Poly(ADP-ribose) polymerase pme-1 - Caenorhabditis elegans

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Reviewed, UniProtKB/Swiss-Prot Q9N4H4 (PME1_CAEEL)

Last modified February 9, 2010. Version 62. History...

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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 names

Recommended name:
    Poly(ADP-ribose) polymerase pme-1
    EC=2.4.2.30
Alternative name(s):
    Poly ADP-ribose metabolism enzyme 1

Gene names

Name:	pme-1
ORF Names:	Y71F9AL.18

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	945 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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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. Involved in protection of the genome against mutations, probably via some participation in DNA repair. Ref.3
Catalytic activity	NAD⁺ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. Ref.1
Subcellular location	Nucleus Probable.
Developmental stage	Predominantly expressed at early embryonic stages and later in L4 and adult stages. Ref.1
Sequence similarities	Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain. Contains 1 PARP-type zinc finger.

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Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding NAD Zinc
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW growth Inferred from mutant phenotype. Source: WormBase hermaphrodite genitalia development Inferred from mutant phenotype. Source: WormBase inductive cell migration Inferred from mutant phenotype. Source: WormBase morphogenesis of an epithelium Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase positive regulation of growth rate Inferred from mutant phenotype. Source: WormBase protein amino acid ADP-ribosylation Inferred from electronic annotation. Source: InterPro receptor-mediated endocytosis Inferred from mutant phenotype. Source: WormBase
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 945

945

Poly(ADP-ribose) polymerase pme-1

PRO_0000211335

Regions

Domain

586 – 704

119

PARP alpha-helical

Domain

717 – 945

229

PARP catalytic

Zinc finger

10 – 96

PARP-type

Experimental info

Sequence conflict

152 – 153

FK → LN in AAM27195. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9N4H4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1D0A62C954BC6AD9
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FASTA

945

108,007

        10         20         30         40         50         60 
MIHSNEPLPY AIEYAKSGRS NCKTCKKNIA LDQLRMSMNR PSTFFDGNMD SWFHYNCFWI 

        70         80         90        100        110        120 
KMIRGRDDIN ISSIRGVDWL RWEDQEKLRQ EIQHFKTASP PTLTPLCSTT TVILSTIKTE 

       130        140        150        160        170        180 
KSLSNRGKCG KCGQNFERGE IKAHNKGKAN HFKCFLQEFD KISGTVEDIP GWADYEENFK 

       190        200        210        220        230        240 
IKAVGEYVEA LAAKRRSTEP ATPASASPTP PEAETPVLSA EGSPESSNKR PASSEIIEID 

       250        260        270        280        290        300 
GEGNPDENDF AKKRRMKKEA RLMEVQKKRM KKQSDLLWEY RQIFERMPYT DKISILRENE 

       310        320        330        340        350        360 
QDIPEGHDPT AQVIERLVDN ALFGCPIICQ TCSNGKIVYN SSCRTYVCTG YATEYSKCTY 

       370        380        390        400        410        420 
ESKNPIRTPF EVSHRLTEKH KLQDIVFNQM SERLYIGEED GESVVKIDKR KSKGGTRGEQ 

       430        440        450        460        470        480 
FIYAAEAFDS TNNVPIKVGD LTSTNTHIIK KGTVVDAKFA LADRCHVFKN EIDGSLYQAT 

       490        500        510        520        530        540 
LSFTDLTQNK NSYYKIQLLK DDQRENYYVF RSWGRVGTEV GGNKHESYSN SNEAILKFQD 

       550        560        570        580        590        600 
VFHEKTKNDW IYRKHFRKMP GMFSYVETDY SEFAQITDTE ITPGSKTLLP KSVKEVVMSI 

       610        620        630        640        650        660 
FDVENMKSAL KSFEMDVNKM PLGRLSHNQI NLAFEVLNDI SDLLVKLPID ASRILDFSNK 

       670        680        690        700        710        720 
FYTIIPHNFG MRVPEPIDSF HKIKEKNNML NALLDIKFAY DQISGGDVPA STSLGIDPVD 

       730        740        750        760        770        780 
INYQKLKCIM EPLQQGCDDW NMIHQYLKNT HGATHDLKVE LIDILKLNRD NESSKFKRHI 

       790        800        810        820        830        840 
GNRRLLWHGS GKMNFAGILG QGLRIAPPEA PVSGYMFGKG VYFADMFSKS FFYCRANAKE 

       850        860        870        880        890        900 
EAYLLLCDVA LGNVQQLMAS KNVSRQTLPA GFQSVQGLGR QCPREIGSYN HPDGYTIPLG 

       910        920        930        940 
LTYMQLQGKQ DVDYHLLYNE FIVYDVDQIQ LKYLVRVKMH HARHL

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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], ENZYME ACTIVITY, DEVELOPMENTAL STAGE.
[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.
[3]	"Identification of genes that protect the C. elegans genome against mutations by genome-wide RNAi." Pothof J., van Haaften G., Thijssen K., Kamath R.S., Fraser A.G., Ahringer J., Plasterk R.H.A., Tijsterman M. Genes Dev. 17:443-448(2003) [PubMed: 12600937] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF499444 mRNA. Translation: AAM27195.1. AC024200 Genomic DNA. Translation: AAF36011.1.
RefSeq	NP_491072.1.
UniGene	Cel.1174
3D structure databases
SMR	Q9N4H4. Positions 4-96, 117-210, 267-378, 443-572.
ModBase	Search...
Genome annotation databases
Ensembl	Y71F9AL.18.1; Y71F9AL.18.1; Y71F9AL.18; Caenorhabditis elegans. [Genome view] Y71F9AL.18.2; Y71F9AL.18.2; Y71F9AL.18; Caenorhabditis elegans. [Genome view]
GeneID	266823.
KEGG	cel:Y71F9AL.18.
NMPDR	fig\|6239.3.peg.533.
UCSC	Y71F9AL.18.1. c. elegans.
Organism-specific databases
CTD	266823.
WormBase	WBGene00004049. pme-1.
WormPep	Y71F9AL.18. CE25556. [WorfDB]
Phylogenomic databases
eggNOG	meNOG05666.
HOGENOM	HBG356841.
InParanoid	Q9N4H4.
OMA	DWLRWED.
PhylomeDB	Q9N4H4.
Enzyme and pathway databases
BRENDA	2.4.2.30. 672.
Gene expression databases
ArrayExpress	Q9N4H4.
Family and domain databases
InterPro	IPR008288. NAD_ADPRT. IPR012982. PADR1. IPR012317. Poly(ADP-ribose)pol_cat_dom. IPR004102. Poly(ADP-ribose)pol_reg_dom. IPR008893. WGR. IPR001510. Znf_PARP. [Graphical view]
Gene3D	G3DSA:1.20.142.10. PARP_reg. 1 hit. G3DSA:3.30.1740.10. Znf_PARP. 1 hit.
Pfam	PF08063. PADR1. 1 hit. PF00644. PARP. 1 hit. PF02877. PARP_reg. 1 hit. PF05406. WGR. 1 hit. PF00645. zf-PARP. 1 hit. [Graphical view]
PIRSF	PIRSF000489. NAD_ADPRT. 1 hit.
SMART	SM00773. WGR. 1 hit. [Graphical view]
PROSITE	PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. PS00347. PARP_ZN_FINGER_1. 1 hit. PS50064. PARP_ZN_FINGER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	953164.

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Entry information

Entry name

PME1_CAEEL

Accession

Primary (citable) accession number: Q9N4H4
Secondary accession number(s): Q8MZU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project

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Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents