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P11491 (PPB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 119. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Repressible alkaline phosphatase
EC=3.1.3.1
Alternative name(s):
Membrane-bound repressible alkaline phosphatase

Cleaved into the following chain:

  1. Soluble alkaline phosphatase
    EC=3.1.7.6
    Alternative name(s):
    Farnesyl diphosphatase
Gene names
Name:PHO8
Ordered Locus Names:YDR481C
ORF Names:D8035.24
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 length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphatase with broad substrate specificity. A truncated (soluble) version of the protein is responsible for the production of (E,E)-farnesol from (E,E)-farnesyl diphosphate.

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.6

(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate. Ref.6

Cofactor

Binds 1 magnesium ion By similarity.

Binds 2 zinc ions By similarity.

Subcellular location

Repressible alkaline phosphatase: Vacuole membrane; Single-pass membrane protein. Note: The full-length version is found in lysosome-like vacuoles. Ref.5

Soluble alkaline phosphatase: Cytoplasm. Note: The truncated version of the protein is soluble. Ref.5

Miscellaneous

Present with 3060 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the alkaline phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0 for farnesyl diphosphatase activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Repressible alkaline phosphatasePRO_0000024017
Chain63 – ?Soluble alkaline phosphatasePRO_0000401198
Propeptide? – 566Removed in mature formPRO_0000024018

Regions

Topological domain1 – 3333Cytoplasmic Ref.5
Transmembrane34 – 5926Helical; Potential
Topological domain60 – ?Vacuolar Ref.5

Sites

Active site1231Phosphoserine intermediate By similarity
Metal binding751Magnesium By similarity
Metal binding751Zinc 2 By similarity
Metal binding1741Magnesium By similarity
Metal binding1761Magnesium By similarity
Metal binding3251Magnesium By similarity
Metal binding3301Zinc 1 By similarity
Metal binding3341Zinc 1 By similarity
Metal binding3731Zinc 2 By similarity
Metal binding3741Zinc 2 By similarity
Metal binding4841Zinc 1 By similarity

Amino acid modifications

Modified residue1211Phosphothreonine Ref.9
Modified residue1231Phosphoserine Ref.8 Ref.9
Modified residue1281Phosphothreonine Ref.9
Glycosylation2681N-linked (GlcNAc...)
Glycosylation4011N-linked (GlcNAc...)

Experimental info

Sequence conflict51T → R in AAA34871. Ref.1
Sequence conflict551S → T in AAA34871. Ref.1
Sequence conflict591L → I in AAA34871. Ref.1
Sequence conflict1321C → S in AAA34871. Ref.1
Sequence conflict2711L → F in AAA34871. Ref.1
Sequence conflict3281R → G in AAU09711. Ref.4
Sequence conflict4471D → E in AAA34871. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P11491 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 9FA2E87B068FF0DB

FASTA56663,004
        10         20         30         40         50         60 
MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ LAFPSSFALR 

        70         80         90        100        110        120 
SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI LTLDEHFIGS SRTRSSDSLV 

       130        140        150        160        170        180 
TDSAAGATAF ACALKSYNGA IGVDPHHRPC GTVLEAAKLA GYLTGLVVTT RITDATPASF 

       190        200        210        220        230        240 
SSHVDYRWQE DLIATHQLGE YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL 

       250        260        270        280        290        300 
IDEAQSNGWQ YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV 

       310        320        330        340        350        360 
KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE AFQYVLEFAE 

       370        380        390        400        410        420 
NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA NATHSGEFLK RKLVDFVHEH 

       430        440        450        460        470        480 
KGASSKIENF IKHEILEKDL GIYDYTDSDL ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT 

       490        500        510        520        530        540 
THGHSAVDVN IYAYANKKAT WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK 

       550        560 
HTSDFDATEI ASEVQHYDEY YHELTN

« Hide

References

« Hide 'large scale' references
[1]"Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae."
Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.
Gene 58:137-148(1987) [PubMed: 3319783] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: P-28-24C.
[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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase."
Klionsky D.J., Emr S.D.
EMBO J. 8:2241-2250(1989) [PubMed: 2676517] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, TOPOLOGY, SUBCELLULAR LOCATION.
[6]"A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E,E-farnesol."
Song L.
Appl. Biochem. Biotechnol. 128:149-158(2006) [PubMed: 16484724] [Abstract]
Cited for: PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL DIPHOSPHATASE, PH DEPENDENCE.
[7]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, MASS SPECTROMETRY.
Strain: ADR376.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123 AND THR-128, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M21134 Genomic DNA. Translation: AAA34871.1.
U33050 Genomic DNA. Translation: AAB64930.1.
AY723794 Genomic DNA. Translation: AAU09711.1.
BK006938 Genomic DNA. Translation: DAA12314.1.
PIRS69648.
RefSeqNP_010769.1. NM_001180789.1.

3D structure databases

ProteinModelPortalP11491.
SMRP11491. Positions 68-526.
ModBaseSearch...

Protein-protein interaction databases

IntActP11491. 2 interactions.
MINTMINT-4482897.
STRINGP11491.

Proteomic databases

PeptideAtlasP11491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR481C; YDR481C; YDR481C.
GeneID852092.
KEGGsce:YDR481C.
NMPDRfig|4932.3.peg.1542.

Organism-specific databases

CYGDYDR481c.
SGDS000002889. PHO8.

Phylogenomic databases

eggNOGfuNOG04370.
HOGENOMHBG617166.
OMAGYNTTPV.
OrthoDBEOG41VPBB.

Gene expression databases

ArrayExpressP11491.
GenevestigatorP11491.
GermOnlineYDR481C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
KOK01077.
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970421.

Entry information

Entry namePPB_YEAST
AccessionPrimary (citable) accession number: P11491
Secondary accession number(s): D6VTA4, E9P949, Q03374
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: December 14, 2011
This is version 119 of the entry and version 2 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

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