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Reviewed, UniProtKB/Swiss-Prot P08091 (PPA1_SCHPO)

Last modified September 22, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acid phosphatase
    EC=3.1.3.2
Gene names
Name: pho1
ORF Names: SPBP4G3.02
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Subcellular location

Secretedcell wall.

Induction

Repressed by phosphate and weakly by thiamine.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay. Source: GeneDB_SPombe

external side of plasma membrane

Non-traceable author statement. Source: GeneDB_SPombe

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

longitudinal side of cell surface

Traceable author statement. Source: GeneDB_SPombe

   Molecular functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 453435Acid phosphatase
PRO_0000023951

Sites

Active site691Nucleophile By similarity
Active site3311Proton donor By similarity

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation3191N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P08091-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 7CF891256EB154D1

FASTA45350,557
        10         20         30         40         50         60 
MFLQNLFLGF LAVVCANAQF AEFTAFDGKF DFKEHLTSRS PYHKPYFYGP SIDFPTTCKI 

        70         80         90        100        110        120 
KQVHTLQRHG SRNPTGGNAA FDAVGIANFQ QRLLNGSVPI DYSVSGNPLS FVPTWTPVIE 

       130        140        150        160        170        180 
AANADALSSS GRVELFDMGR QFYERYHELF NASTYNIYTA AQQRVVDSAL WYGYGMFGED 

       190        200        210        220        230        240 
VHNFTNYILV SENATAGSNS LSSYNACPAS DADDFTTPAL EAWRNVYMPP IRQRLNPYFS 

       250        260        270        280        290        300 
NYNLTNDDIL NLYGICSYEI ALQDYSEFCK LFNSVDFLNF EYEGDLSFSY GMGNSVKWGS 

       310        320        330        340        350        360 
IFGGAYANSL ANSLRSVENN TQQVFFAFTH DANIIPVETA LGFFTDNTPE NPLPTSYQVH 

       370        380        390        400        410        420 
SHSMKASEFV PFAGNLITEL FQCEDSKYYV RHLVNEEVFP LSDCGFGPSN TSDGMCELYA 

       430        440        450 
YLNSPVRVNG TSNGIQNFDT LCNASAVAAV YPY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of the structural gene for secreted acid phosphatase from Schizosaccharomyces pombe."
Elliott S., Chang C., Schweingruber M.E., Schaller J., Rickli E.E., Carbon J.
J. Biol. Chem. 261:2936-2941(1986) [PubMed: 3005272] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

M11857 Genomic DNA. Translation: AAA35321.1.
CU329671 Genomic DNA. Translation: CAB68657.1.
PIRA25326.
RefSeqNP_596847.1.

3D structure databases

HSSPHSSP built from PDB template 1QFX based on UniProtKB P34755.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08091.

Genome annotation databases

GeneID2541339.
GenomeReviewsGene locus pho1 in contig CU329671_GR.
KEGGspo:SPBP4G3.02.
NMPDRfig|4896.1.peg.2713.

Organism-specific databases

GeneDB_SpombeSPBP4G3.02.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004819-MON.
BRENDA3.1.3.2. 653.

Gene expression databases

ArrayExpressP08091.

Family and domain databases

InterProIPR000560. Histidine_acid_Pase.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. Acid_phosphat_A. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPA1_SCHPO
AccessionPrimary (citable) accession number: P08091
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 22, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents