ID A0A3B1J2X9_ASTMX Unreviewed; 995 AA.
AC A0A3B1J2X9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|PIRNR:PIRNR000489, ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.30 {ECO:0000256|PIRNR:PIRNR000489};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000036210.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000036210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair.
CC {ECO:0000256|PIRNR:PIRNR000489}.
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:0000256|ARBA:ARBA00024164};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000256|ARBA:ARBA00024164};
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:0000256|ARBA:ARBA00024159};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000256|ARBA:ARBA00024159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D-
CC ribosyl)-L-histidyl-[protein] + nicotinamide; Xref=Rhea:RHEA:72071,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:18085, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29979, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:191398; Evidence={ECO:0000256|ARBA:ARBA00034220};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72072;
CC Evidence={ECO:0000256|ARBA:ARBA00034220};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000256|ARBA:ARBA00024165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000256|ARBA:ARBA00024165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000256|ARBA:ARBA00024171};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000256|ARBA:ARBA00024171};
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 ECO:0000256|PIRNR:PIRNR000489};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|PIRNR:PIRNR000489}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000489}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR AlphaFoldDB; A0A3B1J2X9; -.
DR Ensembl; ENSAMXT00000032513.1; ENSAMXP00000036210.1; ENSAMXG00000006465.2.
DR GeneTree; ENSGT00940000156058; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000006465; Expressed in testis and 14 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140815; F:NAD+-protein-histidine ADP-ribosyltransferase activity; IEA:RHEA.
DR GO; GO:0140805; F:NAD+-protein-serine ADP-ribosyltransferase activity; IEA:RHEA.
DR GO; GO:0140808; F:NAD+-protein-tyrosine ADP-ribosyltransferase activity; IEA:RHEA.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR CDD; cd17747; BRCT_PARP1; 1.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd08001; WGR_PARP1_like; 1.
DR Gene3D; 1.10.20.130; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR038650; PADR1_C_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR049296; PARP1-like_PADR1_N.
DR InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF112; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF21728; PADR1_N; 1.
DR Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS52007; PADR1; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
DR PROSITE; PS00347; ZF_PARP_1; 2.
DR PROSITE; PS50064; ZF_PARP_2; 2.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|PIRNR:PIRNR000489};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000489};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR000489}; Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000489};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000489};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000489};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000489};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 10..92
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 113..203
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 391..467
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 549..645
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 669..786
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 795..995
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 198..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..455
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 369..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 111249 MW; 2707A1E7DFA459C0 CRC64;
MADAQDDKRY KAEYAKSGRA SCKKCKDNIA KDSLRMAIMV QSPMFDGKVP HWHHFSCFWH
RAAVQETSDI SGFTDLRWED QEKVKKAIEG GGAPGAKSDQ KGAAKGEKTL NDFAVEYAKS
NRSTCKGCDQ KIEKDQIRVS KKTVDPEKPQ LGLIDRWYHT SCFVSRREEL VFKPEYSAAQ
LKGFAALRAE DKDELKKRLP AVKTEGKRKA DSVDGEGAAK KQKKEAEEEK QLQQQLKEQS
QLVWGIKDKL KKYCSTNDMK ELLIANDQEV PSGESNVLDR LSDCMAFGAL KPCETCQGQI
VFKSDAYYCT GDISAWTKCN VRTQTPNRKD WVTPKEFHEV PFLKKFKFKR QDRLFPKEAP
APPAVPASTA TTAAATSSTS RAPIETPTEV PADKPLTGLK VLTVGKLSKN KDELKAAVEE
LGGKITGTVN KAVFCLSTKK EVEKMSKKME EVRDAGVRVV SEDFLSDIKS SGKALQELIS
LHGISPWGAE VKLEGPAPAP SGASKSTGAM SSKSSGRSNE EEGSSKSKKM KLTVKGGAAV
DPDSGLGNCA HVLDQNGKIH SATLGLVDIV RGTNSYYKLQ LLEDDVQKRY WVFRSWGRVG
TTIGGNKLDK FYDKNSAMDN FRSVYEEKTG NSWTSSSFTK YPNKFYPLEI DYGQDEEAVK
KLAASSGTKS QLAKPIQELI RMIFDVESMK KAMVEFEIDL QKMPLGKLSK RQIQSAYSLL
SEVQQAVSDN APEPMILDLS NRFYTLIPHD FGMKKPPLLS NLDYIQTKVQ MLDNLLDIEV
AYSLLRGGAE DNKKDPIDIN YEKLKTKIEV LDNSSEEAQL IHQYVKNTHA STHNTYTLEV
EEIFKIDREG EYQRYRPFKE LPNRQLLWHG SRTTNYAGIL SQGLRIAPPE APVTGYMFGK
GVYFADMVSK SANYCHTSQA DPVGLILLGE VALGNMHELK KASHITKLPK GKHSVKGKAT
IQIVHTHMLF FLQFKKIKYY EHKCHELLLK EFAVV
//
