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Q04119 (PPN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Endopolyphosphatase

EC=3.6.1.10
EC=3.6.1.11
Alternative name(s):
Exopolyphosphatase
Phosphate metabolism protein 5
Gene names
Name:PPN1
Synonyms:PHM5
Ordered Locus Names:YDR452W
ORF Names:D9461.37
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of inorganic polyphosphate (poly P) chains of many hundreds of phosphate residues into shorter lengths. The limited digestion products are 1 and 3 P(i) residues. Ref.1 Ref.4 Ref.6 Ref.7 Ref.12 Ref.13

Catalytic activity

Polyphosphate + n H2O = (n+1) oligophosphate. Ref.4 Ref.13

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate. Ref.4 Ref.13

Cofactor

Metal ions. Manganese is more active than magnesium. Ref.6

Enzyme regulation

Inhibited by heparin and EDTA. Ref.13

Subunit structure

Homotetramer.

Subcellular location

Vacuole membrane; Single-pass type II membrane protein Ref.6 Ref.8 Ref.9 Ref.10 Ref.14.

Domain

The transmembrane domain contains polar residues that mediate the recognition by TUL1.

Post-translational modification

Processing by proteases in the vacuole is required for activation.

Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 and RSP5 are required for ubiquitination. Other cytoplasmic Lys residues than Lys-6 may also be ubiquitinated. Ref.8 Ref.9 Ref.14

N-glycosylated Probable. N-glycosylation is essential for the protease-mediated maturation. Ref.4

Miscellaneous

Inactivation of PPN1 leads to the inhibition of expression of both exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1.

Present with 319 molecules/cell in log phase SD medium.

Biophysicochemical properties

Kinetic parameters:

KM=185 nM for polyP(750) Ref.6

pH dependence:

Optimum pH is about 7.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 8383Removed in mature form
PRO_0000022089
Chain84 – 384301Endopolyphosphatase
PRO_0000022090
Propeptide385 – 674290Removed in mature form
PRO_0000022091

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Signal-anchor for type II membrane protein; Potential
Topological domain43 – 674632Vacuolar Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Potential
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Mutagenesis61K → R or G: Causes accumulation in vacuoles and abolishes sorting into internal vesicles in late endosomes. Ref.8
Mutagenesis111N → A: Abolishes enzyme activity; when associated with A-505 and A-511. Ref.4
Mutagenesis5051N → A: Abolishes enzyme activity; when associated with A-11 and A-511. Ref.4
Mutagenesis5111N → A: Abolishes enzyme activity; when associated with A-11 and A-505. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q04119 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EEC78BC7568098B3

FASTA67478,344
        10         20         30         40         50         60 
MVVVGKSEVR NVSMSRPKKK SLIAILSTCV LFFLVFIIGA KFQYVSVFSK FLDDRGDNES 

        70         80         90        100        110        120 
LQLLNDIEFT RLGLTPREPV IIKDVKTGKE RKLHGRFLHI TDIHPDPYYV EGSSIDAVCH 

       130        140        150        160        170        180 
TGKPSKKKDV APKFGKAMSG CDSPVILMEE TLRWIKENLR DKIDFVIWTG DNIRHDNDRK 

       190        200        210        220        230        240 
HPRTEAQIFD MNNIVADKMT ELFSAGNEED PRDFDVSVIP SLGNNDVFPH NMFALGPTLQ 

       250        260        270        280        290        300 
TREYYRIWKN FVPQQQQRTF DRSASFLTEV IPGKLAVLSI NTLYLFKANP LVDNCNSKKE 

       310        320        330        340        350        360 
PGYQLLLWFG YVLEELRSRG MKVWLSGHVP PIAKNFDQSC YDKFTLWTHE YRDIIIGGLY 

       370        380        390        400        410        420 
GHMNIDHFIP TDGKKARKSL LKAMEQSTRV QQGEDSNEED EETELNRILD HAMAAKEVFL 

       430        440        450        460        470        480 
MGAKPSNKEA YMNTVRDTYY RKVWNKLERV DEKNVENEKK KKEKKDKKKK KPITRKELIE 

       490        500        510        520        530        540 
RYSIVNIGGS VIPTFNPSFR IWEYNITDIV NDSNFAVSEY KPWDEFFESL NKIMEDSLLE 

       550        560        570        580        590        600 
DEMDSSNIEV GINREKMGEK KNKKKKKNDK TMPIEMPDKY ELGPAYVPQL FTPTRFVQFY 

       610        620        630        640        650        660 
ADLEKINQEL HNSFVESKDI FRYEIEYTSD EKPYSMDSLT VGSYLDLAGR LYENKPAWEK 

       670 
YVEWSFASSG YKDD 

« Hide

References

« Hide 'large scale' references
[1]"The endopolyphosphatase gene: essential in Saccharomyces cerevisiae."
Sethuraman A., Rao N.N., Kornberg A.
Proc. Natl. Acad. Sci. U.S.A. 98:8542-8547(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 184-212, FUNCTION, PROTEOLYTIC PROCESSING.
Strain: ATCC 208353 / W303-1A.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Endopolyphosphatase in Saccharomyces cerevisiae undergoes post-translational activations to produce short-chain polyphosphates."
Shi X., Kornberg A.
FEBS Lett. 579:2014-2018(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 84-95 AND 381-384, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASN-11; ASN-505 AND ASN-511.
[5]Kulakovskaya T.V.
Submitted (APR-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 97-126; 184-198; 243-258; 320-334 AND 580-605.
[6]"Endopolyphosphatases for long chain inorganic polyphosphate in yeast and mammals."
Kumble K.D., Kornberg A.
J. Biol. Chem. 271:27146-27151(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis."
Ogawa N., DeRisi J.L., Brown P.O.
Mol. Biol. Cell 11:4309-4321(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting."
Reggiori F., Pelham H.R.B.
EMBO J. 20:5176-5186(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-6, MUTAGENESIS OF LYS-6.
[9]"A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies."
Reggiori F., Pelham H.R.B.
Nat. Cell Biol. 4:117-123(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ROLE OF UBIQUITINATION.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1 in Saccharomyces cerevisiae."
Lichko L., Kulakovskaya T., Kulaev I.
Biochim. Biophys. Acta 1674:98-102(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Purification and properties of exopolyphosphatase from the cytosol of Saccharomyces cerevisiae not encoded by the PPX1 gene."
Andreeva N.A., Kulakovskaya T.V., Kulaev I.S.
Biochemistry (Mosc.) 69:387-393(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[14]"The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies."
Morvan J., Froissard M., Haguenauer-Tsapis R., Urban-Grimal D.
Traffic 5:383-392(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ROLE OF UBIQUITINATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF322107 Genomic DNA. Translation: AAG37278.1.
U33007 Genomic DNA. Translation: AAB64872.1.
BK006938 Genomic DNA. Translation: DAA12287.1.
PIRS69731.
RefSeqNP_010740.3. NM_001180760.3.

3D structure databases

ProteinModelPortalQ04119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32507. 18 interactions.
DIPDIP-2584N.
IntActQ04119. 13 interactions.
MINTMINT-426113.
STRING4932.YDR452W.

Proteomic databases

MaxQBQ04119.
PaxDbQ04119.
PeptideAtlasQ04119.
PRIDEQ04119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR452W; YDR452W; YDR452W.
GeneID852063.
KEGGsce:YDR452W.

Organism-specific databases

CYGDYDR452w.
SGDS000002860. PPN1.

Phylogenomic databases

eggNOGNOG301848.
GeneTreeENSGT00530000063095.
HOGENOMHOG000207139.
KOK06018.
OMATQYFANL.
OrthoDBEOG7RNK7W.

Enzyme and pathway databases

BioCycYEAST:G3O-29983-MONOMER.
BRENDA3.6.1.10. 984.

Gene expression databases

GenevestigatorQ04119.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR012358. EndopolyPtase_N1.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF027093. EndopolyPtase_N1. 1 hit.
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Other

NextBio970343.

Entry information

Entry namePPN1_YEAST
AccessionPrimary (citable) accession number: Q04119
Secondary accession number(s): D6VT77
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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