LOCUS       NP_001099554            1317 aa            linear   ROD 27-MAR-2024
DEFINITION  poly [ADP-ribose] polymerase tankyrase-1 [Rattus norvegicus].
ACCESSION   NP_001099554 XP_001059294 XP_224923
VERSION     NP_001099554.2
DBSOURCE    REFSEQ: accession NM_001106084.2
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 1317)
  AUTHORS   Accialini,P., Irusta,G., Bechis,A., Bas,D., Parborell,F.,
            Abramovich,D. and Tesone,M.
  TITLE     Tankyrase inhibition regulates corpus luteum development and luteal
            function in gonadotropin-treated rats
  JOURNAL   Mol Reprod Dev 84 (8), 719-730 (2017)
   PUBMED   28628258
  REMARK    GeneRIF: Studied role of tankyrase and effect of tankyrase
            inhibitor XAV939 on corpus luteum development , luteal function,
            and Wnt/beta-catenin signaling in gonadotropin-treated prepubertal
            rats.
REFERENCE   2  (residues 1 to 1317)
  AUTHORS   Ramamoorthy,M. and Smith,S.
  TITLE     Loss of ATRX Suppresses Resolution of Telomere Cohesion to Control
            Recombination in ALT Cancer Cells
  JOURNAL   Cancer Cell 28 (3), 357-369 (2015)
   PUBMED   26373281
REFERENCE   3  (residues 1 to 1317)
  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   4  (residues 1 to 1317)
  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   5  (residues 1 to 1317)
  AUTHORS   Zhong,L., Yeh,T.Y., Hao,J., Pourtabatabaei,N., Mahata,S.K.,
            Shao,J., Chessler,S.D. and Chi,N.W.
  TITLE     Nutritional energy stimulates NAD+ production to promote
            tankyrase-mediated PARsylation in insulinoma cells
  JOURNAL   PLoS One 10 (4), e0122948 (2015)
   PUBMED   25876076
  REMARK    GeneRIF: tankyrase-mediated PARsylation is promoted by nutritional
            energy stimulated NAD+ in insulinoma cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1317)
  AUTHORS   Ye,J.Z. and de Lange,T.
  TITLE     TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length
            control complex
  JOURNAL   Nat Genet 36 (6), 618-623 (2004)
   PUBMED   15133513
REFERENCE   7  (residues 1 to 1317)
  AUTHORS   Chang,W., Dynek,J.N. and Smith,S.
  TITLE     TRF1 is degraded by ubiquitin-mediated proteolysis after release
            from telomeres
  JOURNAL   Genes Dev 17 (11), 1328-1333 (2003)
   PUBMED   12782650
REFERENCE   8  (residues 1 to 1317)
  AUTHORS   Seimiya,H. and Smith,S.
  TITLE     The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains
            multiple binding sites for telomeric repeat binding factor 1 (TRF1)
            and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)
  JOURNAL   J Biol Chem 277 (16), 14116-14126 (2002)
   PUBMED   11854288
REFERENCE   9  (residues 1 to 1317)
  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   10 (residues 1 to 1317)
  AUTHORS   Smith,S., Giriat,I., Schmitt,A. and de Lange,T.
  TITLE     Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
  JOURNAL   Science 282 (5393), 1484-1487 (1998)
   PUBMED   9822378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000016.1.
            
            On Oct 27, 2010 this sequence version replaced NP_001099554.1.
            
            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 :: SRR26643287.32852.1,
                                           SRR26643298.71781.1 [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..1317
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..1317
                     /product="poly [ADP-ribose] polymerase tankyrase-1"
                     /EC_number="2.4.2.30"
                     /note="tankyrase-1; tankyrase, TRF1-interacting
                     ankyrin-related ADP-ribose polymerase"
                     /calculated_mol_wt=140632
     Region          172..494
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          208..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(211..212,215..217,219..220,224,227,236,238,240,
                     244..245,248..250,252..253,257,260,269,271,273,277..278,
                     281..283,285..286,290,293,302)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          238..269
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          278..618
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          361..389
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(364..365,368..370,372..373,377,380,389,391,393,
                     397..398,401..403,405..406,410,413,422,424,426,430..431,
                     434..436,438..439,443,446,455)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          391..422
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          424..455
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(513,517..518,521..523,525,529,533,536,545,547,549,
                     553..554,557..559,561..562,566,569,578,580,582,586..587,
                     590..592,594..595,599,602)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          513..545
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          547..578
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          580..609
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          622..943
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          676..704
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(679..680,683..685,687..688,692,695,704,706,708,
                     712..713,716..718,720..721,725,728,737,739,741,745..746,
                     749..751,753..754,758,761,770)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          706..737
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          739..770
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          796..847
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Site            order(826,828,832..833,836..838,840..841,845,848,857,859,
                     861,865..866,869..871,873..874,878,881,890,892,894,
                     898..899,902..904,906..907,911,914,923)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          826..857
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          859..890
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          892..923
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1014..1079
                     /region_name="SAM_tankyrase1,2"
                     /note="SAM domain of tankyrase1,2 subfamily; cd09524"
                     /db_xref="CDD:188923"
     Region          1081..1303
                     /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..1317
                     /gene="Tnks"
                     /coded_by="NM_001106084.2:26..3979"
                     /db_xref="GeneID:290794"
                     /db_xref="RGD:1308784"
ORIGIN      
        1 maasrrsqhh hhhhqqqlqp apgasapppp pppplspgla pgptpaspta gglapfaspr
       61 hglalpegdg srdppdrprs pdpvdgavct vaataaapaa saavgvapsp aggggnnsas
      121 stssptssss sspsspgssi aespeaagvg statlgpgaa glgpgvpavs galrelleac
      181 rngdvsrvkr lvdaanvnak dmagrksspl hfaagfgrkd vvehllqmga nvharddggl
      241 iplhnacsfg haevvslllc qgadpnardn wnytplheaa ikgkidvciv llqhgadpni
      301 rntdgksald ladpsakavl tgeykkdell eaarsgneek lmalltplnv nchasdgrks
      361 tplhlaagyn rvrivqlllq hgadvhakdk gglvplhnac syghyevtel llkhgacvna
      421 mdlwqftplh eaasknrvev cslllshgad ptlvnchgks avdmaptpel rerltyefkg
      481 hsllqaarea dlakvkktla leiinfkqpq shetalhcav aslhpkrkqv aelllrkgan
      541 vneknkdfmt plhvaaerah ndvmevlhkh gakmnaldsl gqtalhraal aghlqtcrll
      601 lsygsdpsii slqgftaaqm gneavqqils estpirtsdv dyrlleaska gdletvkqlc
      661 spqnvncrdl egrhstplhf aagynrvsvv eyllhhgadv hakdkgglvp lhnacsyghy
      721 evaellvrhg asvnvadlwk ftplheaaak gkyeicklll khgadptkkn rdgntpldlv
      781 kegdtdiqdl lrgdaallda akkgclarvq klctpeninc rdtqgrnstp lhlaagynnl
      841 evaeyllerg advnaqdkgg liplhnaasy ghvdiaalli kyntcvnatd kwaftplhea
      901 aqkgrtqlca lllahgadpt mknqegqtpl dlataddira llidamppea lptcfkpqat
      961 vvsaslispa stpsclsaas sidnltgpla elavggasna gdgaagaerk egevagldmn
     1021 isqflkslgl ehlrdifete qitldvladm gheelkeigi nayghrhkli kgverllggq
     1081 qgtnpyltfh cvnqgtilld lapedkeyqs veeemqstir ehrdggnagg ifnrynviri
     1141 qkvvnkklre rfchrqkevs eenhnhhner mlfhgspfin aiihkgfder hayiggmfga
     1201 giyfaenssk snqyvygigg gtgcpthkdr scyvchrqml fcrvtlgksf lqfstmkmah
     1261 appghhsvig rpsvnglaya eyviyrgeqa ypeylityqi mkpeapsqta taaeqkt
//
