TNKS1_HUMAN
ID TNKS1_HUMAN Reviewed; 1327 AA.
AC O95271; O95272; Q4G0F2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 212.
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, 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]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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).
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 Acts as an activator of the Wnt signaling pathway by mediating poly-
CC ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of
CC the beta-catenin destruction complex: poly-ADP-ribosylated target
CC proteins are recognized by RNF146, which mediates their ubiquitination
CC and subsequent degradation (PubMed:19759537, PubMed:21478859). Also
CC mediates PARsylation of BLZF1 and CASC3, followed by recruitment of
CC RNF146 and subsequent ubiquitination (PubMed:21478859). Mediates
CC PARsylation of TERF1, thereby contributing to the regulation of
CC telomere length (PubMed:11739745). Involved in centrosome maturation
CC during prometaphase by mediating PARsylation of HEPACAM2/MIKI
CC (PubMed:22864114). May also regulate vesicle trafficking and modulate
CC 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}.
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. {ECO:0000269|PubMed:19759537}.
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; Q9H2G9: BLZF1; NbExp=2; IntAct=EBI-1105254, EBI-2548012;
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; P52272: HNRNPM; NbExp=3; IntAct=EBI-1105254, EBI-486809;
CC O95271; Q3KP66: INAVA; NbExp=2; IntAct=EBI-1105254, EBI-7545562;
CC O95271; O75367-2: MACROH2A1; NbExp=6; IntAct=EBI-1105254, EBI-6249599;
CC O95271; Q14980: NUMA1; NbExp=2; IntAct=EBI-1105254, EBI-521611;
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; Q9BS91: SLC35A5; NbExp=2; IntAct=EBI-1105254, EBI-18915901;
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. {ECO:0000269|PubMed:21478859}.
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="http://atlasgeneticsoncology.org/Genes/TNKSID43534ch8p23.html";
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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 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 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 AlphaFoldDB; O95271; -.
DR SMR; O95271; -.
DR BioGRID; 114207; 94.
DR CORUM; O95271; -.
DR DIP; DIP-36652N; -.
DR ELM; O95271; -.
DR IntAct; O95271; 128.
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; O95271; -.
DR PeptideAtlas; O95271; -.
DR PRIDE; O95271; -.
DR ProteomicsDB; 50772; -. [O95271-1]
DR ProteomicsDB; 50773; -. [O95271-2]
DR ABCD; O95271; 1 sequenced antibody.
DR Antibodypedia; 22078; 383 antibodies from 36 providers.
DR DNASU; 8658; -.
DR Ensembl; ENST00000310430.11; ENSP00000311579.6; ENSG00000173273.16. [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 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; CPDGKRK; -.
DR OrthoDB; 111565at2759; -.
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; 13 hits in 1085 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 202 other tissues.
DR ExpressionAtlas; O95271; baseline and differential.
DR Genevisible; O95271; HS.
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: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:0006471; P:protein ADP-ribosylation; IDA:BHF-UCL.
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; IC:BHF-UCL.
DR GO; GO:0051225; P:spindle assembly; TAS:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 5.
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 InterPro; IPR028731; TANK1.
DR PANTHER; PTHR24180:SF3; PTHR24180:SF3; 3.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF13857; Ank_5; 1.
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; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 3.
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.
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 A-
FT 1291."
FT /evidence="ECO:0000269|PubMed:11739745"
FT MUTAGEN 1291
FT /note="E->A: Loss of activity; when associated with A-
FT 1184."
FT /evidence="ECO:0000269|PubMed:11739745"
FT CONFLICT 83
FT /note="P -> Q (in Ref. 3; 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. 3; AAH98394)"
FT /evidence="ECO:0000305"
FT CONFLICT 1266
FT /note="M -> I (in Ref. 3; 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
