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Protein

Thiamine-repressible acid phosphatase pho4

Gene

pho4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May dephosphorylate thiamine phosphates.

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691NucleophileBy similarity
Active sitei341 – 3411Proton donorBy similarity

GO - Molecular functioni

  • acid phosphatase activity Source: PomBase

GO - Biological processi

  • dephosphorylation Source: PomBase
  • thiamine biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-repressible acid phosphatase pho4 (EC:3.1.3.2)
Gene namesi
Name:pho4
ORF Names:SPBC428.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC428.03c.
PomBaseiSPBC428.03c.

Subcellular locationi

GO - Cellular componenti

  • cell wall-bounded periplasmic space Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • external side of plasma membrane Source: PomBase
  • extracellular region Source: PomBase
  • fungal-type cell wall Source: PomBase
  • Golgi apparatus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 463445Thiamine-repressible acid phosphatase pho4PRO_0000023952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ01682.
PaxDbiQ01682.

Expressioni

Inductioni

Repressed by thiamine.

Interactioni

Protein-protein interaction databases

BioGridi277132. 12 interactions.
MINTiMINT-4693366.
STRINGi4896.SPBC428.03c-1.

Structurei

3D structure databases

ProteinModelPortaliQ01682.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000115655.
InParanoidiQ01682.
KOiK01078.
OMAiANSLAMY.
OrthoDBiEOG7TQV9N.
PhylomeDBiQ01682.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSGISLWL LAASIVHAGK SQFEAFENEF YFKDHLGTIS VYHEPYFNGP
60 70 80 90 100
TTSFPESCAI KQVHLLQRHG SRNPTGDDTA TDVSSAQYID IFQNKLLNGS
110 120 130 140 150
IPVNFSYPEN PLYFVKHWTP VIKAENADQL SSSGRIELFD LGRQVFERYY
160 170 180 190 200
ELFDTDVYDI NTAAQERVVD SAEWFSYGMF GDDMQNKTNF IVLPEDDSAG
210 220 230 240 250
ANSLAMYYSC PVYEDNNIDE NTTEAAHTSW RNVFLKPIAN RLNKYFDSGY
260 270 280 290 300
NLTVSDVRSL YYICVYEIAL RDNSDFCSLF TPSEFLNFEY DSDLDYAYWG
310 320 330 340 350
GPASEWASTL GGAYVNNLAN NLRKGVNNAS DRKVFLAFTH DSQIIPVEAA
360 370 380 390 400
LGFFPDITPE HPLPTDKNIF TYSLKTSSFV PFAGNLITEL FLCSDNKYYV
410 420 430 440 450
RHLVNQQVYP LTDCGYGPSG ASDGLCELSA YLNSSVRVNS TSNGIANFNS
460
QCQAHSTNVT VYY
Length:463
Mass (Da):52,119
Last modified:July 1, 1993 - v1
Checksum:iF48EAFF8BB6B234A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56939 Genomic DNA. Translation: CAA40258.1.
CU329671 Genomic DNA. Translation: CAA22278.1.
AB027777 Genomic DNA. Translation: BAA87081.1.
PIRiS14119.
RefSeqiNP_595181.1. NM_001021089.2.

Genome annotation databases

EnsemblFungiiSPBC428.03c.1; SPBC428.03c.1:pep; SPBC428.03c.
GeneIDi2540606.
KEGGispo:SPBC428.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56939 Genomic DNA. Translation: CAA40258.1.
CU329671 Genomic DNA. Translation: CAA22278.1.
AB027777 Genomic DNA. Translation: BAA87081.1.
PIRiS14119.
RefSeqiNP_595181.1. NM_001021089.2.

3D structure databases

ProteinModelPortaliQ01682.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277132. 12 interactions.
MINTiMINT-4693366.
STRINGi4896.SPBC428.03c-1.

Proteomic databases

MaxQBiQ01682.
PaxDbiQ01682.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC428.03c.1; SPBC428.03c.1:pep; SPBC428.03c.
GeneIDi2540606.
KEGGispo:SPBC428.03c.

Organism-specific databases

EuPathDBiFungiDB:SPBC428.03c.
PomBaseiSPBC428.03c.

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000115655.
InParanoidiQ01682.
KOiK01078.
OMAiANSLAMY.
OrthoDBiEOG7TQV9N.
PhylomeDBiQ01682.

Miscellaneous databases

NextBioi20801731.
PROiQ01682.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The structural gene coding for thiamin-repressible acid phosphatase in Schizosaccharomyces pombe."
    Yang J., Schweingruber M.E.
    Curr. Genet. 18:269-272(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-30.
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-71.
    Strain: ATCC 38364 / 968.

Entry informationi

Entry nameiPPA2_SCHPO
AccessioniPrimary (citable) accession number: Q01682
Secondary accession number(s): Q9UU70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 27, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.