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P25353 (NPP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase 1

Short name=E-NPP 1

Including the following 2 domains:

  1. Alkaline phosphodiesterase 1
    EC=3.1.4.1
  2. Nucleotide pyrophosphatase
    Short name=NPPase
    EC=3.6.1.9
Gene names
Name:NPP1
Ordered Locus Names:YCR026C
ORF Names:YCR246, YCR26C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP2 and PHO5. Ref.6

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.6

Post-translational modification

Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity. Ref.6

N-glycosylated.

Miscellaneous

Present with 3420 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 742742Ectonucleotide pyrophosphatase/phosphodiesterase 1
PRO_0000202566

Regions

Topological domain1 – 113113Cytoplasmic Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 742608Extracellular Potential
Region168 – 545378Phosphodiesterase
Compositional bias692 – 70211Poly-Ser

Sites

Active site2191Nucleophile By similarity

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P25353 [UniParc].

Last modified June 27, 2003. Version 2.
Checksum: 83BD5F00D69B09C5

FASTA74284,734
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-742.
[5]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, NPP ACTIVITY, INDUCTION, AUTOPHOSPHORYLATION.
[7]"Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAC42978.1.
BK006937 Genomic DNA. Translation: DAA07505.1.
PIRS19437.
S27380.
RefSeqNP_009955.2. NM_001178741.1.

3D structure databases

ProteinModelPortalP25353.
SMRP25353. Positions 168-606.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31008. 18 interactions.
STRING4932.YCR026C.

Proteomic databases

PaxDbP25353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR026C; YCR026C; YCR026C.
GeneID850391.
KEGGsce:YCR026C.

Organism-specific databases

CYGDYCR026c.
SGDS000000621. NPP1.

Phylogenomic databases

eggNOGCOG1524.
GeneTreeENSGT00660000095322.
OMAGNFPKEW.
OrthoDBEOG74J9HK.

Enzyme and pathway databases

BioCycYEAST:G3O-29341-MONOMER.

Gene expression databases

GenevestigatorP25353.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PANTHERPTHR10151. PTHR10151. 1 hit.
PfamPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
ProtoNetSearch...

Other

NextBio965909.

Entry information

Entry nameNPP1_YEAST
AccessionPrimary (citable) accession number: P25353
Secondary accession number(s): D6VR36, Q8NIL9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families