ID U3BMA9_CALJA Unreviewed; 1013 AA.
AC U3BMA9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
GN Name=PARP1 {ECO:0000313|EMBL:JAB06909.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB06909.1};
RN [1] {ECO:0000313|EMBL:JAB06909.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB06909.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB14549.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB34479.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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 -!- FUNCTION: This cleavage form irreversibly binds to DNA breaks and
CC interferes with DNA repair, promoting DNA damage-induced apoptosis.
CC {ECO:0000256|ARBA:ARBA00034299}.
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 -!- SUBUNIT: Interacts (when auto-poly-ADP-ribosylated) with AIFM1.
CC {ECO:0000256|ARBA:ARBA00034324}.
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 EMBL; GAMT01004952; JAB06909.1; -; mRNA.
DR EMBL; GAMS01008587; JAB14549.1; -; mRNA.
DR EMBL; GAMQ01007372; JAB34479.1; -; mRNA.
DR AlphaFoldDB; U3BMA9; -.
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: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 GO; GO:0051052; P:regulation of DNA metabolic process; IEA:UniProt.
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; 1.
DR PROSITE; PS50064; ZF_PARP_2; 2.
PE 2: Evidence at transcript level;
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 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 9..93
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 384..460
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 541..637
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 661..778
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 787..1013
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 198..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..455
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1013 AA; 113078 MW; 02AB8372CA04E46F CRC64;
MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
GHSIRHPDIE VDGFSELRWD DQQKVKKTAE AGGMTGKGQD GIGSKAEKTL GDFAAEYAKS
NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ LGMIDRWYHP DCFVKNREEL GFRPEYSASQ
LKGFSLLATE DKEALKKQLP GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA
QNDLIWNIKD ELKKVCSTND LKELLIFNKQ QVPSGESAIL DQVADGMAFG ALLPCEECSG
QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV KKQNRIFPPE
TSAPVAAAPP PSTASKPAAV NSASAGKPLS NMKILTLGKL SRNKDEVKAM IEKLGGKLTG
TANKASLCIS TKKEVEKMNK KMEEVKEANV RVVSEDFLQD VSTTTKSLQE LFSAHILSPW
GAEVKAEPVE VVAPKGKSGA PLSKKSKGQV KEEGINKSEK RMKLTLKGGA AVDPDSGLEH
SAHVLEKSGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR VGTVIGSNKL
EQMPSKEDAI EHFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVNPGT
KSKLPKAVQD LIKMIFDVES MKKAMVEYEI DLQKMPLGKL SKRQIQAAYS ILSEVQQAVS
QGSSDSQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG
SDDSSKDPID VNYEKLRTDI KVVNRDSEEA EIIRKYVKNT HATTHNAYDL EVVDIFKIER
EGECQRYKPF KQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
SKSANYCHTS QGDPIGLILL GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS
ITLDGVEVPL GTGISSGVND TCLLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW
//
