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Protein

Peroxisomal membrane protein PEX25

Gene

PEX25

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for regulation of peroxisome size and maintenance. Has a role in the import of peroxisomal matrix proteins. Imports RHO1 into the peroxisome. Also promotes peroxisome division and biogenesis.5 Publications

GO - Biological processi

  1. peroxisome fission Source: UniProtKB
  2. peroxisome organization Source: SGD
  3. protein import into peroxisome matrix Source: SGD
  4. regulation of peroxisome size Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Peroxisome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-34013-MONOMER.

Protein family/group databases

TCDBi3.A.20.1.5. the peroxisomal protein importer (ppi) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal membrane protein PEX25
Alternative name(s):
Peroxin-25
Gene namesi
Name:PEX25
Ordered Locus Names:YPL112C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL112c.
SGDiS000006033. PEX25.

Subcellular locationi

Peroxisome membrane 4 Publications; Single-pass membrane protein 4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 366366CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei367 – 38317HelicalSequence AnalysisAdd
BLAST
Topological domaini384 – 39411LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of peroxisomal membrane Source: InterPro
  2. peroxisomal membrane Source: SGD
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Peroxisomal membrane protein PEX25PRO_0000270568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei289 – 2891Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02969.
PaxDbiQ02969.
PeptideAtlasiQ02969.

Expressioni

Gene expression databases

GenevestigatoriQ02969.

Interactioni

Subunit structurei

Homooligomer. Interacts with PEX27 and PEX34.3 Publications

Protein-protein interaction databases

BioGridi36068. 26 interactions.
DIPiDIP-5292N.
IntActiQ02969. 5 interactions.
MINTiMINT-504153.
STRINGi4932.YPL112C.

Structurei

3D structure databases

ProteinModelPortaliQ02969.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40921.
HOGENOMiHOG000066022.
InParanoidiQ02969.
OMAiYGIMDEL.
OrthoDBiEOG7PCJS4.

Family and domain databases

InterProiIPR008733. PEX11.
[Graphical view]
PfamiPF05648. PEX11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQFGTTDIV SGSETPPYSG ASYQDAQDDN THPHSSDAGA EKFSAGSGSE
60 70 80 90 100
SHTESSRSDD EDSQAKTKMV DNITILKYIL DSLSGRDKLA KIIKYALDIL
110 120 130 140 150
KLFIEKSKRN LTVLDPSVLT YYTKILKNLT VKVALRHPIT VIKVLLLSLL
160 170 180 190 200
RNFDKKIDFI SQQLSTFRYI LRFGGTPFRV CSFLGKFNKT RKCNFQIDQI
210 220 230 240 250
KKIWFNEASL REFLDLYYGI FDELDLLYKL KIWTNKSFYS FVSRQESLAW
260 270 280 290 300
QYDILLSLKD HWLNLQSLQK RQLELEVQLK VQNNALLLSP ILMHQAHKDD
310 320 330 340 350
GSQSPIRKQL LNDLNVNNDA EVLIHKQLKA IKDEKTLVYL DIARLSFDCM
360 370 380 390
ANTSDILNLK TPKGTYAVLS LGSGLTGLVK LWITTKRSLC SSKD
Length:394
Mass (Da):44,911
Last modified:November 1, 1996 - v1
Checksum:iA453AF4B5E41DB68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81D → N in AAT92840 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43503 Genomic DNA. Translation: AAB68249.1.
AY692821 Genomic DNA. Translation: AAT92840.1.
BK006949 Genomic DNA. Translation: DAA11321.1.
PIRiS62009.
RefSeqiNP_015213.1. NM_001183926.1.

Genome annotation databases

EnsemblFungiiYPL112C; YPL112C; YPL112C.
GeneIDi855991.
KEGGisce:YPL112C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43503 Genomic DNA. Translation: AAB68249.1.
AY692821 Genomic DNA. Translation: AAT92840.1.
BK006949 Genomic DNA. Translation: DAA11321.1.
PIRiS62009.
RefSeqiNP_015213.1. NM_001183926.1.

3D structure databases

ProteinModelPortaliQ02969.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36068. 26 interactions.
DIPiDIP-5292N.
IntActiQ02969. 5 interactions.
MINTiMINT-504153.
STRINGi4932.YPL112C.

Protein family/group databases

TCDBi3.A.20.1.5. the peroxisomal protein importer (ppi) family.

Proteomic databases

MaxQBiQ02969.
PaxDbiQ02969.
PeptideAtlasiQ02969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL112C; YPL112C; YPL112C.
GeneIDi855991.
KEGGisce:YPL112C.

Organism-specific databases

CYGDiYPL112c.
SGDiS000006033. PEX25.

Phylogenomic databases

eggNOGiNOG40921.
HOGENOMiHOG000066022.
InParanoidiQ02969.
OMAiYGIMDEL.
OrthoDBiEOG7PCJS4.

Enzyme and pathway databases

BioCyciYEAST:G3O-34013-MONOMER.

Miscellaneous databases

NextBioi980843.

Gene expression databases

GenevestigatoriQ02969.

Family and domain databases

InterProiIPR008733. PEX11.
[Graphical view]
PfamiPF05648. PEX11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis."
    Rottensteiner H., Stein K., Sonnenhol E., Erdmann R.
    Mol. Biol. Cell 14:4316-4328(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 56-70 AND 337-354, FUNCTION, SUBUNIT, INTERACTION WITH PEX27, SUBCELLULAR LOCATION.
    Strain: ATCC 201389 / BY4742.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Pex11-related proteins in peroxisome dynamics: a role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae."
    Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M., Aitchison J.D., Rachubinski R.A.
    Mol. Biol. Cell 14:4089-4102(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PEX27.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane."
    Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H., Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R., Rachubinski R.A., Aitchison J.D.
    J. Cell Biol. 167:1099-1112(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "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-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The peroxin Pex34p functions with the Pex11 family of peroxisomal divisional proteins to regulate the peroxisome population in yeast."
    Tower R.J., Fagarasanu A., Aitchison J.D., Rachubinski R.A.
    Mol. Biol. Cell 22:1727-1738(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PEX34.

Entry informationi

Entry nameiPEX25_YEAST
AccessioniPrimary (citable) accession number: Q02969
Secondary accession number(s): D6W3Q5, Q6B2A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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.