TNKS1_CAEEL
ID TNKS1_CAEEL Reviewed; 2276 AA.
AC Q9TXQ1; Q8I0N5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Poly [ADP-ribose] polymerase tankyrase {ECO:0000303|PubMed:14706351};
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:Q9H2K2};
DE AltName: Full=Poly ADP-ribose metabolism enzyme 5 {ECO:0000303|PubMed:14706351};
DE AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9H2K2};
GN Name=tank-1 {ECO:0000312|WormBase:ZK1005.1a};
GN Synonyms=pme-5 {ECO:0000303|PubMed:14706351};
GN ORFNames=ZK1005.1 {ECO:0000312|WormBase:ZK1005.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RC STRAIN=Bristol N2;
RX PubMed=14706351; DOI=10.1016/j.dnarep.2003.10.012;
RA Gravel C., Stergiou L., Gagnon S.N., Desnoyers S.;
RT "The C. elegans gene pme-5: molecular cloning and role in the DNA-damage
RT response of a tankyrase orthologue.";
RL DNA Repair 3:171-182(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION BY IRRADIATION.
RX PubMed=19104912; DOI=10.1007/s11010-008-9986-z;
RA White C., Gagnon S.N., St-Laurent J.F., Gravel C., Proulx L.I.,
RA Desnoyers S.;
RT "The DNA damage-inducible C. elegans tankyrase is a nuclear protein closely
RT linked to chromosomes.";
RL Mol. Cell. Biochem. 324:73-83(2009).
CC -!- FUNCTION: Poly[ADP-ribose] polymerases modify various nuclear proteins
CC by poly(ADP-ribosyl)ation, a post-translational modification
CC synthesized after DNA damage that appears as an obligatory step in a
CC detection/signaling pathway leading to the reparation of DNA strand
CC breaks and programmed cell death. {ECO:0000269|PubMed:14706351}.
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:0000250|UniProtKB:Q9H2K2};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19104912}. Chromosome
CC {ECO:0000269|PubMed:19104912}. Note=Associated with condensing
CC chromosomes. {ECO:0000269|PubMed:19104912}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=PME-5L;
CC IsoId=Q9TXQ1-1; Sequence=Displayed;
CC Name=b; Synonyms=PME-5S;
CC IsoId=Q9TXQ1-2; Sequence=VSP_012461;
CC -!- TISSUE SPECIFICITY: Expressed throughout the head and tail, in germ
CC cells and somatic cells. {ECO:0000269|PubMed:19104912}.
CC -!- DEVELOPMENTAL STAGE: Detected at all stages (PubMed:14706351,
CC PubMed:19104912). Expressed at low level in embryos compared to larvae
CC (PubMed:14706351). Peaks in young adults (PubMed:14706351).
CC {ECO:0000269|PubMed:14706351, ECO:0000269|PubMed:19104912}.
CC -!- INDUCTION: By irradiation (PubMed:14706351, PubMed:19104912). This
CC induction is dependent on hus-1 (PubMed:14706351).
CC {ECO:0000269|PubMed:14706351, ECO:0000269|PubMed:19104912}.
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DR EMBL; AF548287; AAN40683.1; -; mRNA.
DR EMBL; FO081160; CCD69563.1; -; Genomic_DNA.
DR EMBL; FO081160; CCD69564.1; -; Genomic_DNA.
DR PIR; C88948; C88948.
DR PIR; D88948; D88948.
DR RefSeq; NP_001024306.1; NM_001029135.3. [Q9TXQ1-2]
DR RefSeq; NP_503401.3; NM_071000.6. [Q9TXQ1-1]
DR AlphaFoldDB; Q9TXQ1; -.
DR SMR; Q9TXQ1; -.
DR BioGRID; 43692; 6.
DR STRING; 6239.ZK1005.1a; -.
DR EPD; Q9TXQ1; -.
DR PaxDb; Q9TXQ1; -.
DR PeptideAtlas; Q9TXQ1; -.
DR PRIDE; Q9TXQ1; -.
