[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; Nature 387:78-81(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] 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., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[3]	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).

Comments

FUNCTION: Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and PHO5.
CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
CATALYTIC ACTIVITY: A dinucleotide + H₂O = 2 mononucleotides.
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein (Potential).
INDUCTION: Up-regulated during phosphate starvation.
PTM: Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.
SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

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

U18530; AAB64493.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692687; AAT92706.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S50443; S50443.

RefSeq

NP_010900.1; -.

3D structure databases

ModBase

P39997.

Protein-protein interaction databases

DIP

DIP:5279N; -.

Organism-specific databases

YEL016c; -.

S000000742; NPP2.

Gene expression databases

ArrayExpress

P39997; -.

GermOnline

YEL016C; Saccharomyces cerevisiae.

Ontologies

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: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.

BLOCKS

P39997.

Genome annotation databases

Ensembl

YEL016C; Saccharomyces cerevisiae. [Contig view]

856699; -.

U00092_GR; YEL016C.

sce:YEL016C; -.

fig|4932.3.peg.1956; -.

Phylogenomic databases

HOGENOM

P39997; -.

Other

P39997; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glycoprotein; Hydrolase; Membrane; Multifunctional enzyme; Phosphoprotein; Signal-anchor; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 493`	`493`	`Ectonucleotide pyrophosphatase/phosphodiesterase 2.`	`PRO_0000202612`
`TOPO_DOM`	`1 28`	`28`	`Cytoplasmic (Potential).`
`TRANSMEM`	`29 45`	`17`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`46 493`	`448`	`Extracellular (Potential).`
`REGION`	`76 438`	`363`	`Phosphodiesterase.`
`ACT_SITE`	`127 127`		`By similarity.`
`CARBOHYD`	`62 62`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`69 69`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`112 112`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`153 153`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`441 441`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`125 125`		`T -> I (in Ref. 2; AAT92706).`

Sequence information

Length: 493 AA [This is the length of the unprocessed precursor]

Molecular weight: 57355 Da [This is the MW of the unprocessed precursor]

CRC64: 10E67A05C6DEDF09 [This is a checksum on the sequence]

        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

P39997 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools