Reviewed, UniProtKB/Swiss-Prot P25353 (NPP1_YEAST)

Names and origin

Protein names

Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase 1
      Short name=E-NPP 1
Including the following 2 domains:
    1- Recommended name:
            Alkaline phosphodiesterase 1
              EC=3.1.4.1
    2- Recommended name:
            Nucleotide pyrophosphatase
                Short name=NPPase
              EC=3.6.1.9

Gene names

Name:	NPP1
Ordered Locus Names:	YCR026C
ORF Names:	YCR26C, YCR246

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	742 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP2 and PHO5. Ref.5
Catalytic activity	Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides. A dinucleotide + H2O = 2 mononucleotides.
Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Induction	Up-regulated during phosphate starvation. Ref.5
Post-translational modification	Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity. Ref.5 Ref.6
Miscellaneous	Present with 3420 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cellular response to phosphate starvation Ref.5 Inferred from expression pattern. Source: SGD phosphate metabolic process Ref.5 Inferred from mutant phenotype. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleoside-triphosphatase activity Ref.5 Inferred from genetic interaction. Source: SGD nucleoside-triphosphate diphosphatase activity Ref.5 Inferred from direct assay. Source: SGD nucleotide diphosphatase activity Inferred from electronic annotation. Source: EC phosphodiesterase I activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 742	742	Ectonucleotide pyrophosphatase/phosphodiesterase 1		PRO_0000202566
Regions
	Topological domain	1 – 113	113	Cytoplasmic Potential
	Transmembrane	114 – 134	21	Potential
	Topological domain	135 – 742	608	Extracellular Potential
	Region	168 – 545	378	Phosphodiesterase
	Compositional bias	692 – 702	11	Poly-Ser
Sites
	Active site	219	1	By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.6
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Glycosylation	296	1	N-linked (GlcNAc...) Potential
	Glycosylation	403	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P25353-1 [UniParc]. Last modified June 27, 2003. Version 2. Checksum: 83BD5F00D69B09C5	FASTA	742	84,734
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete DNA sequence of yeast chromosome III." 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. Nature 357:38-46(1992) [PubMed: 1574125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"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." Bolle P.-A., Gilliquet V., Berben G., Dumont J., Hilger F. Yeast 8:205-213(1992) [PubMed: 1574926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-742.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae." Kennedy E.J., Pillus L., Ghosh G. Eukaryot. Cell 4:1892-1901(2005) [PubMed: 16278456] [Abstract] Cited for: FUNCTION, NPP ACTIVITY, INDUCTION, AUTOPHOSPHORYLATION.
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59720 Genomic DNA. Translation: CAC42978.1.
PIR	S19437. S27380.
RefSeq	NP_009955.2.
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	YCR026C. Saccharomyces cerevisiae. [Contig view]
GeneID	850391.
GenomeReviews	Gene locus YCR026C in contig X59720_GR.
KEGG	sce:YCR026C.
NMPDR	fig|4932.3.peg.680.
Organism-specific databases
CYGD	YCR026c.
SGD	S000000621. NPP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P25353.
OMA	P25353. GNFPKEW.
Enzyme and pathway databases
BRENDA	3.1.4.1. 250. 3.6.1.9. 250.
Gene expression databases
ArrayExpress	P25353.
GermOnline	YCR026C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR002591. Phosphodiest/P_Trfase. [Graphical view]
Gene3D	G3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
Pfam	PF01663. Phosphodiest. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	965909.

Entry information

Entry name

NPP1_YEAST

Accession

Primary (citable) accession number: P25353
Secondary accession number(s): Q8NIL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	June 27, 2003
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)