TNKS_DROME
ID TNKS_DROME Reviewed; 1181 AA.
AC Q9VBP3; Q9XZ37;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase;
DE Short=dTNKS {ECO:0000303|PubMed:23622245};
DE EC=2.4.2.30 {ECO:0000269|PubMed:23622245};
DE AltName: Full=Poly [ADP-ribose] polymerase;
DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9H2K2};
GN Name=Tnks {ECO:0000312|FlyBase:FBgn0027508};
GN Synonyms=tankyrase {ECO:0000312|EMBL:AAF56487.1,
GN ECO:0000312|FlyBase:FBgn0027508}; ORFNames=CG4719;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF56487.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|EMBL:AAF56487.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAD34784.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731138};
RC TISSUE=Embryo {ECO:0000269|PubMed:10731138};
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4] {ECO:0000312|EMBL:ACH92236.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH PI31.
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).
CC -!- FUNCTION: Stimulates proteasome activity, probably by ADP-ribosylation
CC of PI31 (PubMed:23622245). Modulates 26S proteasome assembly
CC (PubMed:23622245). {ECO:0000269|PubMed:23622245}.
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:23622245};
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 -!- SUBUNIT: Interacts (via ANK repeats) with PI31.
CC {ECO:0000269|PubMed:23622245}.
CC -!- INTERACTION:
CC Q9VBP3; Q9V637: PI31; NbExp=3; IntAct=EBI-124451, EBI-144377;
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AE014297; AAF56487.1; -; Genomic_DNA.
DR EMBL; AF132196; AAD34784.1; -; mRNA.
DR EMBL; BT044171; ACH92236.1; -; mRNA.
DR RefSeq; NP_651410.1; NM_143153.3.
DR AlphaFoldDB; Q9VBP3; -.
DR SMR; Q9VBP3; -.
DR BioGRID; 68007; 20.
DR IntAct; Q9VBP3; 6.
DR STRING; 7227.FBpp0084264; -.
DR PaxDb; Q9VBP3; -.
DR DNASU; 43095; -.
DR EnsemblMetazoa; FBtr0084890; FBpp0084264; FBgn0027508.
DR GeneID; 43095; -.
DR KEGG; dme:Dmel_CG4719; -.
DR UCSC; CG4719-RA; d. melanogaster.
DR CTD; 8658; -.
DR FlyBase; FBgn0027508; Tnks.
DR VEuPathDB; VectorBase:FBgn0027508; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000171680; -.
DR HOGENOM; CLU_004303_0_0_1; -.
DR InParanoid; Q9VBP3; -.
DR OMA; CPDGKRK; -.
DR OrthoDB; 1115202at2759; -.
DR PhylomeDB; Q9VBP3; -.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DME-4641257; Degradation of AXIN.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR SignaLink; Q9VBP3; -.
DR BioGRID-ORCS; 43095; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tnks; fly.
DR GenomeRNAi; 43095; -.
DR PRO; PR:Q9VBP3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027508; Expressed in spermathecum and 22 other tissues.
DR ExpressionAtlas; Q9VBP3; baseline and differential.
DR Genevisible; Q9VBP3; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:1904355; P:positive regulation of telomere capping; IBA:GO_Central.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:InterPro.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:FlyBase.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IBA:GO_Central.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:InterPro.
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; 3.
DR Pfam; PF12796; Ank_2; 3.
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; 14.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase; Zinc.
FT CHAIN 1..1181
FT /note="Poly [ADP-ribose] polymerase tankyrase"
FT /id="PRO_0000424892"
FT REPEAT 56..85
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 89..118
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 122..151
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 209..238
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 242..271
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 275..304
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 362..394
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 398..427
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 431..458
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 483..513
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 519..548
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT REPEAT 552..581
FT /note="ANK 12"
FT /evidence="ECO:0000255"
FT REPEAT 585..614
FT /note="ANK 13"
FT /evidence="ECO:0000255"
FT REPEAT 638..668
FT /note="ANK 14"
FT /evidence="ECO:0000255"
FT REPEAT 672..701
FT /note="ANK 15"
FT /evidence="ECO:0000255"
FT REPEAT 705..734
FT /note="ANK 16"
FT /evidence="ECO:0000255"
FT REPEAT 738..767
FT /note="ANK 17"
FT /evidence="ECO:0000255"
FT REPEAT 771..799
FT /note="ANK 18"
FT /evidence="ECO:0000255"
FT DOMAIN 889..952
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 969..1174
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 807..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1091
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1099
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT BINDING 1102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O95271"
FT CONFLICT 28
FT /note="F -> S (in Ref. 3; AAD34784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1181 AA; 127945 MW; EB6F0F94E6A3D504 CRC64;
MANSSRSRAI LSVNLDAVMA NDPLRELFEA CKTGEIAKVK KLITPQTVNA RDTAGRKSTP
LHFAAGYGRR EVVEFLLNSG ASIQACDEGG LHPLHNCCSF GHAEVVRLLL KAGASPNTTD
NWNYTPLHEA ASKGKVDVCL ALLQHGANHT IRNSEQKTPL ELADEATRPV LTGEYRKDEL
LEAARSGAED RLLALLTPLN VNCHASDGRR STPLHLAAGY NRIGIVEILL ANGADVHAKD
KGGLVPLHNA CSYGHFDVTK LLIQAGANVN ANDLWAFTPL HEAASKSRVE VCSLLLSRGA
DPTLLNCHSK SAIDAAPTRE LRERIAFEYK GHCLLDACRK CDVSRAKKLV CAEIVNFVHP
YTGDTPLHLA VVSPDGKRKQ LMELLTRKGS LLNEKNKAFL TPLHLAAELL HYDAMEVLLK
QGAKVNALDS LGQTPLHRCA RDEQAVRLLL SYAADTNIVS LEGLTAAQLA SDSVLKLLKN
PPDSETHLLE AAKAGDLDTV RRIVLNNPIS VNCRDLDGRH STPLHFAAGF NRVPVVQFLL
EHGAEVYAAD KGGLVPLHNA CSYGHYEVTE LLVKHGANVN VSDLWKFTPL HEAAAKGKYD
ICKLLLKHGA DPMKKNRDGA TPADLVKESD HDVAELLRGP SALLDAAKKG NLARVQRLVT
PESINCRDAQ GRNSTPLHLA AGYNNFECAE YLLENGADVN AQDKGGLIPL HNASSYGHLD
IAALLIKHKT VVNATDKWGF TPLHEAAQKG RTQLCSLLLA HGADAYMKNQ EGQTPIELAT
ADDVKCLLQD AMATSLSQQA LSASTQSLTS SSPAPDATAA AAPGTSSSSS SAILSPTTET
VLLPTGASMI LSVPVPLPLS SSTRISPAQG AEANGAEGSS SDDLLPDADT ITNVSGFLSS
QQLHHLIELF EREQITLDIL AEMGHDDLKQ VGVSAYGFRH KILKGIAQLR STTGIGNNVN
LCTLLVDLLP DDKEFVAVEE EMQATIREHR DNGQAGGYFT RYNIIRVQKV QNRKLWERYA
HRRQEIAEEN FLQSNERMLF HGSPFINAIV QRGFDERHAY IGGMFGAGIY FAEHSSKSNQ
YVYGIGGGIG CPSHKDKSCY VCPRQLLLCR VALGKSFLQY SAMKMAHAPP GHHSVVGRPS
AGGLHFAEYV VYRGEQSYPE YLITYQIVKP DDSSSGTEDT R
