PARP_SARPE
ID PARP_SARPE Reviewed; 996 AA.
AC Q11208;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Poly [ADP-ribose] polymerase;
DE Short=PARP;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase;
DE Short=ADPRT;
DE AltName: Full=Poly[ADP-ribose] synthase;
DE AltName: Full=Protein ADP-ribosyltransferase {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
OS Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Sarcophagidae; Sarcophaga; Boettcherisca.
OX NCBI_TaxID=7386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8125121; DOI=10.1111/j.1432-1033.1994.tb18662.x;
RA Masutani M., Nozaki T., Hitomi Y., Ikejima M., Nagasaki K., de Prati A.C.,
RA Kurata S., Natori S., Sugimura T., Esumi H.;
RT "Cloning and functional expression of poly(ADP-ribose) polymerase cDNA from
RT Sarcophaga peregrina.";
RL Eur. J. Biochem. 220:607-614(1994).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair. Mainly
CC mediates glutamate and aspartate ADP-ribosylation of target proteins:
CC the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor
CC carboxyl group of glutamate and aspartate residues and further ADP-
CC ribosyl groups are transferred to the 2'-position of the terminal
CC adenosine moiety, building up a polymer with an average chain length of
CC 20-30 units. {ECO:0000250|UniProtKB:P09874}.
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:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: The ADP-D-ribosyl group of NAD(+) is transferred to an
CC acceptor carboxyl group on a histone or the enzyme itself, and further
CC ADP-ribosyl groups are transferred to the 2'-position of the terminal
CC adenosine moiety, building up a polymer with an average chain length of
CC 20-30 units.
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DR EMBL; D16482; BAA03943.1; -; mRNA.
DR PIR; S42208; S42208.
DR AlphaFoldDB; Q11208; -.
DR SMR; Q11208; -.
DR PRIDE; Q11208; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
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 Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 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; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 1.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Direct protein sequencing; DNA-binding;
KW Glycosyltransferase; Metal-binding; NAD; Nucleotidyltransferase; Nucleus;
KW Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..996
FT /note="Poly [ADP-ribose] polymerase"
FT /id="PRO_0000211326"
FT DOMAIN 382..473
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 527..625
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 647..764
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 773..996
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DNA_BIND 1..369
FT /evidence="ECO:0000250"
FT ZN_FING 7..89
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 114..203
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 370..507
FT /note="Automodification domain"
FT MOTIF 211..214
FT /note="Nuclear localization signal"
FT MOTIF 232..235
FT /note="Nuclear localization signal"
SQ SEQUENCE 996 AA; 113019 MW; 690DDD36E7487298 CRC64;
MEIDLPFKVE YSKSSRASCK GCKNKIEAGI LRIAAMVQSA FHDGKQPNWF HEQCFFQKQR
PTSAGDIENF ENIRFEDQER IKKAIDNCTT VISAGGSKKG AKRSKGENNA IKDFGIEYAK
SGRASCRGCE QKILKDQIRI RKTVFDTEVG MKYGGQPLWH HVECFAQLRG ELGWLDTGEN
LPGFQTLKSD DKADVKKALP VIKDEGVSSA KKAKIEKIDE EDAASIKELT EKIKKQSKRL
FKFRDEIKNE MSKDDMVALL EANNMEPVKG DSEKLLDQVA DLLTFGALLP CTDCKGRQLL
FHKSGYLCNG DLTEWTKCTK LLKEPERKSC KIPGYLKYKF LKDVRKNPEV RAIRYIPPST
STILKNISLK KGDELDGPKV KRERPPLYNI EIALIAPKER EGIVKDRISK LGGTVSTKIT
EKTTVVLSTP EEVERMSSRM KKAKTLGLHV IPEDYLEAVE QNGAGAINYI SSMSLCDWGT
DPATRITQEE SKSSKSKSIY TKSVPKSMTL KIKDGLAVDP DSGLEDVAHV YVSRNKEKYN
VVLGITDIQK NKNSFYKLQL LESDMKNRFW VFRSWGRIGT TIGGNKLDNF SNLVDAIVQF
KELYLEKSGN HFENRENFVK VAGRMYPIDI DYAEDSKIDL SAEHDIKSKL PLSVQDIIKL
MFDVDSMKRT MMEFDLDMEK MPLGKLSQKQ IQSAYKVLTE IYELIQGGGT NAKFIDATNR
FYTLIPHNFG TQSPPLLDTT EQVEQLRQML DSLIEIECAY SLLQTEDSKA DINPIDKHYE
QLKTKLEPLD KNSEEYILLQ KYVKNTHAET HKLYDLEVVD IFKVARQGEA RRYKPFKKLH
NRRLLWHGSR LTNFAGILSH GLKIAPPEAP VTGYMFGKGI YFADMVSKSA NYCCTSHHNS
TGLMLLSEVA LGDMMECTAA KYVTKLPNDK HSCFGRGRTM PNPSESIIRE DGVEIPLGKP
ITNDSLKSSL LYNEFIIYDI AQVNIQYMLR MNFKYK
