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P11491

- PPB_YEAST

UniProt

P11491 - PPB_YEAST

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Protein
Repressible alkaline phosphatase
Gene
PHO8, YDR481C, D8035.24
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Acts as a fructose-2,6-bisphosphate 6-phosphatase (1 Publication).1 Publication

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.1 Publication
(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate.1 Publication
Beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructofuranose 2-phosphate + phosphate.1 Publication

Cofactori

Binds 1 magnesium ion By similarity.
Binds 2 zinc ions By similarity.

pH dependencei

Optimum pH is 7.0 for farnesyl diphosphatase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi75 – 751Magnesium By similarity
Metal bindingi75 – 751Zinc 2 By similarity
Active sitei123 – 1231Phosphoserine intermediate By similarity
Metal bindingi174 – 1741Magnesium By similarity
Metal bindingi176 – 1761Magnesium By similarity
Metal bindingi325 – 3251Magnesium By similarity
Metal bindingi330 – 3301Zinc 1 By similarity
Metal bindingi334 – 3341Zinc 1 By similarity
Metal bindingi373 – 3731Zinc 2 By similarity
Metal bindingi374 – 3741Zinc 2 By similarity
Metal bindingi484 – 4841Zinc 1 By similarity

GO - Molecular functioni

  1. alkaline phosphatase activity Source: SGD
  2. fructose-2,6-bisphosphate 6-phosphatase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. nicotinamide nucleotide metabolic process Source: SGD
  2. protein dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16788.
YEAST:YDR481C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Repressible alkaline phosphatase (EC:3.1.3.1)
Alternative name(s):
Fructose-2,6-bisphosphate 6-phosphatase (EC:3.1.3.54)
Membrane-bound repressible alkaline phosphatase
Cleaved into the following chain:
Alternative name(s):
Farnesyl diphosphatase
Gene namesi
Name:PHO8
Ordered Locus Names:YDR481C
ORF Names:D8035.24
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR481c.
SGDiS000002889. PHO8.

Subcellular locationi

Chain Repressible alkaline phosphatase : Vacuole membrane; Single-pass membrane protein
Note: The full-length version is found in lysosome-like vacuoles.1 Publication
Chain Soluble alkaline phosphatase : Cytoplasm
Note: The truncated version of the protein is soluble.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333Cytoplasmic1 Publication
Add
BLAST
Transmembranei34 – 5926Helical; Reviewed prediction
Add
BLAST
Topological domaini60 – ?Vacuolar1 Publication

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 566Removed in mature formPRO_0000024018
Chaini1 – ?Repressible alkaline phosphatasePRO_0000024017
Chaini63 – ?Soluble alkaline phosphatasePRO_0000401198

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231Phosphoserine3 Publications
Glycosylationi268 – 2681N-linked (GlcNAc...)
Glycosylationi401 – 4011N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11491.
PaxDbiP11491.
PeptideAtlasiP11491.

Expressioni

Gene expression databases

GenevestigatoriP11491.

Interactioni

Protein-protein interaction databases

BioGridi32533. 21 interactions.
IntActiP11491. 2 interactions.
MINTiMINT-4482897.

Structurei

3D structure databases

ProteinModelPortaliP11491.
SMRiP11491. Positions 67-525.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1785.
GeneTreeiENSGT00390000008704.
HOGENOMiHOG000099116.
KOiK01077.
OMAiLKSYNGA.
OrthoDBiEOG71K6C1.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11491-1 [UniParc]FASTAAdd to Basket

« Hide

MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ    50
LAFPSSFALR SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI 100
LTLDEHFIGS SRTRSSDSLV TDSAAGATAF ACALKSYNGA IGVDPHHRPC 150
GTVLEAAKLA GYLTGLVVTT RITDATPASF SSHVDYRWQE DLIATHQLGE 200
YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL IDEAQSNGWQ 250
YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV 300
KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE 350
AFQYVLEFAE NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA 400
NATHSGEFLK RKLVDFVHEH KGASSKIENF IKHEILEKDL GIYDYTDSDL 450
ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT THGHSAVDVN IYAYANKKAT 500
WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK HTSDFDATEI 550
ASEVQHYDEY YHELTN 566
Length:566
Mass (Da):63,004
Last modified:July 15, 1998 - v2
Checksum:i9FA2E87B068FF0DB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51T → R in AAA34871. 1 Publication
Sequence conflicti55 – 551S → T in AAA34871. 1 Publication
Sequence conflicti59 – 591L → I in AAA34871. 1 Publication
Sequence conflicti132 – 1321C → S in AAA34871. 1 Publication
Sequence conflicti271 – 2711L → F in AAA34871. 1 Publication
Sequence conflicti328 – 3281R → G in AAU09711. 1 Publication
Sequence conflicti447 – 4471D → E in AAA34871. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21134 Genomic DNA. Translation: AAA34871.1.
U33050 Genomic DNA. Translation: AAB64930.1.
AY723794 Genomic DNA. Translation: AAU09711.1.
BK006938 Genomic DNA. Translation: DAA12314.1.
PIRiS69648.
RefSeqiNP_010769.3. NM_001180789.3.

Genome annotation databases

EnsemblFungiiYDR481C; YDR481C; YDR481C.
GeneIDi852092.
KEGGisce:YDR481C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21134 Genomic DNA. Translation: AAA34871.1 .
U33050 Genomic DNA. Translation: AAB64930.1 .
AY723794 Genomic DNA. Translation: AAU09711.1 .
BK006938 Genomic DNA. Translation: DAA12314.1 .
PIRi S69648.
RefSeqi NP_010769.3. NM_001180789.3.

3D structure databases

ProteinModelPortali P11491.
SMRi P11491. Positions 67-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32533. 21 interactions.
IntActi P11491. 2 interactions.
MINTi MINT-4482897.

Proteomic databases

MaxQBi P11491.
PaxDbi P11491.
PeptideAtlasi P11491.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR481C ; YDR481C ; YDR481C .
GeneIDi 852092.
KEGGi sce:YDR481C.

Organism-specific databases

CYGDi YDR481c.
SGDi S000002889. PHO8.

Phylogenomic databases

eggNOGi COG1785.
GeneTreei ENSGT00390000008704.
HOGENOMi HOG000099116.
KOi K01077.
OMAi LKSYNGA.
OrthoDBi EOG71K6C1.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16788.
YEAST:YDR481C-MONOMER.

Miscellaneous databases

NextBioi 970421.

Gene expression databases

Genevestigatori P11491.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view ]
Pfami PF00245. Alk_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00113. ALKPHPHTASE.
SMARTi SM00098. alkPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 2 hits.
PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL DIPHOSPHATASE, PH DEPENDENCE.
  7. "Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase."
    Plankert U., Purwin C., Holzer H.
    Eur. J. Biochem. 196:191-196(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPPB_YEAST
AccessioniPrimary (citable) accession number: P11491
Secondary accession number(s): D6VTA4, E9P949, Q03374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: May 14, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi