Skip Header

Contribute Send feedback
Read comments (?) or add your own

P39997 (NPP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. 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
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 2
Short name=E-NPP 2

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:NPP2
Ordered Locus Names:YEL016C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and PHO5. Ref.4

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.4

Post-translational modification

Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity. Ref.4

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Ectonucleotide pyrophosphatase/phosphodiesterase 2
PRO_0000202612

Regions

Topological domain1 – 2828Cytoplasmic Potential
Transmembrane29 – 4517Helical; Signal-anchor for type II membrane protein; Potential
Topological domain46 – 493448Extracellular Potential
Region76 – 438363Phosphodiesterase

Sites

Active site1271 By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1251T → I in AAT92706. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P39997 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 10E67A05C6DEDF09

FASTA49357,355
        10         20         30         40         50         60 
MLLFEQPVDL EKNNEDDTNI KPFAISRHFL LKLLLCGIIL IELLLYSKCP KPIDNGPRTI 

        70         80         90        100        110        120 
ANRSNTYFNG THDFKTLTIL ISIDGFHPRL IDAKYTPFLY NLHNLRSPYD MNITTAPYMI 

       130        140        150        160        170        180 
PSFPTQTFPN HWSMVTGKYP IEHGIVSNIF WDNFTSSEFR PNNLDARIWS NTADPIWQLL 

       190        200        210        220        230        240 
QTESQGEYKV ATHMWPGSEV VYEDHGDVPR ERMPFYFGKF NQWEKLQDKL AQIFRYIDMP 

       250        260        270        280        290        300 
QLKDRPELVI SYIPNVDSYG HSFGYDLRDK RLQKLIGEVD GFFLDLIEGL QKRNLLKISN 

       310        320        330        340        350        360 
VMIVSDHGMS NVNANDGEHV VVWERVFPAD AMSAFISHLY NEGPMMMVCL KNPRDKQWIC 

       370        380        390        400        410        420 
DLIEAQLEKA YGDEISRKFH VILKEDFDPS WKYFQYDNRK HRYDDRVGDI WILADEYYAI 

       430        440        450        460        470        480 
VKEMGDVPIG IMGTHGYNFN NCSDMASIFI GMGPMFNNEV VPPFENIEVY NMLIKASALL 

       490 
GEEKTKKEKS LLQ

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed: 9169868] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U18530 Genomic DNA. Translation: AAB64493.1.
AY692687 Genomic DNA. Translation: AAT92706.1.
BK006939 Genomic DNA. Translation: DAA07638.1.
PIRS50443.
RefSeqNP_010900.1. NM_001178831.1.

3D structure databases

ProteinModelPortalP39997.
SMRP39997. Positions 75-492.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5279N.
IntActP39997. 1 interaction.
MINTMINT-511815.
STRINGP39997.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL016C; YEL016C; YEL016C.
GeneID856699.
KEGGsce:YEL016C.
NMPDRfig|4932.3.peg.1956.

Organism-specific databases

CYGDYEL016c.
SGDS000000742. NPP2.

Phylogenomic databases

eggNOGfuNOG07343.
GeneTreeEFGT00050000006214.
OMADIQGHEY.
OrthoDBEOG43246W.

Gene expression databases

ArrayExpressP39997.
GenevestigatorP39997.
GermOnlineYEL016C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024873. E-NPP.
IPR002591. Phosphodiest/P_Trfase.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
PANTHERPTHR10151. PTHR10151. 1 hit.
PfamPF01663. Phosphodiest. 1 hit.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
ProtoNetSearch...

Other

NextBio982760.

Entry information

Entry nameNPP2_YEAST
AccessionPrimary (citable) accession number: P39997
Secondary accession number(s): D3DLN4, Q6B2P3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents