ID A0A2K5K2Q7_COLAP Unreviewed; 1015 AA.
AC A0A2K5K2Q7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000035342.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000035342.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- 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 AlphaFoldDB; A0A2K5K2Q7; -.
DR STRING; 336983.ENSCANP00000035342; -.
DR Ensembl; ENSCANT00000058578.1; ENSCANP00000035342.1; ENSCANG00000041340.1.
DR Proteomes; UP000233080; Unplaced.
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 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; 1.
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 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:UP000233080};
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 24..94
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 114..204
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 386..462
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 543..639
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 663..780
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 789..1015
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 199..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..457
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1015 AA; 112832 MW; 22856C60D7C44AD9 CRC64;
APASSFQFAD VSLCINNSGS HLPCSSSLPT YYPSLVLMVK ISPMFDGKVP HWYHFSCFWK
VGHSIRHPDV EVDGFSELRW DDQQKVKKTA EAGGVTGKGQ DGIGSKAEKM LGDFAAEYAK
SNRSTCKGCM EKIEKGQVRL SKKMLDPEKP QLGMIDRWYH PHCFVKNREE LGFRPEYSAS
QLKGFSLLAA EDKEALKKQL PGVKSEGKRK GDEVDGVDEV TKKKPKKEKD KDSKLEKALK
AQNDLIWNIK DELKKVCSTN DLKELLIFNK QQVPSGESAI LDQVADGMAF GALLPCKECS
GQLVFKSDAY YCTGDVTAWT KCMVKTQTPN RKEWVTPKEF REISYLKKLK VKKQDRIFPP
ETSAPVVATP PPSTASVPAA GNSSASADKP LSNMKILTLG KLSRNKDEVK AMIEKLGGKL
TGTANKASLC ISTKKEVEKM NKKMEEVKEA NIRVVSEDFL QDVSASTKSL QELFLAHILS
PWGAEVKAEP VEVVAPKGKS GAALSKKSKG QVKEEGINKS EKRMKLTLKG GAAVDPDSGL
EHSAHVLEKG GKVFSATLGL VDIVKGTNSY YKLQLLEDDK ESRYWIFRSW GRVGTVIGSN
KLEQMPSKED AIEHFVKLYE EKTGNAWHSK NFTKYPKKFY PLEIDYGQDE EAVKKLTVNP
GTKSKLPKPV QDLIKLIFDV ESMKKAMVEY EIDLQKMPLG KLSKRQIQAA YSILSEVQQA
VSQGSSDSQI LDLSNRFYTL IPHDFGMKKP PLLNSADSVQ AKVEMLDNLL DIEVAYSLLR
GGSDDSSKDP IDVNYEKLKT DIKVVGRDSE EAEIIRKYVK NTHATTHNAY DLEVIDIFKI
EREGECQRYK PFKQLHNRRL LWHGSRTTNF AGILSQGLRI APPEAPVTGY MFGKGIYFAD
MVSKSANYCH TSQGDPIGLI VLGEVALGNM YELKHASHIS KLPKGKHSVK GLGKTTPDPS
ASISLDGVEV PLGTGISSGV NDTCLLYNEY IVYDIAQVNL KYLLKLKFNF KTSLW
//