DR EnsemblMetazoa; ZK1005.1a.1; ZK1005.1a.1; WBGene00004053. [Q9TXQ1-1]
DR EnsemblMetazoa; ZK1005.1b.1; ZK1005.1b.1; WBGene00004053. [Q9TXQ1-2]
DR GeneID; 178623; -.
DR KEGG; cel:CELE_ZK1005.1; -.
DR UCSC; ZK1005.1b; c. elegans. [Q9TXQ1-1]
DR CTD; 178623; -.
DR WormBase; ZK1005.1a; CE24712; WBGene00004053; tank-1. [Q9TXQ1-1]
DR WormBase; ZK1005.1b; CE33259; WBGene00004053; tank-1. [Q9TXQ1-2]
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000170301; -.
DR InParanoid; Q9TXQ1; -.
DR OMA; NSTICLM; -.
DR OrthoDB; 18682at2759; -.
DR PhylomeDB; Q9TXQ1; -.
DR PRO; PR:Q9TXQ1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004053; Expressed in larva and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:WormBase.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IGI:WormBase.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:WormBase.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0010332; P:response to gamma radiation; IEP:WormBase.
DR Gene3D; 1.20.142.10; -; 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; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00248; ANK; 16.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF48403; SSF48403; 4.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Chromosome; DNA damage; DNA repair;
KW Glycosyltransferase; NAD; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..2276
FT /note="Poly [ADP-ribose] polymerase tankyrase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000211337"
FT REPEAT 345..374
FT /note="ANK 1"
FT REPEAT 378..407
FT /note="ANK 2"
FT REPEAT 411..440
FT /note="ANK 3"
FT REPEAT 461..490
FT /note="ANK 4"
FT REPEAT 498..527
FT /note="ANK 5"
FT REPEAT 531..560
FT /note="ANK 6"
FT REPEAT 564..593
FT /note="ANK 7"
FT REPEAT 598..627
FT /note="ANK 8"
FT REPEAT 675..725
FT /note="ANK 9"
FT REPEAT 729..758
FT /note="ANK 10"
FT REPEAT 970..999
FT /note="ANK 11"
FT REPEAT 1171..1200
FT /note="ANK 12"
FT REPEAT 1204..1233
FT /note="ANK 13"
FT REPEAT 1472..1501
FT /note="ANK 14"
FT REPEAT 1505..1535
FT /note="ANK 15"
FT REPEAT 1662..1706
FT /note="ANK 16"
FT DOMAIN 1788..1889
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 1910..2045
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 2047..2276
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 852..889
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:14706351"
FT /id="VSP_012461"
SQ SEQUENCE 2276 AA; 254576 MW; 8D1ADA31DBD2794F CRC64;
MARRVNKKKS PVKAARKIDG QIGRRVVDGV RAKSSRQRHQ AVLYQAPTPT VIRRKTTKTA
IVKKTVVVVK KGGKVVKKSS KTGQKVKAVK APKVKAPSKK GNDRLTPRVI TEYQENPFFY
DPQVPEYISA SVYHRWITRA VRNGNMKEIK DYYKSKKCQK SAIYTSFAYS FDTSACDEAL
RQDIKFATEF FKMNNKMEVD NSYHPGKEPN LLQKKTTGRK NYYMLGRHTR QIEMGRGGKE
GNNALLNYDT RTDEPNPLTK LIEDNVTYTK LYQLCKIPDG PIVEHHIEMH FVTAVRMGHR
DLASALAQGP VKMHCNDLHR ATLKDQKLPA KILPVSVAKK AYMNKNITPL HTAAISNSTH
MLEAMRAVYP TINIPDQDNW YTMHYAACAP GTAPMEFLLK NGGSVTMLTK QTETPLHVAA
RAGRAVNCTF LMKEMLDLEK GDDGESTIRA DRSIINARTR SGNSALHLAV LRNNLDVVDA
LLAEPTIVVD NPTSTGQNRL TPLMMACGKG YLEMAKKLVE KGALVEGKDK KKRTPLIHAM
LNGQIHTAAF LLAKGASLTL ADSSGNTAAH YAAAYGFLDC LKLLASIDDN ILSEPNDWQL
YPLSVAYLKG HYGIVTWLLE GPHKDKANIN AKDNNGATLL SNLLSYADET MHKELLSQIE
YLVARKADAS LADSSGQTPL HLFSMQRIIL KGSGEAAEND AMRMTLDNYK KCFNTLIKAG
AKVDVYDHED NTPLHYALTN GNLMLFNLML DKVANKRNLF EKWANHQNFL HEILALPMKV
YGDQVLWKGE TLTKPAYDVL PILKELHENL PDLFEKWISE VNKAGYSPIV EAIKQYQALA
ANKKLRGEAD QNGNPGFGNA IARGRVHNQF GRDRMNQSQA PHCDSYELKT FISTVNELFE
WVIRLGPFQL TQKYINSENS AAVTLANLAM SIPIECGRHQ QNQLALFKIL IKLSKEFNKV
DEFLTQKNEK DDVLIVQAIM FDKPNVVELI LDTASEMHLI HGTHNAIKEN ELEVVVHKTI
IMYMIEMRMW ELIPKVNASS EFWKSKDAKG NSVWHYAARV NSHKTVGLFK MIESKGVRRE
TNDDGRSVLH VATLACDGSA DSVLEPIAWL STRCPIDAVD KFNRTALHYA FGNENDFKEG
NVPFGESDPI AVVSLLSSLI RPEQIEIADV NGNTILHLAA IKNSTICLMT LIRKKCHVDL
KNKDGNTPLA LAVHHGRQSS ALTLIQANAD VTEKIFVPAL KPTSDFDQNS SGTEAEKFWK
WHGKEKKVLE DLHTTIPASV VSKGGSWEAM VYVLLDVLGQ NTGSMAQLTD AALRRGQLNL
ANQLLKSIEA LIDGAVLNSS YDLLDTFAEK CFGALTSEET IEKTVLNRII LTRGLGLKQP
ETMKIIRTAL QNGNWNLLNF LKSEMGTAWK NQKIETPTEN PIRSLLIYMN EKSVSSEAIG
FLEELRQMRG VNIDALCQLE IPGKFKKILD YGLIPPISFA VLQENPNMIR ALRNAGASLK
TQDDYGRTPL MYAIMTNNRS VVDAIVGDGK LAVVLHKQKA VATGPRCVAV PMRFGATSRA
FIPAAAFASV PARVESDEEE EDNSGSESGE DGAASENKSE HGSENGESGN GSDDEDDDDD
DSSPPPAKKS RIAKEAAGPS TGPKRKKLVI TDPSLFSARD HKENNPLHYF IEPLAWENVE
LLGDLAAANK TAIVQCLIDK RSPNPIELAA MKMNRRMKSE MLKIVKNAAF PRPIKETKLT
LQQVHIEPLS DVDEDAAKFL AKWVEEKDKK KTSEAPKPHK SSTYSTNGLV SFCDETQQYF
DVLMNKTDLM YGRCGFHNFY RMQIIKRRDA ELFILFTNWG RIGSGMGEFQ TTPFNSLELA
AKEFKSIFKS KSGNEWAPLA NFRDMPKKYR LVETDSTPTS LAEIELTWKK NTEKDPIRRM
IADISDAKTL KTYASQVQMY GGSSQPFGRF TKENIEKAKL VLDKLEKNAN RIKQMVEAQT
GVVESNLLDA YITTSELSGD YYSLIPSGEY EFSNLTRLDN VEEIARHRAR LNRCQEIETA
TRLLCAAEFR QDLDRVDYIR SAIQCEYRLE TPDSDISQRL LQWIHNSGGK QAKVKMILEI
SPMLSTEKFE PFVNDDNQKF LWHGTKATNL MSILKNGFLI DPPSACKNGN LFGSGIYLAD
SFEKSTHYCQ PSAGGINYML VCQTALGKVR TLDTIPYHYM NQSSSSAEKY EDTLHYIGDR
FPAGSLTNDG VGMPLLPLRK RDPIQGSNYG FGTLDFSEYI VRNPNRVLPK YIVMYK
