LOCUS       NP_001101077            1166 aa            linear   ROD 31-MAR-2024
DEFINITION  poly [ADP-ribose] polymerase tankyrase-2 [Rattus norvegicus].
ACCESSION   NP_001101077 XP_001080123 XP_220047
VERSION     NP_001101077.2
DBSOURCE    REFSEQ: accession NM_001107607.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1166)
  AUTHORS   Kuusela,S., Wang,H., Wasik,A.A., Suleiman,H. and Lehtonen,S.
  TITLE     Tankyrase inhibition aggravates kidney injury in the absence of
            CD2AP
  JOURNAL   Cell Death Dis 7 (7), e2302 (2016)
   PUBMED   27441654
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1166)
  AUTHORS   Kulak,O., Chen,H., Holohan,B., Wu,X., He,H., Borek,D.,
            Otwinowski,Z., Yamaguchi,K., Garofalo,L.A., Ma,Z., Wright,W.,
            Chen,C., Shay,J.W., Zhang,X. and Lum,L.
  TITLE     Disruption of Wnt/beta-Catenin Signaling and Telomeric Shortening
            Are Inextricable Consequences of Tankyrase Inhibition in Human
            Cells
  JOURNAL   Mol Cell Biol 35 (14), 2425-2435 (2015)
   PUBMED   25939383
REFERENCE   3  (residues 1 to 1166)
  AUTHORS   Barkauskaite,E., Jankevicius,G. and Ahel,I.
  TITLE     Structures and Mechanisms of Enzymes Employed in the Synthesis and
            Degradation of PARP-Dependent Protein ADP-Ribosylation
  JOURNAL   Mol Cell 58 (6), 935-946 (2015)
   PUBMED   26091342
  REMARK    Review article
REFERENCE   4  (residues 1 to 1166)
  AUTHORS   Vyas,S., Matic,I., Uchima,L., Rood,J., Zaja,R., Hay,R.T., Ahel,I.
            and Chang,P.
  TITLE     Family-wide analysis of poly(ADP-ribose) polymerase activity
  JOURNAL   Nat Commun 5, 4426 (2014)
   PUBMED   25043379
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1166)
  AUTHORS   Cerone,M.A., Burgess,D.J., Naceur-Lombardelli,C., Lord,C.J. and
            Ashworth,A.
  TITLE     High-throughput RNAi screening reveals novel regulators of
            telomerase
  JOURNAL   Cancer Res 71 (9), 3328-3340 (2011)
   PUBMED   21531765
REFERENCE   6  (residues 1 to 1166)
  AUTHORS   Hsiao,S.J., Poitras,M.F., Cook,B.D., Liu,Y. and Smith,S.
  TITLE     Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit
            growth defects but have normal telomere length and capping
  JOURNAL   Mol Cell Biol 26 (6), 2044-2054 (2006)
   PUBMED   16507985
REFERENCE   7  (residues 1 to 1166)
  AUTHORS   Chiang,Y.J., Nguyen,M.L., Gurunathan,S., Kaminker,P.,
            Tessarollo,L., Campisi,J. and Hodes,R.J.
  TITLE     Generation and characterization of telomere length maintenance in
            tankyrase 2-deficient mice
  JOURNAL   Mol Cell Biol 26 (6), 2037-2043 (2006)
   PUBMED   16507984
REFERENCE   8  (residues 1 to 1166)
  AUTHORS   Cook,B.D., Dynek,J.N., Chang,W., Shostak,G. and Smith,S.
  TITLE     Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2
            at human telomeres
  JOURNAL   Mol Cell Biol 22 (1), 332-342 (2002)
   PUBMED   11739745
REFERENCE   9  (residues 1 to 1166)
  AUTHORS   Kaminker,P.G., Kim,S.H., Taylor,R.D., Zebarjadian,Y., Funk,W.D.,
            Morin,G.B., Yaswen,P. and Campisi,J.
  TITLE     TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes
            rapid induction of cell death upon overexpression
  JOURNAL   J Biol Chem 276 (38), 35891-35899 (2001)
   PUBMED   11454873
REFERENCE   10 (residues 1 to 1166)
  AUTHORS   Lyons,R.J., Deane,R., Lynch,D.K., Ye,Z.S., Sanderson,G.M.,
            Eyre,H.J., Sutherland,G.R. and Daly,R.J.
  TITLE     Identification of a novel human tankyrase through its interaction
            with the adaptor protein Grb14
  JOURNAL   J Biol Chem 276 (20), 17172-17180 (2001)
   PUBMED   11278563
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from
            JAXUCZ010000001.1.
            
            On Jan 9, 2008 this sequence version replaced NP_001101077.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26360190.741940.1,
                                           SRR26643297.5208.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760386
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1166
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q53"
     Protein         1..1166
                     /product="poly [ADP-ribose] polymerase tankyrase-2"
                     /EC_number="2.4.2.30"
                     /note="tankyrase, TRF1-interacting ankyrin-related
                     ADP-ribose polymerase 2; tankyrase-2-like"
                     /calculated_mol_wt=126649
     Region          60..343
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          60..88
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(63..64,67..69,71..72,76,79,88,90,92,96..97,100..102,
                     104..105,109,112,121,123,125,129..130,133..135,137..138,
                     142,145,154)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          90..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          160..470
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          213..241
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(216..217,220..222,224..225,229,232,241,243,245,
                     249..250,253..255,257..258,262,265,274,276,278,282..283,
                     286..288,290..291,295,298,307)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          243..274
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          276..307
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          365..397
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          399..430
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          433..521
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          487..789
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          528..556
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(531..532,535..537,539..540,544,547,556,558,560,
                     564..565,568..570,572..573,577,580,589,591,593,597..598,
                     601..603,605..606,610,613,622)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          558..589
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          591..622
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          644..674
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          648..699
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Region          681..709
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(684..685,688..690,692..693,697,700,709,711,713,
                     717..718,721..723,725..726,730,733,742,744,746,750..751,
                     754..756,758..759,763,766,775)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          711..742
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          744..775
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          871..936
                     /region_name="SAM_tankyrase1,2"
                     /note="SAM domain of tankyrase1,2 subfamily; cd09524"
                     /db_xref="CDD:188923"
     Region          938..1160
                     /region_name="tankyrase_like"
                     /note="Tankyrases interact with the telomere reverse
                     transcriptase complex (TERT). Tankyrase 1
                     poly-ADP-ribosylates Telomere Repeat Binding Factor 1
                     (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or
                     TRF1. The tankyrases also contain multiple ankyrin...;
                     cd01438"
                     /db_xref="CDD:238718"
     CDS             1..1166
                     /gene="Tnks2"
                     /coded_by="NM_001107607.2:1..3501"
                     /db_xref="GeneID:309512"
                     /db_xref="RGD:1305026"
ORIGIN      
        1 msgrrcaggg aacssavaea vepsarelfe acrngdverv krlvtpekvn srdtagrkst
       61 plhfaagfgr kdvveyllqn ganvqarddg gliplhnacs fghaevvnll lqhgadpnar
      121 dnwnytplhe aaikgkidvc ivllqhgaep tirntdgrta ldladpsaka vltgdykkde
      181 llesarsgne ekmmalltpl nvnchasdgr kstplhlaag ynrvkivqll lqhgadvhak
      241 dkgdlvplhn acsyghyevt ellvkhgacv namdlwqftp lheaasknrv evcslllsyg
      301 adptllnchn ksaidlapta qlkerlsyef kghsllqaar eadvtrikkh lslemvnfkh
      361 pqthetalhc aaaspypkrk qicelllrkg antnektkef ltplhvasen ahndvvevvv
      421 kheakvnald slgqtslhra ahcghlqtcr lllsygcdpn iislqgltal qmgnenvqql
      481 lqegvslghs eadrqlleaa kagdvetvkk lctvqsvncr diegrqstpl hfaagynrvs
      541 vveyllqhga dvhakdkggl vplhnacsyg hyevaellvk hgavvnvadl wkftplheaa
      601 akgkyeickl llqhgadptk knrdgntpld lvkdgdtdiq dllrgdaall daakkgclar
      661 vkklsspdnv ncrdtqgrhs tplhlaagyn nlevaeyllq hgadvnaqdk ggliplhnaa
      721 syghvdvaal likynacvna tdkwaftplh eaaqkgrtql calllahgad ptlknqegqt
      781 pldlvsaddv salltaampp salptcykpq vlsgvrspga tadalssgps spsslsaass
      841 ldnlagsfse lsavvssstt egatglerke dsgidfsitq firnlglehl mdifereqit
      901 ldvlvemghk elkeigisay ghrhrlikgv erlisgqqgl npyltlnnsg sgtilidlsp
      961 ddkefqsvee emqstvrehr dgghaggifn rysilkiqkv cnkklweryt hrrkevseen
     1021 hnhanermlf hgspfvnaii hkgfderhay iggmfgagiy faenssksnq yvygigggtg
     1081 cpvhkdrscy ichrqllfcr vtlgksflqf samkmahspp ghhsvtgrps vnglalaeyv
     1141 iyrgeqaype ylityqivrp egmgdg
//
