IPYR_DROME
ID IPYR_DROME Reviewed; 338 AA.
AC O77460; Q9W150;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1 {ECO:0000269|PubMed:9784495};
DE AltName: Full=Nucleosome-remodeling factor 38 kDa subunit;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=Nurf-38; ORFNames=CG4634;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-129.
RX PubMed=9784495; DOI=10.1101/gad.12.20.3206;
RA Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.;
RT "Inorganic pyrophosphatase is a component of the Drosophila nucleosome
RT remodeling factor complex.";
RL Genes Dev. 12:3206-3216(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RX PubMed=8521501; DOI=10.1016/0092-8674(95)90216-3;
RA Tsukiyama T., Wu C.;
RT "Purification and properties of an ATP-dependent nucleosome remodeling
RT factor.";
RL Cell 83:1011-1020(1995).
CC -!- FUNCTION: Component of NURF (nucleosome remodeling factor), a complex
CC which catalyzes ATP-dependent nucleosome sliding and facilitates
CC transcription of chromatin (PubMed:9784495). NURF is required for
CC homeotic gene expression, proper larval blood cell development, normal
CC male X chromosome morphology, ecdysteroid signaling and metamorphosis
CC (PubMed:9784495, PubMed:8521501). Inorganic pyrophosphatase (PPase),
CC hydrolyzes inorganic pyrophosphate to inorganic phosphate, essential
CC for driving critical biosynthetic reactions including transcription,
CC replication, and DNA repair (PubMed:9784495).
CC {ECO:0000269|PubMed:9784495, ECO:0000303|PubMed:8521501,
CC ECO:0000303|PubMed:9784495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000269|PubMed:9784495};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC Evidence={ECO:0000269|PubMed:9784495};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the NURF complex composed of Caf1-55, E(bx),
CC Nurf-38 and Iswi. {ECO:0000269|PubMed:9784495}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000269|PubMed:9784495}.
CC -!- MISCELLANEOUS: The ATPase activity of NURF is stimulated by the
CC presence of nucleosomes rather than by free DNA.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC97111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL68291.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF085600; AAC97111.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF085601; AAC97112.1; -; mRNA.
DR EMBL; AE013599; AAF47227.2; -; Genomic_DNA.
DR EMBL; AY075479; AAL68291.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001137758.1; NM_001144286.3.
DR RefSeq; NP_523849.3; NM_079125.3.
DR AlphaFoldDB; O77460; -.
DR SMR; O77460; -.
DR BioGRID; 63494; 26.
DR IntAct; O77460; 2.
DR MINT; O77460; -.
DR STRING; 7227.FBpp0072250; -.
DR PaxDb; O77460; -.
DR PRIDE; O77460; -.
DR DNASU; 37922; -.
DR EnsemblMetazoa; FBtr0072343; FBpp0072250; FBgn0016687.
DR GeneID; 37922; -.
DR KEGG; dme:Dmel_CG4634; -.
DR CTD; 37922; -.
DR FlyBase; FBgn0016687; Nurf-38.
DR VEuPathDB; VectorBase:FBgn0016687; -.
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR InParanoid; O77460; -.
DR PhylomeDB; O77460; -.
DR Reactome; R-DME-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-DME-379726; Mitochondrial tRNA aminoacylation.
DR Reactome; R-DME-71737; Pyrophosphate hydrolysis.
DR BioGRID-ORCS; 37922; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 37922; -.
DR PRO; PR:O77460; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0016687; Expressed in secondary oocyte and 24 other tissues.
DR ExpressionAtlas; O77460; baseline and differential.
DR Genevisible; O77460; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016589; C:NURF complex; IDA:FlyBase.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:FlyBase.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IDA:FlyBase.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..338
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137572"
FT BINDING 129
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MUTAGEN 129
FT /note="R->A: Drastic reduction of activity."
FT /evidence="ECO:0000269|PubMed:9784495"
FT CONFLICT 193..194
FT /note="TI -> QF (in Ref. 1; AAC97111/AAC97112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37939 MW; B4B7341CD5A3E5F2 CRC64;
MLAKITRSSF YASRAVGRLS GSIPTSPAAL ASNCRYIQIE RKRTKSHEMA LYETVEKGAK
NSPSYSLYFK NKCGNVISPM HDIPLYANEE KTIYNMVVEV PRWTNAKMEI SLKTPMNPIK
QDIKKGKLRF VANCFPHKGY IWNYGALPQT WENPDHIEPS TGCKGDNDPI DVIEIGYRVA
KRGDVLKVKV LGTIALIDEG ETDWKIIAID VNDPLASKVN DIADVDQYFP GLLRATVEWF
KIYKIPDGKP ENQFAFNGDA KNADFANTII AETHKFWQNL VHQSPASGSI STTNITNRNS
EHVIPKEEAE KILAEAPDGG QVEEVSDTVD TWHFIHLK
