Reviewed, UniProtKB/Swiss-Prot O46043 (PARG_DROME)

Names and origin

Protein names

Recommended name:
    Poly(ADP-ribose) glycohydrolase
    EC=3.2.1.143

Gene names

Name:	Parg
ORF Names:	CG2864

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	768 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism is required for maintenance of the normal function of neuronal cells. Ref.6 UniProtKB Q86W56
Catalytic activity	Hydrolyzes poly(ADP-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose. UniProtKB Q86W56
Disruption phenotype	Progressive neurodegeneration. Ref.6
Sequence similarities	Belongs to the poly(ADP-ribose) glycohydrolase family.

Ontologies

Keywords
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.6 Inferred from mutant phenotype. Source: UniProtKB chromatin silencing Inferred from mutant phenotype. Source: FlyBase maintenance of protein location in nucleus Inferred from mutant phenotype. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase regulation of RNA splicing Inferred from mutant phenotype. Source: FlyBase regulation of histone acetylation Inferred from mutant phenotype. Source: FlyBase response to heat Inferred from mutant phenotype. Source: FlyBase
Cellular component	nucleoplasm Inferred from direct assay. Source: FlyBase
Molecular function	poly(ADP-ribose) glycohydrolase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q961B9	1	EBI-145677,EBI-102715

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 768	768	Poly(ADP-ribose) glycohydrolase		PRO_0000066607
Amino acid modifications
	Modified residue	69	1	Phosphoserine Ref.7
	Modified residue	73	1	Phosphoserine Ref.7
	Modified residue	624	1	Phosphoserine Ref.7
	Modified residue	627	1	Phosphoserine Ref.7
	Modified residue	628	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O46043-1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: 2E620C42E643FC04	FASTA	768	86,288
	10 20 30 40 50 60 MQEFRSHLIF PIFQKVYQST ANRRRASASV LTNRLGKALC LNCARMSKSP DGGISEIETE 70 80 90 100 110 120 EEPENLANSL DDSWRGVSME AIHRNRQPFE LENLPPVTAG NLHRVMYQLP IRETPPRPYK 130 140 150 160 170 180 SPGKWDSEHV RLPCAPESKY PRENPDGSTT IDFRWEMIER ALLQPIKTCE ELQAAIISYN 190 200 210 220 230 240 TTYRDQWHFR ALHQLLDEEL DESETRVFFE DLLPRIIRLA LRLPDLIQSP VPLLKHHKNA 250 260 270 280 290 300 SLSLSQQQIS CLLANAFLCT FPRRNTLKRK SEYSTFPDIN FNRLYQSTGP AVLEKLKCIM 310 320 330 340 350 360 HYFRRVCPTE RDASNVPTGV VTFVRRSGLP EHLIDWSQSA APLGDVPLHV DAEGTIEDEG 370 380 390 400 410 420 IGLLQVDFAN KYLGGGVLGH GCVQEEIRFV ICPELLVGKL FTECLRPFEA LVMLGAERYS 430 440 450 460 470 480 NYTGYAGSFE WSGNFEDSTP RDSSGRRQTA IVAIDALHFA QSHHQYREDL MERELNKAYI 490 500 510 520 530 540 GFVHWMVTPP PGVATGNWGC GAFGGDSYLK ALLQLMVCAQ LGRPLAYYTF GNVEFRDDFH 550 560 570 580 590 600 EMWLLFRNDG TTVQQLWSIL RSYSRLIKEK SSKEPRENKA SKKKLYDFIK EELKKVRDVP 610 620 630 640 650 660 GEGASAEAGS SRVAGLGEGK SETSAKSSPE LNKQPARPQI TITQQSTDLL PAQLSQDNSN 670 680 690 700 710 720 SSEDQALLML SDDEEANAMM EAASLEAKSS VEISNSSTTS KTSSTATKSM GSGGRQLSLL 730 740 750 760 EMLDTHYEKG SASKRPRKSP NCSKAEGSAK SRKEIDVTDK DEKDDIVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the cDNA encoding Drosophila poly(ADP-ribose) glycohydrolase." Ame J.-C., Jacobson M.K. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed: 10731137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-768. Strain: Berkeley. Tissue: Embryo.
[6]	"Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster." Hanai S., Kanai M., Ohashi S., Okamoto K., Yamada M., Takahashi H., Miwa M. Proc. Natl. Acad. Sci. U.S.A. 101:82-86(2004) [PubMed: 14676324] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-73; SER-624; SER-627 AND SER-628, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF079556 mRNA. Translation: AAC28734.1. AE014298 Genomic DNA. Translation: AAF45886.1. Z98254 Genomic DNA. Translation: CAB10913.1. Different initiation. AY051955 mRNA. Translation: AAK93379.1. Different initiation.
RefSeq	NP_477321.1.
UniGene	Dm.2967
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O46043. 1 interaction.
STRING	O46043.
Genome annotation databases
Ensembl	FBtr0070585; FBpp0070560; FBgn0023216; Drosophila melanogaster. [Genome view]
GeneID	31329.
KEGG	dme:Dmel_CG2864.
NMPDR	fig|7227.3.peg.16388.
Organism-specific databases
CTD	31329.
FlyBase	FBgn0023216. Parg.
Phylogenomic databases
OMA	TFPRRNT.
Enzyme and pathway databases
BRENDA	3.2.1.143. 48.
Gene expression databases
Bgee	O46043.
GermOnline	CG2864. Drosophila melanogaster.
Family and domain databases
InterPro	IPR007724. Poly_GlycHdrlase. [Graphical view]
PANTHER	PTHR12837. Poly_glchydro. 1 hit.
Pfam	PF05028. PARG_cat. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	773078.

Entry information

Entry name

PARG_DROME

Accession

Primary (citable) accession number: O46043
Secondary accession number(s): Q960N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project