IPYR_MOUSE
ID IPYR_MOUSE Reviewed; 289 AA.
AC Q9D819;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=Ppa1; Synonyms=Pp, Pyp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 26-41, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK008575; BAB25754.1; -; mRNA.
DR EMBL; BC010468; AAH10468.1; -; mRNA.
DR CCDS; CCDS23882.1; -.
DR RefSeq; NP_080714.2; NM_026438.4.
DR AlphaFoldDB; Q9D819; -.
DR SMR; Q9D819; -.
DR BioGRID; 212519; 11.
DR IntAct; Q9D819; 4.
DR MINT; Q9D819; -.
DR STRING; 10090.ENSMUSP00000020286; -.
DR iPTMnet; Q9D819; -.
DR PhosphoSitePlus; Q9D819; -.
DR SwissPalm; Q9D819; -.
DR REPRODUCTION-2DPAGE; IPI00110684; -.
DR REPRODUCTION-2DPAGE; Q9D819; -.
DR CPTAC; non-CPTAC-3340; -.
DR CPTAC; non-CPTAC-3923; -.
DR EPD; Q9D819; -.
DR jPOST; Q9D819; -.
DR MaxQB; Q9D819; -.
DR PaxDb; Q9D819; -.
DR PRIDE; Q9D819; -.
DR ProteomicsDB; 267000; -.
DR Antibodypedia; 14866; 255 antibodies from 32 providers.
DR DNASU; 67895; -.
DR Ensembl; ENSMUST00000020286; ENSMUSP00000020286; ENSMUSG00000020089.
DR GeneID; 67895; -.
DR KEGG; mmu:67895; -.
DR UCSC; uc007fge.1; mouse.
DR CTD; 5464; -.
DR MGI; MGI:97831; Ppa1.
DR VEuPathDB; HostDB:ENSMUSG00000020089; -.
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR HOGENOM; CLU_040684_0_2_1; -.
DR InParanoid; Q9D819; -.
DR OMA; DWKILCI; -.
DR OrthoDB; 1398991at2759; -.
DR PhylomeDB; Q9D819; -.
DR TreeFam; TF300887; -.
DR BRENDA; 3.6.1.1; 3474.
DR Reactome; R-MMU-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-MMU-71737; Pyrophosphate hydrolysis.
DR BioGRID-ORCS; 67895; 29 hits in 73 CRISPR screens.
DR ChiTaRS; Ppa1; mouse.
DR PRO; PR:Q9D819; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D819; protein.
DR Bgee; ENSMUSG00000020089; Expressed in seminal vesicle and 276 other tissues.
DR ExpressionAtlas; Q9D819; baseline and differential.
DR Genevisible; Q9D819; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IDA:MGI.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
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 Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15181"
FT CHAIN 2..289
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137569"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15181"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15181"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15181"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15181"
SQ SEQUENCE 289 AA; 32667 MW; 4E2D35387CCFED8B CRC64;
MSGFSSEERA APFTLEYRVF LKNEKGQYIS PFHDVPIYAD KDVFHMVVEV PRWSNAKMEI
ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT WEDPGHSDKH TGCCGDNDPI
DVCEIGSKVC ARGEIIRVKV LGILAMIDEG ETDWKVIAIN VDDPDAANYK DISDVERLKP
GYLEATVDWF RRYKVPDGKP ENEFAFNAEF KNKDFAVDII KSTHDYWKAL VTKKTDGKGI
SCMNTTVSES PFKCDPDAAK AIVDALPPPC ESACSLPTDV DKWFHQQKN
