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Reviewed, UniProtKB/Swiss-Prot Q11208 (PARP_SARPE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Poly [ADP-ribose] polymerase
      Short name=PARP
    EC=2.4.2.30
Alternative name(s):
    ADPRT
    NAD(+) ADP-ribosyltransferase
    Poly[ADP-ribose] synthetase
OrganismSarcophaga peregrina (Flesh fly) (Boettcherisca peregrina)
Taxonomic identifier7386 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Oestroidea › Sarcophagidae › Sarcophaga › Boettcherisca

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Protein attributes

Sequence length996 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage.

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.

Subcellular location

Nucleus.

Miscellaneous

The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 PARP-type zinc fingers.

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Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processprotein amino acid ADP-ribosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD or NADH binding

Inferred from electronic annotation. Source: InterPro

NAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 996996Poly [ADP-ribose] polymerase
PRO_0000211326

Regions

Domain382 – 47392BRCT
Domain647 – 764118PARP alpha-helical
Domain773 – 996224PARP catalytic
DNA binding1 – 369369 By similarity
Zinc finger7 – 8983PARP-type 1
Zinc finger114 – 20390PARP-type 2
Region370 – 507138Automodification domain
Motif211 – 2144Nuclear localization signal
Motif232 – 2354Nuclear localization signal

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Sequences

Sequence LengthMass (Da)Tools
Q11208-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 690DDD36E7487298

FASTA996113,019
        10         20         30         40         50         60 
MEIDLPFKVE YSKSSRASCK GCKNKIEAGI LRIAAMVQSA FHDGKQPNWF HEQCFFQKQR 

        70         80         90        100        110        120 
PTSAGDIENF ENIRFEDQER IKKAIDNCTT VISAGGSKKG AKRSKGENNA IKDFGIEYAK 

       130        140        150        160        170        180 
SGRASCRGCE QKILKDQIRI RKTVFDTEVG MKYGGQPLWH HVECFAQLRG ELGWLDTGEN 

       190        200        210        220        230        240 
LPGFQTLKSD DKADVKKALP VIKDEGVSSA KKAKIEKIDE EDAASIKELT EKIKKQSKRL 

       250        260        270        280        290        300 
FKFRDEIKNE MSKDDMVALL EANNMEPVKG DSEKLLDQVA DLLTFGALLP CTDCKGRQLL 

       310        320        330        340        350        360 
FHKSGYLCNG DLTEWTKCTK LLKEPERKSC KIPGYLKYKF LKDVRKNPEV RAIRYIPPST 

       370        380        390        400        410        420 
STILKNISLK KGDELDGPKV KRERPPLYNI EIALIAPKER EGIVKDRISK LGGTVSTKIT 

       430        440        450        460        470        480 
EKTTVVLSTP EEVERMSSRM KKAKTLGLHV IPEDYLEAVE QNGAGAINYI SSMSLCDWGT 

       490        500        510        520        530        540 
DPATRITQEE SKSSKSKSIY TKSVPKSMTL KIKDGLAVDP DSGLEDVAHV YVSRNKEKYN 

       550        560        570        580        590        600 
VVLGITDIQK NKNSFYKLQL LESDMKNRFW VFRSWGRIGT TIGGNKLDNF SNLVDAIVQF 

       610        620        630        640        650        660 
KELYLEKSGN HFENRENFVK VAGRMYPIDI DYAEDSKIDL SAEHDIKSKL PLSVQDIIKL 

       670        680        690        700        710        720 
MFDVDSMKRT MMEFDLDMEK MPLGKLSQKQ IQSAYKVLTE IYELIQGGGT NAKFIDATNR 

       730        740        750        760        770        780 
FYTLIPHNFG TQSPPLLDTT EQVEQLRQML DSLIEIECAY SLLQTEDSKA DINPIDKHYE 

       790        800        810        820        830        840 
QLKTKLEPLD KNSEEYILLQ KYVKNTHAET HKLYDLEVVD IFKVARQGEA RRYKPFKKLH 

       850        860        870        880        890        900 
NRRLLWHGSR LTNFAGILSH GLKIAPPEAP VTGYMFGKGI YFADMVSKSA NYCCTSHHNS 

       910        920        930        940        950        960 
TGLMLLSEVA LGDMMECTAA KYVTKLPNDK HSCFGRGRTM PNPSESIIRE DGVEIPLGKP 

       970        980        990 
ITNDSLKSSL LYNEFIIYDI AQVNIQYMLR MNFKYK

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References

[1]"Cloning and functional expression of poly(ADP-ribose) polymerase cDNA from Sarcophaga peregrina."
Masutani M., Nozaki T., Hitomi Y., Ikejima M., Nagasaki K., de Prati A.C., Kurata S., Natori S., Sugimura T., Esumi H.
Eur. J. Biochem. 220:607-614(1994) [PubMed: 8125121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

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Cross-references

Sequence databases

D16482 mRNA. Translation: BAA03943.1.
PIRS42208.

3D structure databases

HSSPHSSP built from PDB template 1A26 based on UniProtKB P26446.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.4.2.30. 67068.

Family and domain databases

InterProIPR001357. BRCT.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. PARP_catalytic.
IPR004102. PARP_reg.
IPR008893. WGR.
IPR001510. Znf_PARP.
[Graphical view]
Gene3DG3DSA:1.20.142.10. PARP_reg. 1 hit.
G3DSA:3.30.1740.10. Znf_PARP. 2 hits.
PfamPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFPIRSF000489. NAD_ADPRT. 1 hit.
ProDomPD004675. Znf_PolyADPpol. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
PROSITEPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 1 hit.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePARP_SARPE
AccessionPrimary (citable) accession number: Q11208
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents