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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase 1

Gene

NPP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP2 and PHO5.1 Publication

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
A dinucleotide + H2O = 2 mononucleotides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei219 – 2191NucleophileBy similarity

GO - Molecular functioni

  1. NADH pyrophosphatase activity Source: UniProtKB-EC
  2. nucleoside-triphosphatase activity Source: SGD
  3. nucleoside-triphosphate diphosphatase activity Source: SGD
  4. nucleotide diphosphatase activity Source: SGD
  5. phosphodiesterase I activity Source: SGD

GO - Biological processi

  1. cellular response to phosphate starvation Source: SGD
  2. nucleic acid phosphodiester bond hydrolysis Source: GOC
  3. nucleoside triphosphate metabolic process Source: SGD
  4. phosphate-containing compound metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciYEAST:G3O-29341-MONOMER.
ReactomeiREACT_307521. Glycosphingolipid metabolism.
REACT_324957. Vitamin B2 (riboflavin) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase 1
Short name:
E-NPP 1
Including the following 2 domains:
Alkaline phosphodiesterase 1 (EC:3.1.4.1)
Nucleotide pyrophosphatase (EC:3.6.1.9)
Short name:
NPPase
Gene namesi
Name:NPP1
Ordered Locus Names:YCR026C
ORF Names:YCR246, YCR26C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome III

Organism-specific databases

CYGDiYCR026c.
EuPathDBiFungiDB:YCR026C.
SGDiS000000621. NPP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 113113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 742608ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Ectonucleotide pyrophosphatase/phosphodiesterase 1PRO_0000202566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.
N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25353.
PaxDbiP25353.

Expressioni

Inductioni

Up-regulated during phosphate starvation.1 Publication

Gene expression databases

GenevestigatoriP25353.

Interactioni

Protein-protein interaction databases

BioGridi31008. 19 interactions.
STRINGi4932.YCR026C.

Structurei

3D structure databases

ProteinModelPortaliP25353.
SMRiP25353. Positions 168-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni168 – 545378PhosphodiesteraseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi692 – 70211Poly-SerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
GeneTreeiENSGT00760000119157.
InParanoidiP25353.
OMAiGNFPKEW.
OrthoDBiEOG74J9HK.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.

Sequencei

Sequence statusi: Complete.

P25353-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELQNDLESL DNELNDFSED PFRDDFITDE DAVRSGWRSA WTRMKYWFYK
60 70 80 90 100
NRLKWTNNPI VIGDAKDSRD GSNFRRGIPL YELDANGQPI DTELVDENEL
110 120 130 140 150
SFGTGFHSKV PFKIIFRTLF GSLVFAIFLI LMINIAKPHH STRVLSHFGS
160 170 180 190 200
PEFDPYVKYF NGTHEFFPLT IVISLDGFHP SLISKRNTPF LHDLYELKYD
210 220 230 240 250
GGMNITSTPF MVPSFPTETF PNHWTLVTGQ YPIHHGIVSN VFWDPDLNEE
260 270 280 290 300
FHPGVLDPRI WNNNDTEPIW QTVQSAFDGD IPFKAATHMW PGSDVNYTKY
310 320 330 340 350
NEEKLQPEHK NPIARERTPF YFDEFNAKEP LSQKLSKIIE YVDMSTLNER
360 370 380 390 400
PQLILGYVPN VDAFGHKHGY PSESEYYYED FTETLGEVDT FLKQLVESLQ
410 420 430 440 450
ERNLTSFTNL VIVSDHGMSD IVVPSNVIIW EDLLDEKLRK DYVSHAYLEG
460 470 480 490 500
PMMAISLKDS GNINEVYHNL KTSIDEDKYT VYVNGNFPKE WNFNDGKNHH
510 520 530 540 550
MASIWIVPEP GYAVMKKEQL KKVAKGDHKD KNEDNVFTIG SHGYDNNAID
560 570 580 590 600
MRSVFIGMGP YFPQGYIEPF QNTEIYNLLC DICGVAEKDR NSNDGTGMLM
610 620 630 640 650
NQLREPQSSE EVEIEDDFDY LVSKFGEFST YNIIWGGYPE ETEQDNVDND
660 670 680 690 700
NDDNDDGNTD EIAAMPSSSL TIKLEMTTSI PSATETLLGE TSPSSRSSSS
710 720 730 740
SSIQASATAS TVGDWLQDII NDAKDLIDDI IDSIDDLVDS DT
Length:742
Mass (Da):84,734
Last modified:June 27, 2003 - v2
Checksum:i83BD5F00D69B09C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42978.1.
BK006937 Genomic DNA. Translation: DAA07505.1.
PIRiS19437.
S27380.
RefSeqiNP_009955.2. NM_001178741.1.

Genome annotation databases

EnsemblFungiiYCR026C; YCR026C; YCR026C.
GeneIDi850391.
KEGGisce:YCR026C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42978.1.
BK006937 Genomic DNA. Translation: DAA07505.1.
PIRiS19437.
S27380.
RefSeqiNP_009955.2. NM_001178741.1.

3D structure databases

ProteinModelPortaliP25353.
SMRiP25353. Positions 168-606.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31008. 19 interactions.
STRINGi4932.YCR026C.

Proteomic databases

MaxQBiP25353.
PaxDbiP25353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCR026C; YCR026C; YCR026C.
GeneIDi850391.
KEGGisce:YCR026C.

Organism-specific databases

CYGDiYCR026c.
EuPathDBiFungiDB:YCR026C.
SGDiS000000621. NPP1.

Phylogenomic databases

eggNOGiCOG1524.
GeneTreeiENSGT00760000119157.
InParanoidiP25353.
OMAiGNFPKEW.
OrthoDBiEOG74J9HK.

Enzyme and pathway databases

BioCyciYEAST:G3O-29341-MONOMER.
ReactomeiREACT_307521. Glycosphingolipid metabolism.
REACT_324957. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

NextBioi965909.
PROiP25353.

Gene expression databases

GenevestigatoriP25353.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PfamiPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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. 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. 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].

Entry informationi

Entry nameiNPP1_YEAST
AccessioniPrimary (citable) accession number: P25353
Secondary accession number(s): D6VR36, Q8NIL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 27, 2003
Last modified: April 29, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.