Full text data of PPA2
PPA2
[Confidence: low (only semi-automatic identification from reviews)]
Inorganic pyrophosphatase 2, mitochondrial; 3.6.1.1 (Pyrophosphatase SID6-306; Pyrophosphate phospho-hydrolase 2; PPase 2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Inorganic pyrophosphatase 2, mitochondrial; 3.6.1.1 (Pyrophosphatase SID6-306; Pyrophosphate phospho-hydrolase 2; PPase 2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H2U2
ID IPYR2_HUMAN Reviewed; 334 AA.
AC Q9H2U2; B4DLP7; F8WDN9; I6L9B6; Q4W5E9; Q6PG51; Q8TBW0; Q96E55;
read moreAC Q9H0T0; Q9NX37; Q9P033; Q9ULX0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Inorganic pyrophosphatase 2, mitochondrial;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphatase SID6-306;
DE AltName: Full=Pyrophosphate phospho-hydrolase 2;
DE Short=PPase 2;
DE Flags: Precursor;
GN Name=PPA2; ORFNames=HSPC124;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Saito T., Hattori A., Miyajima N.;
RT "Putative inorganic pyrophosphatase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kanni L., Johansson M., Karlsson A.;
RT "Cloning of the mitochondrial inorganic pyrophosphatase 2 cDNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ASN-282.
RC TISSUE=Fibroblast, and Gastric carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 3-334 (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 12-334 (ISOFORM 5).
RC TISSUE=Lung, Ovary, and Skeletal muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-334 (ISOFORM 2), AND
RP VARIANT ASN-282.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-334 (ISOFORM 2), AND
RP VARIANT ASN-282.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP PROTEIN SEQUENCE OF 33-40.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15210126; DOI=10.1016/j.bbapap.2004.03.014;
RA Afjehi-Sadat L., Krapfenbauer K., Slavc I., Fountoulakis M., Lubec G.;
RT "Hypothetical proteins with putative enzyme activity in human amnion,
RT lymphocyte, bronchial epithelial and kidney cell lines.";
RL Biochim. Biophys. Acta 1700:65-74(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H2U2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2U2-2; Sequence=VSP_011651;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=Q9H2U2-3; Sequence=VSP_011652;
CC Name=4;
CC IsoId=Q9H2U2-4; Sequence=VSP_011649, VSP_011650;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9H2U2-6; Sequence=VSP_046256;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in brain, gastric carcinoma, lung,
CC ovary, skeletal muscle, umbilical cord blood and a cell line
CC derived from kidney proximal tubule epithelium.
CC -!- SIMILARITY: Belongs to the PPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29088.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAF29088.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=BAA84701.1; Type=Erroneous initiation;
CC Sequence=BAA91184.1; Type=Erroneous termination; Positions=59; Note=Translated as Tyr;
CC Sequence=BAG59609.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=CAB66590.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB66590.2; Type=Frameshift; Positions=75;
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DR EMBL; AB026722; BAA84701.1; ALT_INIT; mRNA.
DR EMBL; AF217187; AAG36781.1; -; mRNA.
DR EMBL; AK000466; BAA91184.1; ALT_SEQ; mRNA.
DR EMBL; AK297096; BAG59609.1; ALT_SEQ; mRNA.
DR EMBL; AC004066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106888; AAY41040.1; -; Genomic_DNA.
DR EMBL; BC022803; AAH22803.1; -; mRNA.
DR EMBL; BC039462; AAH39462.2; -; mRNA.
DR EMBL; BC057219; AAH57219.1; -; mRNA.
DR EMBL; AF161473; AAF29088.1; ALT_SEQ; mRNA.
DR EMBL; AL136655; CAB66590.2; ALT_SEQ; mRNA.
DR RefSeq; NP_008834.3; NM_006903.4.
DR RefSeq; NP_789842.2; NM_176866.2.
DR RefSeq; NP_789843.2; NM_176867.3.
DR RefSeq; NP_789845.1; NM_176869.2.
DR UniGene; Hs.654957; -.
DR ProteinModelPortal; Q9H2U2; -.
DR SMR; Q9H2U2; 35-332.
DR IntAct; Q9H2U2; 1.
DR MINT; MINT-3066899; -.
DR PhosphoSite; Q9H2U2; -.
DR DMDM; 116242592; -.
DR OGP; Q9H2U2; -.
DR PaxDb; Q9H2U2; -.
DR PeptideAtlas; Q9H2U2; -.
DR PRIDE; Q9H2U2; -.
DR DNASU; 27068; -.
DR Ensembl; ENST00000341695; ENSP00000343885; ENSG00000138777.
DR Ensembl; ENST00000348706; ENSP00000313061; ENSG00000138777.
DR Ensembl; ENST00000354147; ENSP00000340352; ENSG00000138777.
DR Ensembl; ENST00000357415; ENSP00000349996; ENSG00000138777.
DR Ensembl; ENST00000432483; ENSP00000389957; ENSG00000138777.
DR Ensembl; ENST00000509031; ENSP00000423467; ENSG00000138777.
DR GeneID; 27068; -.
DR KEGG; hsa:27068; -.
DR UCSC; uc003hxo.3; human.
DR CTD; 27068; -.
DR GeneCards; GC04M106290; -.
DR HGNC; HGNC:28883; PPA2.
DR HPA; HPA031671; -.
DR MIM; 609988; gene.
DR neXtProt; NX_Q9H2U2; -.
DR PharmGKB; PA142671159; -.
DR eggNOG; COG0221; -.
DR HOVERGEN; HBG000491; -.
DR KO; K01507; -.
DR OMA; ASKFHDI; -.
DR OrthoDB; EOG7R2BKH; -.
DR PhylomeDB; Q9H2U2; -.
DR BRENDA; 3.6.1.1; 2681.
DR Reactome; REACT_21259; Pyrophosphate hydrolysis.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PPA2; human.
DR GenomeRNAi; 27068; -.
DR NextBio; 35533887; -.
DR PRO; PR:Q9H2U2; -.
DR ArrayExpress; Q9H2U2; -.
DR Bgee; Q9H2U2; -.
DR CleanEx; HS_PPA2; -.
DR Genevestigator; Q9H2U2; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0004427; F:inorganic diphosphatase activity; TAS:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0071344; P:diphosphate metabolic process; TAS:Reactome.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 32 Mitochondrion.
FT CHAIN 33 334 Inorganic pyrophosphatase 2,
FT mitochondrial.
FT /FTId=PRO_0000025411.
FT METAL 164 164 Magnesium 1 (By similarity).
FT METAL 169 169 Magnesium 1 (By similarity).
FT METAL 169 169 Magnesium 2 (By similarity).
FT METAL 201 201 Magnesium 1 (By similarity).
FT MOD_RES 224 224 N6-acetyllysine (By similarity).
FT MOD_RES 261 261 N6-acetyllysine.
FT MOD_RES 317 317 Phosphoserine.
FT VAR_SEQ 53 53 K -> N (in isoform 4).
FT /FTId=VSP_011649.
FT VAR_SEQ 54 219 Missing (in isoform 4).
FT /FTId=VSP_011650.
FT VAR_SEQ 74 74 E -> EDTEAQGIFIDLSKIW (in isoform 2).
FT /FTId=VSP_011651.
FT VAR_SEQ 75 176 Missing (in isoform 5).
FT /FTId=VSP_046256.
FT VAR_SEQ 148 176 Missing (in isoform 3).
FT /FTId=VSP_011652.
FT VARIANT 282 282 K -> N (in dbSNP:rs13787).
FT /FTId=VAR_019723.
FT CONFLICT 11 11 G -> V (in Ref. 1; BAA84701 and 2;
FT AAG36781).
FT CONFLICT 19 19 R -> G (in Ref. 7; CAB66590).
FT CONFLICT 103 103 N -> K (in Ref. 7; CAB66590).
FT CONFLICT 241 241 Y -> C (in Ref. 7; CAB66590).
FT CONFLICT 288 288 I -> T (in Ref. 7; CAB66590).
SQ SEQUENCE 334 AA; 37920 MW; F8C85F64CDA447F1 CRC64;
MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI
SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR WTNAKMEIAT KEPMNPIKQY
VKDGKLRYVA NIFPYKGYIW NYGTLPQTWE DPHEKDKSTN CFGDNDPIDV CEIGSKILSC
GEVIHVKILG ILALIDEGET DWKLIAINAN DPEASKFHDI DDVKKFKPGY LEATLNWFRL
YKVPDGKPEN QFAFNGEFKN KAFALEVIKS THQCWKALLM KKCNGGAINC TNVQISDSPF
RCTQEEARSL VESVSSSPNK ESNEEEQVWH FLGK
//
ID IPYR2_HUMAN Reviewed; 334 AA.
AC Q9H2U2; B4DLP7; F8WDN9; I6L9B6; Q4W5E9; Q6PG51; Q8TBW0; Q96E55;
read moreAC Q9H0T0; Q9NX37; Q9P033; Q9ULX0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Inorganic pyrophosphatase 2, mitochondrial;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphatase SID6-306;
DE AltName: Full=Pyrophosphate phospho-hydrolase 2;
DE Short=PPase 2;
DE Flags: Precursor;
GN Name=PPA2; ORFNames=HSPC124;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Saito T., Hattori A., Miyajima N.;
RT "Putative inorganic pyrophosphatase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kanni L., Johansson M., Karlsson A.;
RT "Cloning of the mitochondrial inorganic pyrophosphatase 2 cDNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ASN-282.
RC TISSUE=Fibroblast, and Gastric carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 3-334 (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 12-334 (ISOFORM 5).
RC TISSUE=Lung, Ovary, and Skeletal muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-334 (ISOFORM 2), AND
RP VARIANT ASN-282.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-334 (ISOFORM 2), AND
RP VARIANT ASN-282.
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP PROTEIN SEQUENCE OF 33-40.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15210126; DOI=10.1016/j.bbapap.2004.03.014;
RA Afjehi-Sadat L., Krapfenbauer K., Slavc I., Fountoulakis M., Lubec G.;
RT "Hypothetical proteins with putative enzyme activity in human amnion,
RT lymphocyte, bronchial epithelial and kidney cell lines.";
RL Biochim. Biophys. Acta 1700:65-74(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H2U2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2U2-2; Sequence=VSP_011651;
CC Note=May be produced at very low levels due to a premature stop
CC codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=Q9H2U2-3; Sequence=VSP_011652;
CC Name=4;
CC IsoId=Q9H2U2-4; Sequence=VSP_011649, VSP_011650;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q9H2U2-6; Sequence=VSP_046256;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in brain, gastric carcinoma, lung,
CC ovary, skeletal muscle, umbilical cord blood and a cell line
CC derived from kidney proximal tubule epithelium.
CC -!- SIMILARITY: Belongs to the PPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29088.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAF29088.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC Sequence=BAA84701.1; Type=Erroneous initiation;
CC Sequence=BAA91184.1; Type=Erroneous termination; Positions=59; Note=Translated as Tyr;
CC Sequence=BAG59609.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=CAB66590.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAB66590.2; Type=Frameshift; Positions=75;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AB026722; BAA84701.1; ALT_INIT; mRNA.
DR EMBL; AF217187; AAG36781.1; -; mRNA.
DR EMBL; AK000466; BAA91184.1; ALT_SEQ; mRNA.
DR EMBL; AK297096; BAG59609.1; ALT_SEQ; mRNA.
DR EMBL; AC004066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106888; AAY41040.1; -; Genomic_DNA.
DR EMBL; BC022803; AAH22803.1; -; mRNA.
DR EMBL; BC039462; AAH39462.2; -; mRNA.
DR EMBL; BC057219; AAH57219.1; -; mRNA.
DR EMBL; AF161473; AAF29088.1; ALT_SEQ; mRNA.
DR EMBL; AL136655; CAB66590.2; ALT_SEQ; mRNA.
DR RefSeq; NP_008834.3; NM_006903.4.
DR RefSeq; NP_789842.2; NM_176866.2.
DR RefSeq; NP_789843.2; NM_176867.3.
DR RefSeq; NP_789845.1; NM_176869.2.
DR UniGene; Hs.654957; -.
DR ProteinModelPortal; Q9H2U2; -.
DR SMR; Q9H2U2; 35-332.
DR IntAct; Q9H2U2; 1.
DR MINT; MINT-3066899; -.
DR PhosphoSite; Q9H2U2; -.
DR DMDM; 116242592; -.
DR OGP; Q9H2U2; -.
DR PaxDb; Q9H2U2; -.
DR PeptideAtlas; Q9H2U2; -.
DR PRIDE; Q9H2U2; -.
DR DNASU; 27068; -.
DR Ensembl; ENST00000341695; ENSP00000343885; ENSG00000138777.
DR Ensembl; ENST00000348706; ENSP00000313061; ENSG00000138777.
DR Ensembl; ENST00000354147; ENSP00000340352; ENSG00000138777.
DR Ensembl; ENST00000357415; ENSP00000349996; ENSG00000138777.
DR Ensembl; ENST00000432483; ENSP00000389957; ENSG00000138777.
DR Ensembl; ENST00000509031; ENSP00000423467; ENSG00000138777.
DR GeneID; 27068; -.
DR KEGG; hsa:27068; -.
DR UCSC; uc003hxo.3; human.
DR CTD; 27068; -.
DR GeneCards; GC04M106290; -.
DR HGNC; HGNC:28883; PPA2.
DR HPA; HPA031671; -.
DR MIM; 609988; gene.
DR neXtProt; NX_Q9H2U2; -.
DR PharmGKB; PA142671159; -.
DR eggNOG; COG0221; -.
DR HOVERGEN; HBG000491; -.
DR KO; K01507; -.
DR OMA; ASKFHDI; -.
DR OrthoDB; EOG7R2BKH; -.
DR PhylomeDB; Q9H2U2; -.
DR BRENDA; 3.6.1.1; 2681.
DR Reactome; REACT_21259; Pyrophosphate hydrolysis.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PPA2; human.
DR GenomeRNAi; 27068; -.
DR NextBio; 35533887; -.
DR PRO; PR:Q9H2U2; -.
DR ArrayExpress; Q9H2U2; -.
DR Bgee; Q9H2U2; -.
DR CleanEx; HS_PPA2; -.
DR Genevestigator; Q9H2U2; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0004427; F:inorganic diphosphatase activity; TAS:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0071344; P:diphosphate metabolic process; TAS:Reactome.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Phosphoprotein; Polymorphism; Reference proteome;
KW Transit peptide.
FT TRANSIT 1 32 Mitochondrion.
FT CHAIN 33 334 Inorganic pyrophosphatase 2,
FT mitochondrial.
FT /FTId=PRO_0000025411.
FT METAL 164 164 Magnesium 1 (By similarity).
FT METAL 169 169 Magnesium 1 (By similarity).
FT METAL 169 169 Magnesium 2 (By similarity).
FT METAL 201 201 Magnesium 1 (By similarity).
FT MOD_RES 224 224 N6-acetyllysine (By similarity).
FT MOD_RES 261 261 N6-acetyllysine.
FT MOD_RES 317 317 Phosphoserine.
FT VAR_SEQ 53 53 K -> N (in isoform 4).
FT /FTId=VSP_011649.
FT VAR_SEQ 54 219 Missing (in isoform 4).
FT /FTId=VSP_011650.
FT VAR_SEQ 74 74 E -> EDTEAQGIFIDLSKIW (in isoform 2).
FT /FTId=VSP_011651.
FT VAR_SEQ 75 176 Missing (in isoform 5).
FT /FTId=VSP_046256.
FT VAR_SEQ 148 176 Missing (in isoform 3).
FT /FTId=VSP_011652.
FT VARIANT 282 282 K -> N (in dbSNP:rs13787).
FT /FTId=VAR_019723.
FT CONFLICT 11 11 G -> V (in Ref. 1; BAA84701 and 2;
FT AAG36781).
FT CONFLICT 19 19 R -> G (in Ref. 7; CAB66590).
FT CONFLICT 103 103 N -> K (in Ref. 7; CAB66590).
FT CONFLICT 241 241 Y -> C (in Ref. 7; CAB66590).
FT CONFLICT 288 288 I -> T (in Ref. 7; CAB66590).
SQ SEQUENCE 334 AA; 37920 MW; F8C85F64CDA447F1 CRC64;
MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI
SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR WTNAKMEIAT KEPMNPIKQY
VKDGKLRYVA NIFPYKGYIW NYGTLPQTWE DPHEKDKSTN CFGDNDPIDV CEIGSKILSC
GEVIHVKILG ILALIDEGET DWKLIAINAN DPEASKFHDI DDVKKFKPGY LEATLNWFRL
YKVPDGKPEN QFAFNGEFKN KAFALEVIKS THQCWKALLM KKCNGGAINC TNVQISDSPF
RCTQEEARSL VESVSSSPNK ESNEEEQVWH FLGK
//
MIM
609988
*RECORD*
*FIELD* NO
609988
*FIELD* TI
*609988 PYROPHOSPHATASE, INORGANIC, 2; PPA2
*FIELD* TX
DESCRIPTION
Inorganic pyrophosphates are generated as byproducts of many
read morebiosynthetic reactions, including DNA and RNA synthesis, fatty acid and
amino acid activation, and cyclic nucleotide synthesis. Inorganic
pyrophosphatases (EC 3.6.1.1), such as PPA2, maintain the thermodynamic
favorability of these reactions by catalyzing the hydrolysis of
pyrophosphates into organic phosphates, which are then exported across
the cell membrane (Curbo et al., 2006).
CLONING
By searching databases using PPA1 (179030) as query, Curbo et al. (2006)
identified PPA2. The deduced 334-amino acid protein has a calculated
molecular mass of 38 kD. PPA2 shares about 60% amino acid identity with
PPA1, and it has a 31-amino acid N-terminal extension not found in PPA1
that functions as a mitochondrial import signal. Northern blot analysis
detected a 1.4-kb PPA2 transcript in all 12 tissues examined, with
highest levels in heart, skeletal muscle, kidney, and liver.
Fluorescence-tagged PPA2 localized with a mitochondrial marker in
transfected HeLa cells.
GENE FUNCTION
Curbo et al. (2006) found that recombinant PPA2 hydrolyzed pyrophosphate
in vitro. The reaction was dependent on Mg(2+) and inhibited by Ca(2+).
GENE STRUCTURE
Curbo et al. (2006) determined that the PPA2 gene contains 12 exons and
spans about 100 kb.
MAPPING
By genomic sequence analysis, Curbo et al. (2006) mapped the PPA2 gene
to chromosome 4q25.
*FIELD* RF
1. Curbo, S.; Lagier-Tourenne, C.; Carrozzo, R.; Palenzuela, L.; Lucioli,
S.; Hirano, M.; Santorelli, F.; Arenas, J.; Karlsson, A.; Johansson,
M.: Human mitochondrial pyrophosphatase: cDNA cloning and analysis
of the gene in patients with mtDNA depletion syndromes. Genomics 87:
410-416, 2006.
*FIELD* CD
Patricia A. Hartz: 3/21/2006
*FIELD* ED
mgross: 03/21/2006
*RECORD*
*FIELD* NO
609988
*FIELD* TI
*609988 PYROPHOSPHATASE, INORGANIC, 2; PPA2
*FIELD* TX
DESCRIPTION
Inorganic pyrophosphates are generated as byproducts of many
read morebiosynthetic reactions, including DNA and RNA synthesis, fatty acid and
amino acid activation, and cyclic nucleotide synthesis. Inorganic
pyrophosphatases (EC 3.6.1.1), such as PPA2, maintain the thermodynamic
favorability of these reactions by catalyzing the hydrolysis of
pyrophosphates into organic phosphates, which are then exported across
the cell membrane (Curbo et al., 2006).
CLONING
By searching databases using PPA1 (179030) as query, Curbo et al. (2006)
identified PPA2. The deduced 334-amino acid protein has a calculated
molecular mass of 38 kD. PPA2 shares about 60% amino acid identity with
PPA1, and it has a 31-amino acid N-terminal extension not found in PPA1
that functions as a mitochondrial import signal. Northern blot analysis
detected a 1.4-kb PPA2 transcript in all 12 tissues examined, with
highest levels in heart, skeletal muscle, kidney, and liver.
Fluorescence-tagged PPA2 localized with a mitochondrial marker in
transfected HeLa cells.
GENE FUNCTION
Curbo et al. (2006) found that recombinant PPA2 hydrolyzed pyrophosphate
in vitro. The reaction was dependent on Mg(2+) and inhibited by Ca(2+).
GENE STRUCTURE
Curbo et al. (2006) determined that the PPA2 gene contains 12 exons and
spans about 100 kb.
MAPPING
By genomic sequence analysis, Curbo et al. (2006) mapped the PPA2 gene
to chromosome 4q25.
*FIELD* RF
1. Curbo, S.; Lagier-Tourenne, C.; Carrozzo, R.; Palenzuela, L.; Lucioli,
S.; Hirano, M.; Santorelli, F.; Arenas, J.; Karlsson, A.; Johansson,
M.: Human mitochondrial pyrophosphatase: cDNA cloning and analysis
of the gene in patients with mtDNA depletion syndromes. Genomics 87:
410-416, 2006.
*FIELD* CD
Patricia A. Hartz: 3/21/2006
*FIELD* ED
mgross: 03/21/2006