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Reviewed, UniProtKB/Swiss-Prot Q9FK91 (PARP3_ARATH)

Last modified October 13, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3
      Short name=PARP-3
    EC=2.4.2.30
Alternative name(s):
    ADPRT 3
    NAD(+) ADP-ribosyltransferase 3
    Poly[ADP-ribose] synthetase 3
Gene names
Name: PARP3
Ordered Locus Names: At5g22470
ORF Names: MQJ16_1
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks By similarity.

Catalytic activity

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

Subcellular location

Nucleus Potential.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 TPR repeats.

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Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
TPR repeat
   LigandNAD
   Molecular functionGlycosyltransferase
Transferase
   PTMADP-ribosylation
   Technical termComplete proteome
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 functionNAD+ ADP-ribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Poly [ADP-ribose] polymerase 3
PRO_0000260498

Regions

Domain183 – 27593BRCT
Repeat183 – 21634TPR 1
Repeat278 – 31134TPR 2
Domain450 – 569120PARP alpha-helical
Domain578 – 809232PARP catalytic

Experimental info

Sequence conflict4451G → V in BAC42749. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9FK91-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 4B1B602057D46B60

FASTA81591,534
        10         20         30         40         50         60 
MKVHETRSHA HMSGDEQKKG NLRKHKAEGK LPESEQSQKK AKPENDDGRS VNGAGDAASE 

        70         80         90        100        110        120 
YNEFCKAVEE NLSIDQIKEV LEINGQDCSA PEETLLAQCQ DLLFYGALAK CPLCGGTLIC 

       130        140        150        160        170        180 
DNEKRFVCGG EISEWCSCVF STKDPPRKEE PVKIPDSVMN SAISDLIKKH QDPKSRPKRE 

       190        200        210        220        230        240 
LGSADKPFVG MMISLMGRLT RTHQYWKKKI ERNGGKVSNT VQGVTCLVVS PAERERGGTS 

       250        260        270        280        290        300 
KMVEAMEQGL PVVSEAWLID SVEKHEAQPL EAYDVVSDLS VEGKGIPWDK QDPSEEAIES 

       310        320        330        340        350        360 
FSAELKMYGK RGVYMDTKLQ ERGGKIFEKD GLLYNCAFSI CDLGKGRNEY CIMQLVTVPD 

       370        380        390        400        410        420 
SNLNMYFKRG KVGDDPNAEE RLEEWEDEEA AIKEFARLFE EIAGNEFEPW EREKKIQKKP 

       430        440        450        460        470        480 
HKFFPIDMDD GIEVRSGALG LRQLGIASAH CKLDSFVANF IKVLCGQEIY NYALMELGLD 

       490        500        510        520        530        540 
PPDLPMGMLT DIHLKRCEEV LLEFVEKVKT TKETGQKAEA MWADFSSRWF SLMHSTRPMR 

       550        560        570        580        590        600 
LHDVNELADH AASAFETVRD INTASRLIGD MRGDTLDDPL SDRYKKLGCK ISVVDKESED 

       610        620        630        640        650        660 
YKMVVKYLET TYEPVKVSDV EYGVSVQNVF AVESDAIPSL DDIKKLPNKV LLWCGSRSSN 

       670        680        690        700        710        720 
LLRHIYKGFL PAVCSLPVPG YMFGRAIVCS DAAAEAARYG FTAVDRPEGF LVLAVASLGE 

       730        740        750        760        770        780 
EVTEFTSPPE DTKTLEDKKI GVKGLGRKKT EESEHFMWRD DIKVPCGRLV PSEHKDSPLE 

       790        800        810 
YNEYAVYDPK QTSIRFLVEV KYEEKGTEIV DVEPE

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References

[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed: 9734815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-815.
Strain: cv. Columbia.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB012244 Genomic DNA. Translation: BAB09119.1.
AK118123 mRNA. Translation: BAC42749.1.
IPIIPI00532124.

3D structure databases

HSSPHSSP built from PDB template 1GS0 based on UniProtKB O88554.
ModBaseSearch...

Proteomic databases

PRIDEQ9FK91.

Genome annotation databases

GenomeReviewsGene locus AT5G22470 in contig BA000015_GR.
NMPDRfig|3702.1.peg.24407.

Organism-specific databases

GeneFarm4816. 467.
TAIRAt5g22470.

Enzyme and pathway databases

BRENDA2.4.2.30. 302.

Gene expression databases

GenevestigatorQ9FK91.
GermOnlineAT5G22470. Arabidopsis thaliana.

Family and domain databases

InterProIPR001357. BRCT.
IPR012982. PADR1.
IPR012317. PARP_catalytic.
IPR004102. PARP_reg.
IPR008893. WGR.
[Graphical view]
Gene3DG3DSA:1.20.142.10. PARP_reg. 1 hit.
PfamPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
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.
PS50005. TPR. False negative.
PS50293. TPR_REGION. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePARP3_ARATH
AccessionPrimary (citable) accession number: Q9FK91
Secondary accession number(s): Q8GXP3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: March 1, 2001
Last modified: October 13, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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