Reviewed, UniProtKB/Swiss-Prot Q09525 (PME2_CAEEL)

Names and origin

Protein names

Recommended name:
    Poly(ADP-ribose) polymerase pme-2
    EC=2.4.2.30
Alternative name(s):
    Poly ADP-ribose metabolism enzyme 2

Gene names

Name:	pme-2
ORF Names:	E02H1.4

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death.
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subcellular location	Nucleus Probable.
Developmental stage	Predominantly expressed at early embryonic stages and later in L4 and adult stages.
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Ligand	NAD
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid ADP-ribosylation Inferred from electronic annotation. Source: InterPro reproduction Inferred from mutant phenotype. Source: WormBase
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD+ ADP-ribosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 538	538	Poly(ADP-ribose) polymerase pme-2		PRO_0000211336
Regions
	Domain	148 – 285	138	PARP alpha-helical
	Domain	309 – 535	227	PARP catalytic

Sequences

	Sequence		Length	Mass (Da)
	Q09525-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 3144E25465FC7341	FASTA	538	61,268
	10 20 30 40 50 60 MSIINDENGR GYKVHLCKTN IAQNNNKFYD MELLDEGGDF IVKLINGRIG YRGVTQLKDF 70 80 90 100 110 120 DDLDRAKKFF ESKFYEKTHL HWEERDDEPV PNKYAVVELA TNARQTEKEV KKEEPEPEPK 130 140 150 160 170 180 VDEKNTRGRK KRGIVKEKKE IKKEEEPVEE VNEKLKELMK CICDEDVHLG LLKQLKFNEA 190 200 210 220 230 240 FGRPIDCLSL AQLTTGYEIL SKIEESIGGK SARRSTRGRP RVADRVLAVK SDGPSLHDIN 250 260 270 280 290 300 KYYSLIPHSF GFCVPPKIDS HAKIQAEREL LDALKGSIEA SLELKDLKKT ASSKDIYQRL 310 320 330 340 350 360 YERLPCHLEP VSEEIAGKIG DCLAMRGPTH CYKLSLIDAF ELKDPNEIPT EAPVEVQEVP 370 380 390 400 410 420 KKRGRKSTKT AAPTVPPPTT KRLLWHGTRV TNVFSILMNG LQFPVGDRCG LMFGNGVYFA 430 440 450 460 470 480 NVPTKSANYC CPEASKRVFM LLCEVETANP LVLYESEIDA DEKMEKAKKT SVYAAGKHTP 490 500 510 520 530 RDTVEINGIP AFKSNLETIE EETRLLYDEY VMFNKEHFKI KYVVEVKVDR LTAKEMMA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in Caenorhabditis elegans." Gagnon S.N., Hengartner M.O., Desnoyers S. Biochem. J. 368:263-271(2002) [PubMed: 12145714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF500111 mRNA. Translation: AAM27196.1. Z47075 Genomic DNA. Translation: CAA87379.1.
PIR	T20414.
RefSeq	NP_001022057.1.
UniGene	Cel.18275
3D structure databases
HSSP	HSSP built from PDB template 1GS0 based on UniProtKB O88554.
ModBase	Search...
Genome annotation databases
Ensembl	E02H1.4; E02H1.4; E02H1.4; Caenorhabditis elegans. [Genome view]
GeneID	3565967.
KEGG	cel:E02H1.4.
NMPDR	fig|6239.3.peg.6966.
UCSC	E02H1.4. c. elegans.
Organism-specific databases
CTD	3565967.
WormBase	WBGene00004050. pme-2.
WormPep	E02H1.4. CE01539. [WorfDB]
Phylogenomic databases
OMA	FGKGIYL.
Enzyme and pathway databases
BRENDA	2.4.2.30. 672.
Gene expression databases
ArrayExpress	Q09525.
Family and domain databases
InterPro	IPR012317. PARP_catalytic. IPR004102. PARP_reg. IPR008893. WGR. [Graphical view]
Gene3D	G3DSA:1.20.142.10. PARP_reg. 1 hit.
Pfam	PF00644. PARP. 1 hit. PF02877. PARP_reg. 1 hit. PF05406. WGR. 1 hit. [Graphical view]
SMART	SM00773. WGR. 1 hit. [Graphical view]
PROSITE	PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	958561.

Entry information

Entry name

PME2_CAEEL

Accession

Primary (citable) accession number: Q09525

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 3, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project