ID A0A3B3IBB7_ORYLA Unreviewed; 1266 AA.
AC A0A3B3IBB7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC105353570 {ECO:0000313|Ensembl:ENSORLP00000041359.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000041359.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000041359.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000041359.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000041359.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000041359.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3IBB7; -.
DR STRING; 8090.ENSORLP00000041359; -.
DR Ensembl; ENSORLT00000026846.1; ENSORLP00000041359.1; ENSORLG00000029690.1.
DR GeneTree; ENSGT00940000156161; -.
DR InParanoid; A0A3B3IBB7; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000001038; Chromosome 9.
DR Bgee; ENSORLG00000029690; Expressed in animal zygote and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:1904355; P:positive regulation of telomere capping; IBA:GO_Central.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IBA:GO_Central.
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; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
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; 17.
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; 15.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
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:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 145..177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 178..210
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 211..243
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 305..337
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 338..370
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 371..403
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 458..493
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 494..526
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 527..559
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 620..652
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 653..685
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 686..718
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 773..805
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 806..838
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 839..871
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 969..1028
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1051..1256
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 136359 MW; 3A3D31A6AC0EA4EC CRC64;
MAVSRRSSQQ QQQSTLQSPP RSSCLSCAAP ASSVVMAMLV STGPPEVERE CSGEIDLALA
SPDLPAPAIA SNSNSTTPTA SGVGSSVSSP GSGAASPTDG STSSSSSSIG GALRELFEAC
RNGDVSRVKR LVDTVNVNAK DMAGRKSTPL HFAAGFGRKD VVEHLLQTGA NVHARDDGGL
IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHESA IKGKIDVCIV LLQHGADPNI
RNTDGKSALD LADSSAKAVL TGEYKKDELL EAARSGNEEK LMALLTPLNV NCHASDGRKS
TSQKMLSTPL HLAAGYNRVR IVQLLLQHGA DVHAKDKGGL VPLHNACSYG HYEVTELLLK
HGACVNAMDL WQFTPLHEAA SKNRMEVCSL LLSHGADPTL LNCHSKSAVD MAPTPELKER
LTYEFKGHSL LQAAREADIA KVKKTLALEV IGFKHPQTNE TALHCAVASP HPKRKQVTEL
LLRKGANINE KNKDFMTPLH ISAERAHNDV LEVLQKHGAK VNAVDTLGQT ALHRAALAGH
IQTCKLLLSF GADAAIVSLQ GFTAAQMGNE AVQQILNENV PTRNSDVDYR FLEAAKAGDL
DTVQQLCTPQ NVNCRDLEGR HSTPLHFAAG YNRVAVVEYL LHHGADVHAK DKGGLVPLHN
ACSYGHYEVA ELLVRHGASV NVADLWKFTP LHEAAAKGKY EICKLLLKHG ADPTKKNRDG
NIPLDMVKDG DTDIQDLLRG DAALLDAAKK GCLARVQKLC SQENINCRDA QGRNSTPLHL
AAGYNNLEVA EYLLEHGADV NAQDKGGLIP LHNAASYGHV DIAALLIKYN TCVNATDKWA
FTPLHEAAQK GRTQLCALLL AHGADPTMKN QEGQTALDLA TADDIRALLM DAMPPDALPS
CFKPQATVVS ASVISPASTP SCLSAASSID NLAGPLTELA AAAAGTSGVA DGATGSDRKE
GEMAVLDMNI SQFLKSLGLE HLRDIFEREQ ITLDVLVDMG HEELKEIGIN AYGHRHKLIK
GVERLLGGQQ GANPYLTFHC ANQGTILIDL SPDDKEYQSV EEEMQSTIRE HRDGGNAGGV
FSRYNIIKIQ KVVNKKLRER CAHRQKEIAD ENHNHHNERM LFHGSPFINA IIHKGFDERH
AYIGGMFGAG IYFAENSSKS NQYVYGIGGG TGCPTHKDRS CYLCHRQMLF CRVTLGKSFL
QFSAMKMAHA PPGHHSVIGR PSVNGLAYAE YVIYRGEQAY PEYLITYQIL KPECAAQSAA
VAEQKS
//
