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UniProtKB/Swiss-Prot entry P25353


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NPP1_YEAST
Primary accession number P25353
Secondary accession number Q8NIL9
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on June 27, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Ectonucleotide pyrophosphatase/phosphodiesterase 1
Synonym E-NPP 1
Includes Alkaline phosphodiesterase 1
     (EC 3.1.4.1)
Nucleotide pyrophosphatase
     (NPPase)
     (EC 3.6.1.9)
Gene name
Name: NPP1
OrderedLocusNames: YCR026C
ORFNames: YCR26C, YCR246
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/357038a0; PubMed=1574125 [NCBI, ExPASy, EBI, Israel, Japan]
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[2]
SEQUENCE REVISION.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-742.
PubMed=1574926 [NCBI, ExPASy, EBI, Israel, Japan]
Bolle P.-A., Gilliquet V., Berben G., Dumont J., Hilger F.;
"The complete sequence of K3B, a 7.9 kb fragment between PGK1 and CRY1 on chromosome III, reveals the presence of seven open reading frames.";
Yeast 8:205-213(1992).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
FUNCTION, NPP ACTIVITY, INDUCTION, AND AUTOPHOSPHORYLATION.
DOI=10.1128/EC.4.11.1892-1901.2005; PubMed=16278456 [NCBI, ExPASy, EBI, Israel, Japan]
Kennedy E.J., Pillus L., Ghosh G.;
"Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae.";
Eukaryot. Cell 4:1892-1901(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X59720; CAC42978.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19437; S19437.
S27380; S27380.
RefSeq NP_009955.2; -.
3D structure databases
ModBase P25353.
Organism-specific databases
CYGD YCR026c; -.
SGD S000000621; NPP1.
Yeast-GFP YCR026C.
Gene expression databases
ArrayExpress P25353; -.
GermOnline YCR026C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0017111; Molecular function: nucleoside-triphosphatase activity (inferred from genetic interaction from SGD).
GO:0047429; Molecular function: nucleoside-triphosphate diphosphatase activity (inferred from direct assay from SGD).
GO:0004551; Molecular function: nucleotide diphosphatase activity (inferred from electronic annotation from EC).
GO:0004528; Molecular function: phosphodiesterase I activity (inferred from electronic annotation from EC).
GO:0016036; Biological process: cellular response to phosphate starvation (inferred from expression pattern from SGD).
GO:0006796; Biological process: phosphate metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR017849; Alkaline_Pase-like_a/b/a.
IPR002591; Phosphodiest/P_Trfase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.720.10; Alk_phosphtse; 1.
Pfam PF01663; Phosphodiest; 1.
Pfam graphical view of domain structure.
ProtoNet P25353.
Genome annotation databases
Ensembl YCR026C; Saccharomyces cerevisiae. [Contig view]
GeneID 850391; -.
GenomeReviews X59720_GR; YCR026C.
KEGG sce:YCR026C; -.
NMPDR fig|4932.3.peg.680; -.
Phylogenomic databases
HOGENOM P25353; -.
Other
LinkHub P25353; -.
NextBio 965909; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycoprotein; Hydrolase; Membrane; Multifunctional enzyme; Phosphoprotein; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   742  742     Ectonucleotide pyrophosphatase/phosphodiesterase 1. PRO_0000202566
TOPO_DOM   1   113  113     Cytoplasmic (Potential). 
TRANSMEM   114   134  21     Potential. 
TOPO_DOM   135   742  608     Extracellular (Potential). 
REGION   168   545  378     Phosphodiesterase. 
COMPBIAS   692   702  11     Poly-Ser. 
ACT_SITE   219   219        By similarity. 
MOD_RES   9     9        Phosphoserine. 
CARBOHYD   161   161        N-linked (GlcNAc...) (Potential). 
CARBOHYD   204   204        N-linked (GlcNAc...) (Potential). 
CARBOHYD   264   264        N-linked (GlcNAc...) (Potential). 
CARBOHYD   296   296        N-linked (GlcNAc...) (Potential). 
CARBOHYD   403   403        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 742 AA [This is the length of the unprocessed precursor] Molecular weight: 84734 Da [This is the MW of the unprocessed precursor] CRC64: 83BD5F00D69B09C5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MELQNDLESL DNELNDFSED PFRDDFITDE DAVRSGWRSA WTRMKYWFYK NRLKWTNNPI 

        70         80         90        100        110        120 
VIGDAKDSRD GSNFRRGIPL YELDANGQPI DTELVDENEL SFGTGFHSKV PFKIIFRTLF 

       130        140        150        160        170        180 
GSLVFAIFLI LMINIAKPHH STRVLSHFGS PEFDPYVKYF NGTHEFFPLT IVISLDGFHP 

       190        200        210        220        230        240 
SLISKRNTPF LHDLYELKYD GGMNITSTPF MVPSFPTETF PNHWTLVTGQ YPIHHGIVSN 

       250        260        270        280        290        300 
VFWDPDLNEE FHPGVLDPRI WNNNDTEPIW QTVQSAFDGD IPFKAATHMW PGSDVNYTKY 

       310        320        330        340        350        360 
NEEKLQPEHK NPIARERTPF YFDEFNAKEP LSQKLSKIIE YVDMSTLNER PQLILGYVPN 

       370        380        390        400        410        420 
VDAFGHKHGY PSESEYYYED FTETLGEVDT FLKQLVESLQ ERNLTSFTNL VIVSDHGMSD 

       430        440        450        460        470        480 
IVVPSNVIIW EDLLDEKLRK DYVSHAYLEG PMMAISLKDS GNINEVYHNL KTSIDEDKYT 

       490        500        510        520        530        540 
VYVNGNFPKE WNFNDGKNHH MASIWIVPEP GYAVMKKEQL KKVAKGDHKD KNEDNVFTIG 

       550        560        570        580        590        600 
SHGYDNNAID MRSVFIGMGP YFPQGYIEPF QNTEIYNLLC DICGVAEKDR NSNDGTGMLM 

       610        620        630        640        650        660 
NQLREPQSSE EVEIEDDFDY LVSKFGEFST YNIIWGGYPE ETEQDNVDND NDDNDDGNTD 

       670        680        690        700        710        720 
EIAAMPSSSL TIKLEMTTSI PSATETLLGE TSPSSRSSSS SSIQASATAS TVGDWLQDII 

       730        740 
NDAKDLIDDI IDSIDDLVDS DT 

P25353 in FASTA format

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