Reviewed, UniProtKB/Swiss-Prot O77460 (IPYR_DROME)

Names and origin

Protein names

Recommended name:
    Inorganic pyrophosphatase
    EC=3.6.1.1
Alternative name(s):
    Pyrophosphate phospho-hydrolase
      Short name=PPase
    Nucleosome-remodeling factor 38 kDa subunit

Gene names

Name:	Nurf-38
ORF Names:	CG4634

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

General annotation (Comments)

Function	Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorphosis. Nurf-38 may have adapted to deliver pyrophosphatase to chromatin to assist in replication or transcription by efficient removal of the inhibitory metabolite. Ref.1 Ref.5
Catalytic activity	Diphosphate + H2O = 2 phosphate.
Cofactor	Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity.
Subunit structure	Component of the NURF complex composed of Caf1, E(bx), Nurf-38 and Iswi.
Subcellular location	Cytoplasm. Nucleus.
Miscellaneous	The ATPase activity of NURF is stimulated by the presence of nucleosomes rather than by free DNA.
Sequence similarities	Belongs to the PPase family.
Sequence caution	The sequence AAL68291.1 differs from that shown. Reason: Frameshift at position 18.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Chromatin regulator Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ecdysone receptor-mediated signaling pathway Inferred from genetic interaction. Source: FlyBase nucleosome mobilization Inferred from direct assay. Source: FlyBase phosphate metabolic process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from direct assay. Source: FlyBase
Cellular component	NURF complex Ref.1 Inferred from direct assay. Source: FlyBase cytoplasm Ref.1 Inferred from direct assay. Source: FlyBase
Molecular function	inorganic diphosphatase activity Ref.1 Inferred from direct assay. Source: FlyBase magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VYT2	1	EBI-96355,EBI-173211

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	Inorganic pyrophosphatase		PRO_0000137572
Sites
	Metal binding	166	1	Magnesium 1 By similarity
	Metal binding	171	1	Magnesium 1 By similarity
	Metal binding	171	1	Magnesium 2 By similarity
	Metal binding	203	1	Magnesium 1 By similarity
	Binding site	129	1	Inorganic pyrophosphate By similarity
Experimental info
	Mutagenesis	129	1	R → A: Drastic reduction of activity. Ref.1
	Sequence conflict	193 – 194	2	TI → QF in AAC97111. Ref.1
	Sequence conflict	193 – 194	2	TI → QF in AAC97112. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O77460-1 [UniParc]. Last modified August 31, 2004. Version 3. Checksum: B4B7341CD5A3E5F2	FASTA	338	37,939
	10 20 30 40 50 60 MLAKITRSSF YASRAVGRLS GSIPTSPAAL ASNCRYIQIE RKRTKSHEMA LYETVEKGAK 70 80 90 100 110 120 NSPSYSLYFK NKCGNVISPM HDIPLYANEE KTIYNMVVEV PRWTNAKMEI SLKTPMNPIK 130 140 150 160 170 180 QDIKKGKLRF VANCFPHKGY IWNYGALPQT WENPDHIEPS TGCKGDNDPI DVIEIGYRVA 190 200 210 220 230 240 KRGDVLKVKV LGTIALIDEG ETDWKIIAID VNDPLASKVN DIADVDQYFP GLLRATVEWF 250 260 270 280 290 300 KIYKIPDGKP ENQFAFNGDA KNADFANTII AETHKFWQNL VHQSPASGSI STTNITNRNS 310 320 330 EHVIPKEEAE KILAEAPDGG QVEEVSDTVD TWHFIHLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex." Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C. Genes Dev. 12:3206-3216(1998) [PubMed: 9784495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, MUTAGENESIS OF ARG-129.
[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]	"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]. Strain: Berkeley. Tissue: Embryo.
[5]	"Purification and properties of an ATP-dependent nucleosome remodeling factor." Tsukiyama T., Wu C. Cell 83:1011-1020(1995) [PubMed: 8521501] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF085600 Genomic DNA. Translation: AAC97111.1. Different initiation. AF085601 mRNA. Translation: AAC97112.1. AE013599 Genomic DNA. Translation: AAF47227.2. AY075479 mRNA. Translation: AAL68291.1. Frameshift.
RefSeq	NP_523849.3.
UniGene	Dm.1958
3D structure databases
HSSP	HSSP built from PDB template 1WGI based on UniProtKB P00817.
ModBase	Search...
Protein-protein interaction databases
IntAct	O77460. 12 interactions.
Genome annotation databases
Ensembl	FBgn0016687. Drosophila melanogaster. [Contig view]
GeneID	37922.
KEGG	dme:Dmel_CG4634.
NMPDR	fig|7227.3.peg.7338.
Organism-specific databases
FlyBase	FBgn0016687. Nurf-38.
Phylogenomic databases
HOGENOM	O77460.
OMA	O77460. TWEDPKH.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-006495-MON.
BRENDA	3.6.1.1. 48.
Gene expression databases
ArrayExpress	O77460.
GermOnline	CG4634. Drosophila melanogaster.
Family and domain databases
InterPro	IPR008162. Pyrophosphatase. [Graphical view]
Gene3D	G3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
PANTHER	PTHR10286. Pyrophosphatase. 1 hit.
Pfam	PF00719. Pyrophosphatase. 1 hit. [Graphical view]
ProDom	PD002014. Inorg_pphsph. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00387. PPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	806063.

Entry information

Entry name

IPYR_DROME

Accession

Primary (citable) accession number: O77460
Secondary accession number(s): Q9W150

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 31, 2004
Last modified:	June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project