; -; mRNA. DR CCDS; CCDS5974.1; -. [O95271-1] DR RefSeq; NP_003738.2; NM_003747.2. [O95271-1] DR PDB; 2RF5; X-ray; 2.30 A; A=1091-1325. DR PDB; 3UDD; X-ray; 1.95 A; A/B=1105-1327. DR PDB; 3UH2; X-ray; 2.00 A; A/B=1105-1327. DR PDB; 3UH4; X-ray; 2.00 A; A/B=1105-1327. DR PDB; 4DVI; X-ray; 1.90 A; A/B=1104-1314. DR PDB; 4I9I; X-ray; 2.40 A; A/B/C/D=1104-1314. DR PDB; 4K4E; X-ray; 2.30 A; A/B=1104-1314. DR PDB; 4K4F; X-ray; 2.90 A; A/B=1104-1314. DR PDB; 4KRS; X-ray; 2.29 A; A/B=1105-1327. DR PDB; 4LI6; X-ray; 2.05 A; A/B=1105-1327. DR PDB; 4LI7; X-ray; 2.20 A; A/B=1105-1327. DR PDB; 4LI8; X-ray; 2.52 A; A/B=1105-1327. DR PDB; 4MSG; X-ray; 1.80 A; A/B=1104-1314. DR PDB; 4MSK; X-ray; 2.30 A; A/B/C/D=1104-1314. DR PDB; 4MT9; X-ray; 2.00 A; A/B=1104-1314. DR PDB; 4N3R; X-ray; 1.90 A; A/B=1104-1314. DR PDB; 4N4V; X-ray; 2.00 A; A/B=1104-1314. DR PDB; 4OA7; X-ray; 2.30 A; A/B/C/D=1105-1313. DR PDB; 4TOR; X-ray; 1.50 A; A/B/C/D=1105-1315. DR PDB; 4TOS; X-ray; 1.80 A; A/B=1105-1315. DR PDB; 4U6A; X-ray; 2.37 A; A=1091-1325. DR PDB; 4UUH; X-ray; 2.52 A; A=1091-1325. DR PDB; 4UW1; X-ray; 3.37 A; A/B/C/D/E/F/G/H=1091-1325. DR PDB; 4W5S; X-ray; 2.80 A; A=1105-1314. DR PDB; 4W6E; X-ray; 1.95 A; A=1106-1314. DR PDB; 5EBT; X-ray; 2.24 A; A/B/C/D=1106-1314. DR PDB; 5ECE; X-ray; 2.20 A; A/B/C/D=1105-1316. DR PDB; 5ETY; X-ray; 2.90 A; A/B/C/D=1091-1324. DR PDB; 5GP7; X-ray; 1.50 A; A=799-957. DR PDB; 5JHQ; X-ray; 3.20 A; A/B/C/D=174-649. DR PDB; 5JTI; X-ray; 2.90 A; A/B/C/D/E/F=1018-1093. DR PDB; 5JU5; X-ray; 2.50 A; A/B/C/D/E/F=1018-1093. DR PDB; 5KNI; X-ray; 2.50 A; A/B/C/D/E/F/G=1026-1091. DR PDB; 6QXU; X-ray; 1.20 A; A=1104-1314. DR PDB; 6URQ; X-ray; 2.05 A; A/B=328-646. DR PDB; 7KKM; X-ray; 1.58 A; A/B/C/D=1104-1314. DR PDB; 7KKN; X-ray; 1.48 A; A/B/C/D=1104-1314. DR PDB; 7KKO; X-ray; 1.56 A; A/B/C=1104-1314. DR PDB; 7KKP; X-ray; 1.40 A; A/B=1104-1314. DR PDB; 7KKQ; X-ray; 1.59 A; A/B/C/D=1104-1314. DR PDB; 7OCV; X-ray; 1.43 A; A=1104-1314. DR PDBsum; 2RF5; -. DR PDBsum; 3UDD; -. DR PDBsum; 3UH2; -. DR PDBsum; 3UH4; -. DR PDBsum; 4DVI; -. DR PDBsum; 4I9I; -. DR PDBsum; 4K4E; -. DR PDBsum; 4K4F; -. DR PDBsum; 4KRS; -. DR PDBsum; 4LI6; -. DR PDBsum; 4LI7; -. DR PDBsum; 4LI8; -. DR PDBsum; 4MSG; -. DR PDBsum; 4MSK; -. DR PDBsum; 4MT9; -. DR PDBsum; 4N3R; -. DR PDBsum; 4N4V; -. DR PDBsum; 4OA7; -. DR PDBsum; 4TOR; -. DR PDBsum; 4TOS; -. DR PDBsum; 4U6A; -. DR PDBsum; 4UUH; -. DR PDBsum; 4UW1; -. DR PDBsum; 4W5S; -. DR PDBsum; 4W6E; -. DR PDBsum; 5EBT; -. DR PDBsum; 5ECE; -. DR PDBsum; 5ETY; -. DR PDBsum; 5GP7; -. DR PDBsum; 5JHQ; -. DR PDBsum; 5JTI; -. DR PDBsum; 5JU5; -. DR PDBsum; 5KNI; -. DR PDBsum; 6QXU; -. DR PDBsum; 6URQ; -. DR PDBsum; 7KKM; -. DR PDBsum; 7KKN; -. DR PDBsum; 7KKO; -. DR PDBsum; 7KKP; -. DR PDBsum; 7KKQ; -. DR PDBsum; 7OCV; -. DR AlphaFoldDB; O95271; -. DR SMR; O95271; -. DR BioGRID; 114207; 103. DR CORUM; O95271; -. DR DIP; DIP-36652N; -. DR ELM; O95271; -. DR IntAct; O95271; 61. DR MINT; O95271; -. DR STRING; 9606.ENSP00000311579; -. DR BindingDB; O95271; -. DR ChEMBL; CHEMBL6164; -. DR DrugCentral; O95271; -. DR GuidetoPHARMACOLOGY; 3108; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR iPTMnet; O95271; -. DR PhosphoSitePlus; O95271; -. DR BioMuta; TNKS; -. DR EPD; O95271; -. DR jPOST; O95271; -. DR MassIVE; O95271; -. DR MaxQB; O95271; -. DR PaxDb; 9606-ENSP00000311579; -. DR PeptideAtlas; O95271; -. DR ProteomicsDB; 50772; -. [O95271-1] DR ProteomicsDB; 50773; -. [O95271-2] DR Pumba; O95271; -. DR ABCD; O95271; 1 sequenced antibody. DR Antibodypedia; 22078; 405 antibodies from 36 providers. DR DNASU; 8658; -. DR Ensembl; ENST00000310430.11; ENSP00000311579.6; ENSG00000173273.17. [O95271-1] DR Ensembl; ENST00000646522.2; ENSP00000493602.2; ENSG00000285372.2. [O95271-1] DR GeneID; 8658; -. DR KEGG; hsa:8658; -. DR MANE-Select; ENST00000310430.11; ENSP00000311579.6; NM_003747.3; NP_003738.2. DR UCSC; uc003wss.4; human. [O95271-1] DR AGR; HGNC:11941; -. DR CTD; 8658; -. DR DisGeNET; 8658; -. DR GeneCards; TNKS; -. DR HGNC; HGNC:11941; TNKS. DR HPA; ENSG00000173273; Low tissue specificity. DR MIM; 603303; gene. DR neXtProt; NX_O95271; -. DR OpenTargets; ENSG00000173273; -. DR PharmGKB; PA36631; -. DR VEuPathDB; HostDB:ENSG00000173273; -. DR eggNOG; KOG4177; Eukaryota. DR GeneTree; ENSGT00940000156161; -. DR InParanoid; O95271; -. DR OMA; TAETINC; -. DR OrthoDB; 5477658at2759; -. DR PhylomeDB; O95271; -. DR TreeFam; TF326036; -. DR BRENDA; 2.4.2.30; 2681. DR PathwayCommons; O95271; -. DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT. DR Reactome; R-HSA-4641257; Degradation of AXIN. DR Reactome; R-HSA-5545619; XAV939 stabilizes AXIN. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity. DR SignaLink; O95271; -. DR SIGNOR; O95271; -. DR BioGRID-ORCS; 8658; 14 hits in 1163 CRISPR screens. DR ChiTaRS; TNKS; human. DR EvolutionaryTrace; O95271; -. DR GeneWiki; TNKS; -. DR GenomeRNAi; 8658; -. DR Pharos; O95271; Tchem. DR PRO; PR:O95271; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; O95271; Protein. DR Bgee; ENSG00000173273; Expressed in middle temporal gyrus and 204 other cell types or tissues. DR ExpressionAtlas; O95271; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005643; C:nuclear pore; TAS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000242; C:pericentriolar material; TAS:BHF-UCL. DR GO; GO:0042393; F:histone binding; IPI:BHF-UCL. DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007052; P:mitotic spindle organization; TAS:BHF-UCL. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; IMP:BHF-UCL. DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IMP:BHF-UCL. DR GO; GO:1904743; P:negative regulation of telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL. DR GO; GO:1904355; P:positive regulation of telomere capping; IDA:BHF-UCL. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:UniProtKB. DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL. DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; TAS:BHF-UCL. DR GO; GO:0051225; P:spindle assembly; TAS:BHF-UCL. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd09524; SAM_tankyrase1_2; 1. DR CDD; cd01438; tankyrase_like; 1. DR Gene3D; 3.90.228.10; -; 1. DR Gene3D; 6.20.320.10; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR PANTHER; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1. DR PANTHER; PTHR24189; MYOTROPHIN; 1. DR Pfam; PF00023; Ank; 2. DR Pfam; PF12796; Ank_2; 5. DR Pfam; PF13637; Ank_4; 2. DR Pfam; PF00644; PARP; 1. DR Pfam; PF07647; SAM_2; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 17. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF56399; ADP-ribosylation; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 3. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 15. DR PROSITE; PS51059; PARP_CATALYTIC; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR Genevisible; O95271; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Alternative splicing; ANK repeat; KW Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton; KW Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding; Mitosis; KW mRNA transport; NAD; Nuclear pore complex; Nucleotidyltransferase; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Telomere; KW Transferase; Translocation; Transport; Ubl conjugation; KW Wnt signaling pathway; Zinc. FT CHAIN 1..1327 FT /note="Poly [ADP-ribose] polymerase tankyrase-1" FT /id="PRO_0000211333" FT REPEAT 181..209 FT /note="ANK 1" FT /evidence="ECO:0000255" FT REPEAT 215..244 FT /note="ANK 2" FT /evidence="ECO:0000255" FT REPEAT 248..277 FT /note="ANK 3" FT /evidence="ECO:0000255" FT REPEAT 281..310 FT /note="ANK 4" FT /evidence="ECO:0000255" FT REPEAT 335..364 FT /note="ANK 5" FT /evidence="ECO:0000255" FT REPEAT 368..397 FT /note="ANK 6" FT /evidence="ECO:0000255" FT REPEAT 401..430 FT /note="ANK 7" FT /evidence="ECO:0000255" FT REPEAT 434..463 FT /note="ANK 8" FT /evidence="ECO:0000255" FT REPEAT 521..553 FT /note="ANK 9" FT /evidence="ECO:0000255" FT REPEAT 557..586 FT /note="ANK 10" FT /evidence="ECO:0000255" FT REPEAT 590..619 FT /note="ANK 11" FT /evidence="ECO:0000255" FT REPEAT 621..647 FT /note="ANK 12" FT /evidence="ECO:0000255" FT REPEAT 649..679 FT /note="ANK 13" FT /evidence="ECO:0000255" FT REPEAT 683..712 FT /note="ANK 14" FT /evidence="ECO:0000255" FT REPEAT 716..745 FT /note="ANK 15" FT /evidence="ECO:0000255" FT REPEAT 749..778 FT /note="ANK 16" FT /evidence="ECO:0000255" FT REPEAT 782..810 FT /note="ANK 17" FT /evidence="ECO:0000255" FT REPEAT 836..865 FT /note="ANK 18" FT /evidence="ECO:0000255" FT REPEAT 869..898 FT /note="ANK 19" FT /evidence="ECO:0000255" FT REPEAT 902..931 FT /note="ANK 20" FT /evidence="ECO:0000255" FT REPEAT 935..964 FT /note="ANK 21" FT /evidence="ECO:0000255" FT DOMAIN 1030..1089 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT DOMAIN 1112..1317 FT /note="PARP catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397" FT REGION 1..91 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 112..173 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 22..41 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 66..80 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..156 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18436240, FT ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, FT ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, FT ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, FT ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, FT ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, FT ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, FT ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, FT ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, FT ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, FT ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, FT ECO:0007744|PDB:4W6E" FT BINDING 1237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18436240, FT ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, FT ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, FT ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, FT ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, FT ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, FT ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, FT ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, FT ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, FT ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, FT ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, FT ECO:0007744|PDB:4W6E" FT BINDING 1242 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18436240, FT ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, FT ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, FT ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, FT ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, FT ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, FT ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, FT ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, FT ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, FT ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, FT ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, FT ECO:0007744|PDB:4W6E" FT BINDING 1245 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18436240, FT ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, FT ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, FT ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, FT ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, FT ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, FT ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, FT ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, FT ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, FT ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, FT ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, FT ECO:0007744|PDB:4W6E" FT VAR_SEQ 641..643 FT /note="EST -> GHS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9822378" FT /id="VSP_004538" FT VAR_SEQ 644..1327 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9822378" FT /id="VSP_004539" FT MUTAGEN 1184 FT /note="H->A: Loss of activity; when associated with FT A-1291." FT /evidence="ECO:0000269|PubMed:11739745" FT MUTAGEN 1291 FT /note="E->A: Loss of activity; when associated with FT A-1184." FT /evidence="ECO:0000269|PubMed:11739745" FT CONFLICT 83 FT /note="P -> Q (in Ref. 4; AAH98394)" FT /evidence="ECO:0000305" FT CONFLICT 802 FT /note="R -> K (in Ref. 1; AAC79841/AAC79842)" FT /evidence="ECO:0000305" FT CONFLICT 1001 FT /note="E -> G (in Ref. 4; AAH98394)" FT /evidence="ECO:0000305" FT CONFLICT 1266 FT /note="M -> I (in Ref. 4; AAH98394)" FT /evidence="ECO:0000305" FT HELIX 182..192 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 195..201 FT /evidence="ECO:0007829|PDB:5JHQ" FT TURN 204..208 FT /evidence="ECO:0007829|PDB:5JHQ" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 219..225 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 229..237 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 252..258 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 262..270 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 285..291 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 295..303 FT /evidence="ECO:0007829|PDB:5JHQ" FT TURN 318..321 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:5JHQ" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:5JHQ" FT HELIX 334..345 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 348..354 FT /evidence="ECO:0007829|PDB:6URQ" FT TURN 357..361 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 372..378 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 382..390 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 405..411 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 415..423 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 438..444 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 448..456 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 471..474 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 478..498 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 502..510 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:6URQ" FT TURN 519..521 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 525..531 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 537..546 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 561..567 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 571..579 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 594..601 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 604..612 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 628..630 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 633..640 FT /evidence="ECO:0007829|PDB:6URQ" FT HELIX 799..813 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 816..822 FT /evidence="ECO:0007829|PDB:5GP7" FT TURN 825..829 FT /evidence="ECO:0007829|PDB:5GP7" FT TURN 833..836 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 840..846 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 850..858 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 873..880 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 883..891 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 906..913 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 916..924 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 939..942 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 946..955 FT /evidence="ECO:0007829|PDB:5GP7" FT HELIX 1031..1037 FT /evidence="ECO:0007829|PDB:5JU5" FT HELIX 1041..1043 FT /evidence="ECO:0007829|PDB:5JU5" FT HELIX 1044..1049 FT /evidence="ECO:0007829|PDB:5JU5" FT HELIX 1054..1058 FT /evidence="ECO:0007829|PDB:5JU5" FT HELIX 1062..1067 FT /evidence="ECO:0007829|PDB:5JU5" FT HELIX 1073..1086 FT /evidence="ECO:0007829|PDB:5JU5" FT STRAND 1107..1110 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1116..1127 FT /evidence="ECO:0007829|PDB:6QXU" FT TURN 1133..1139 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1145..1154 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1156..1172 FT /evidence="ECO:0007829|PDB:6QXU" FT TURN 1173..1175 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1179..1184 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1189..1195 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1199..1201 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1202..1205 FT /evidence="ECO:0007829|PDB:4TOS" FT STRAND 1209..1217 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1218..1222 FT /evidence="ECO:0007829|PDB:6QXU" FT TURN 1223..1226 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1228..1230 FT /evidence="ECO:0007829|PDB:6QXU" FT TURN 1235..1237 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1243..1245 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1247..1255 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1258..1264 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1268..1270 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1276..1280 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1282..1284 FT /evidence="ECO:0007829|PDB:3UDD" FT STRAND 1286..1289 FT /evidence="ECO:0007829|PDB:4TOR" FT STRAND 1291..1296 FT /evidence="ECO:0007829|PDB:6QXU" FT HELIX 1297..1299 FT /evidence="ECO:0007829|PDB:6QXU" FT STRAND 1300..1310 FT /evidence="ECO:0007829|PDB:6QXU" SQ SEQUENCE 1327 AA; 142039 MW; 44BDE985C715BEFF CRC64; MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA SGLAPFASPR HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA AAPVVPAVST SSAAGVAPNP AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL AESPEAAGVS STAPLGPGAA GPGTGVPAVS GALRELLEAC RNGDVSRVKR LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA NVHARDDGGL IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK LMALLTPLNV NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK GGLVPLHNAC SYGHYEVTEL LLKHGACVNA MDLWQFTPLH EAASKNRVEV CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL RERLTYEFKG HSLLQAAREA DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV TELLLRKGAN VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV DYRLLEASKA GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV EYLLHHGADV HAKDKGGLVP LHNACSYGHY EVAELLVRHG ASVNVADLWK FTPLHEAAAK GKYEICKLLL KHGADPTKKN RDGNTPLDLV KEGDTDIQDL LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP LHLAAGYNNL EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA LLIDAMPPEA LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA ELAVGGASNA GDGAAGTERK EGEVAGLDMN ISQFLKSLGL EHLRDIFETE QITLDVLADM GHEELKEIGI NAYGHRHKLI KGVERLLGGQ QGTNPYLTFH CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG IFNRYNVIRI QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML FCRVTLGKSF LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA YPEYLITYQI MKPEAPSQTA TAAEQKT //