ID H9ZDV5_MACMU Unreviewed; 1166 AA.
AC H9ZDV5; A0A1D5QHS5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE Short=PARP {ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN Name=TNKS2 {ECO:0000313|EMBL:AFH34121.1,
GN ECO:0000313|Ensembl:ENSMMUP00000047597.2,
GN ECO:0000313|VGNC:VGNC:78983};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH34121.1};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|EMBL:AFH34121.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH34121.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
RN [3] {ECO:0000313|Ensembl:ENSMMUP00000047597.2}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000047597.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033987};
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; JU477317; AFH34121.1; -; mRNA.
DR RefSeq; NP_001253187.1; NM_001266258.1.
DR PaxDb; 9544-ENSMMUP00000009820; -.
DR Ensembl; ENSMMUT00000068412.2; ENSMMUP00000047597.2; ENSMMUG00000007478.4.
DR GeneID; 698050; -.
DR KEGG; mcc:698050; -.
DR CTD; 80351; -.
DR VEuPathDB; HostDB:ENSMMUG00000007478; -.
DR VGNC; VGNC:78983; TNKS2.
DR GeneTree; ENSGT00940000159911; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000006718; Chromosome 9.
DR Bgee; ENSMMUG00000007478; Expressed in Ammon's horn and 21 other cell types or tissues.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd09524; SAM_tankyrase1_2; 1.
DR CDD; cd01438; tankyrase_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 6.20.320.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
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 PANTHER; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 14.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114}; NAD {ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 57..89
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 90..122
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 123..155
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 210..242
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 243..275
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 276..308
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 363..398
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 399..431
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 432..464
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 525..557
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 558..590
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 591..623
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 678..710
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 711..743
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 744..776
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 877..936
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 959..1164
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 819..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 126904 MW; 57999956F51EB241 CRC64;
MSGRRCAGGG AASASAAAEA MEPAARELFE ACRNGDVERV KRLVTPEKVN SRDTAGRKST
PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS FGHAEVVNLL LRHGADPNAR
DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP TIRNTDGRTA LDLADPSAKA VLTGEYKKDE
LLESARSGNE EKMMALLTPL NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK
DKGDLVPLHN ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG
ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH LSLEMVNFKH
PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF LTPLHVASEK AHNDVVEVVV
KHEAKVNALD NLGQTSLHRA AYCGHLQTCR LLLSYGCDPN IISLQGFTAL QMGNENVQQL
LQEGISLGNS EADRQLLEAA KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS
VVEYLLQHGA DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA
AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL DAAKKGCLAR
VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ HGADVNAQDK GGLIPLHNAA
SYGHVDVAAL LIKYNACVNA TDKWAFTPLH EAAQKGRTQL CALLLAHGAD PTLKNQEGQT
PLDLVSADDV SALLTAAMPP SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS
LDNLSGSFSE LSSVVSSSGT EGASGLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT
LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG SGTILIDLSP
DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV CNKKLWERYT HRRKEVSEEN
HNHANERMLF HGSPFVNAII HKGFDERHAY IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG
CPVHKDRSCY ICHRQLLFCR VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV
IYRGEQAYPE YLITYQIMRP EGMVDG
//
