Endopolyphosphatase (Q04119)

Identification
NameEndopolyphosphatase
Synonyms
  • Exopolyphosphatase
  • Phosphate metabolism protein 5
Gene NamePPN1
Enzyme Class
Biological Properties
General FunctionInvolved in endopolyphosphatase activity
Specific FunctionCatalyzes 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
Cellular LocationVacuole membrane; Single-pass type II membrane protein
SMPDB PathwaysNot Available
KEGG Pathways
Purine metabolismec00230 Map00230
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00907phosphateShow
GO Classification
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
vacuole
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
endopolyphosphatase activity
Process
Not Available
Gene Properties
Chromosome Locationchromosome 4
LocusYDR452W
Gene Sequence>2025 bp ATGGTTGTAGTGGGTAAGAGTGAAGTGCGCAATGTAAGCATGAGTAGGCCGAAGAAGAAA TCATTGATTGCCATCCTGTCGACCTGTGTTTTGTTTTTCCTCGTGTTTATAATTGGTGCT AAATTTCAATATGTTTCCGTTTTCTCCAAATTCTTAGATGACAGGGGGGACAACGAGTCA CTTCAATTGCTCAATGACATAGAATTTACAAGGCTAGGACTGACACCTAGGGAGCCAGTA ATTATCAAAGACGTAAAGACAGGGAAGGAGAGAAAATTACATGGACGGTTCCTTCATATT ACCGATATTCATCCTGACCCTTATTATGTGGAAGGAAGCTCTATTGATGCAGTTTGTCAC ACAGGAAAACCAAGCAAAAAAAAGGATGTGGCACCCAAGTTTGGGAAGGCAATGTCTGGA TGTGATTCTCCCGTTATTTTAATGGAAGAAACTCTGAGATGGATTAAAGAAAATCTTAGA GATAAGATTGATTTTGTCATTTGGACGGGTGATAATATCAGACATGACAATGACCGGAAA CATCCAAGAACAGAAGCACAAATTTTTGATATGAACAATATCGTTGCTGATAAAATGACA GAATTATTTAGTGCTGGCAATGAAGAAGATCCAAGAGATTTTGATGTGTCTGTCATTCCA AGTCTTGGAAACAATGATGTCTTTCCACATAACATGTTTGCACTAGGACCAACTCTACAA ACTAGAGAATATTATAGGATTTGGAAAAATTTTGTTCCGCAGCAGCAGCAAAGAACTTTT GATAGGAGTGCTTCATTTTTGACTGAAGTTATTCCAGGGAAGCTTGCTGTCCTGTCAATT AACACGCTGTACTTATTCAAGGCCAATCCGTTAGTTGACAATTGTAATTCAAAAAAAGAA CCAGGTTACCAACTTTTACTTTGGTTCGGTTATGTATTAGAAGAACTAAGGAGTAGGGGA ATGAAAGTATGGTTAAGTGGACATGTACCTCCAATCGCAAAAAATTTCGATCAGTCGTGC TACGATAAGTTCACGCTATGGACTCACGAATACAGGGATATAATCATTGGAGGATTATAC GGTCACATGAATATTGACCACTTCATCCCAACGGATGGTAAAAAAGCTAGAAAATCGTTA TTGAAAGCCATGGAGCAATCCACTCGTGTTCAACAAGGAGAAGACAGTAATGAAGAGGAC GAAGAAACTGAATTGAATAGAATTCTGGATCACGCTATGGCGGCAAAAGAAGTTTTTTTA ATGGGAGCGAAACCATCTAACAAAGAAGCATATATGAACACCGTCCGCGACACATACTAT CGGAAAGTGTGGAATAAGCTGGAAAGAGTGGATGAAAAAAATGTTGAAAATGAGAAGAAA AAGAAAGAAAAGAAGGACAAAAAAAAGAAAAAGCCAATCACTAGAAAAGAGCTCATTGAA CGCTATTCCATTGTGAACATAGGTGGTTCAGTCATTCCAACTTTCAATCCTTCCTTTAGG ATCTGGGAATATAACATCACCGACATAGTGAATGACTCCAATTTTGCAGTTTCGGAGTAT AAGCCCTGGGATGAATTTTTCGAGTCACTAAATAAGATTATGGAAGACTCTTTGCTAGAA GATGAAATGGACAGCAGTAATATCGAGGTTGGGATCAACCGCGAGAAGATGGGCGAAAAG AAAAACAAGAAGAAAAAGAAAAATGACAAGACTATGCCAATTGAGATGCCAGACAAATAC GAACTCGGCCCTGCATATGTACCGCAGTTATTCACTCCGACGCGTTTCGTCCAATTCTAC GCCGACTTGGAAAAAATCAATCAAGAATTACATAATTCATTTGTTGAATCTAAGGATATT TTCAGGTATGAGATAGAATATACCTCAGACGAGAAACCATACTCAATGGATTCGTTAACA GTAGGAAGTTATTTGGATCTTGCAGGCAGATTATACGAAAACAAACCTGCATGGGAAAAA TACGTCGAATGGTCATTTGCGTCTTCTGGATATAAAGATGATTAA
Protein Properties
Pfam Domain Function
Protein Residues674
Protein Molecular Weight78343.70313
Protein Theoretical pI6.85
Signalling Regions
  • None
Transmembrane Regions
  • 22-42
Protein Sequence>Endopolyphosphatase MVVVGKSEVRNVSMSRPKKKSLIAILSTCVLFFLVFIIGAKFQYVSVFSKFLDDRGDNES LQLLNDIEFTRLGLTPREPVIIKDVKTGKERKLHGRFLHITDIHPDPYYVEGSSIDAVCH TGKPSKKKDVAPKFGKAMSGCDSPVILMEETLRWIKENLRDKIDFVIWTGDNIRHDNDRK HPRTEAQIFDMNNIVADKMTELFSAGNEEDPRDFDVSVIPSLGNNDVFPHNMFALGPTLQ TREYYRIWKNFVPQQQQRTFDRSASFLTEVIPGKLAVLSINTLYLFKANPLVDNCNSKKE PGYQLLLWFGYVLEELRSRGMKVWLSGHVPPIAKNFDQSCYDKFTLWTHEYRDIIIGGLY GHMNIDHFIPTDGKKARKSLLKAMEQSTRVQQGEDSNEEDEETELNRILDHAMAAKEVFL MGAKPSNKEAYMNTVRDTYYRKVWNKLERVDEKNVENEKKKKEKKDKKKKKPITRKELIE RYSIVNIGGSVIPTFNPSFRIWEYNITDIVNDSNFAVSEYKPWDEFFESLNKIMEDSLLE DEMDSSNIEVGINREKMGEKKNKKKKKNDKTMPIEMPDKYELGPAYVPQLFTPTRFVQFY ADLEKINQELHNSFVESKDIFRYEIEYTSDEKPYSMDSLTVGSYLDLAGRLYENKPAWEK YVEWSFASSGYKDD
References
External Links
ResourceLink
Saccharomyces Genome Database PPN1
Uniprot IDQ04119
Uniprot NamePPN1_YEAST
GenBank Gene IDAF322107
Genebank Protein ID11528443
General Reference
  • Sethuraman, A., Rao, N. N., Kornberg, A. (2001). "The endopolyphosphatase gene: essential in Saccharomyces cerevisiae." Proc Natl Acad Sci U S A 98:8542-8547.11447286
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Shi, X., Kornberg, A. (2005). "Endopolyphosphatase in Saccharomyces cerevisiae undergoes post-translational activations to produce short-chain polyphosphates." FEBS Lett 579:2014-2018.15792812
  • Kumble, K. D., Kornberg, A. (1996). "Endopolyphosphatases for long chain inorganic polyphosphate in yeast and mammals." J Biol Chem 271:27146-27151.8900207
  • Ogawa, N., DeRisi, J., Brown, P. O. (2000). "New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis." Mol Biol Cell 11:4309-4321.11102525
  • Reggiori, F., Pelham, H. R. (2001). "Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting." EMBO J 20:5176-5186.11566881
  • Reggiori, F., Pelham, H. R. (2002). "A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies." Nat Cell Biol 4:117-123.11788821
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Lichko, L., Kulakovskaya, T., Kulaev, I. (2004). "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." Biochim Biophys Acta 1674:98-102.15342119
  • Andreeva, N. A., Kulakovskaya, T. V., Kulaev, I. S. (2004). "Purification and properties of exopolyphosphatase from the cytosol of Saccharomyces cerevisiae not encoded by the PPX1 gene." Biochemistry (Mosc) 69:387-393.15170373
  • Morvan, J., Froissard, M., Haguenauer-Tsapis, R., Urban-Grimal, D. (2004). "The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies." Traffic 5:383-392.15086787
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956