PEX25_YEAST
ID PEX25_YEAST Reviewed; 394 AA.
AC Q02969; D6W3Q5; Q6B2A9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Peroxisomal membrane protein PEX25;
DE AltName: Full=Peroxin-25;
GN Name=PEX25; OrderedLocusNames=YPL112C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 56-70 AND 337-354, FUNCTION, SUBUNIT, INTERACTION WITH
RP PEX27, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201389 / BY4742;
RX PubMed=14517338; DOI=10.1091/mbc.e03-03-0153;
RA Rottensteiner H., Stein K., Sonnenhol E., Erdmann R.;
RT "Conserved function of pex11p and the novel pex25p and pex27p in peroxisome
RT biogenesis.";
RL Mol. Biol. Cell 14:4316-4328(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12135984; DOI=10.1083/jcb.200204059;
RA Smith J.J., Marelli M., Christmas R.H., Vizeacoumar F.J., Dilworth D.J.,
RA Ideker T., Galitski T., Dimitrov K., Rachubinski R.A., Aitchison J.D.;
RT "Transcriptome profiling to identify genes involved in peroxisome assembly
RT and function.";
RL J. Cell Biol. 158:259-271(2002).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH PEX27.
RX PubMed=14517321; DOI=10.1091/mbc.e03-03-0150;
RA Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M.,
RA Aitchison J.D., Rachubinski R.A.;
RT "Pex11-related proteins in peroxisome dynamics: a role for the novel
RT peroxin Pex27p in controlling peroxisome size and number in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 14:4089-4102(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15596542; DOI=10.1083/jcb.200404119;
RA Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H.,
RA Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R.,
RA Rachubinski R.A., Aitchison J.D.;
RT "Quantitative mass spectrometry reveals a role for the GTPase Rho1p in
RT actin organization on the peroxisome membrane.";
RL J. Cell Biol. 167:1099-1112(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH PEX34.
RX PubMed=21441307; DOI=10.1091/mbc.e11-01-0084;
RA Tower R.J., Fagarasanu A., Aitchison J.D., Rachubinski R.A.;
RT "The peroxin Pex34p functions with the Pex11 family of peroxisomal
RT divisional proteins to regulate the peroxisome population in yeast.";
RL Mol. Biol. Cell 22:1727-1738(2011).
CC -!- FUNCTION: Required for regulation of peroxisome size and maintenance.
CC Has a role in the import of peroxisomal matrix proteins. Imports RHO1
CC into the peroxisome. Also promotes peroxisome division and biogenesis.
CC {ECO:0000269|PubMed:12135984, ECO:0000269|PubMed:14517321,
CC ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:15596542,
CC ECO:0000269|PubMed:21441307}.
CC -!- SUBUNIT: Homooligomer. Interacts with PEX27 and PEX34.
CC {ECO:0000269|PubMed:14517321, ECO:0000269|PubMed:14517338,
CC ECO:0000269|PubMed:21441307}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:12135984,
CC ECO:0000269|PubMed:14517338, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15596542}; Single-pass membrane protein
CC {ECO:0000269|PubMed:12135984, ECO:0000269|PubMed:14517338,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15596542}.
CC -!- MISCELLANEOUS: Present with 2420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U43503; AAB68249.1; -; Genomic_DNA.
DR EMBL; AY692821; AAT92840.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11321.1; -; Genomic_DNA.
DR PIR; S62009; S62009.
DR RefSeq; NP_015213.1; NM_001183926.1.
DR AlphaFoldDB; Q02969; -.
DR BioGRID; 36068; 74.
DR DIP; DIP-5292N; -.
DR IntAct; Q02969; 6.
DR MINT; Q02969; -.
DR STRING; 4932.YPL112C; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q02969; -.
DR MaxQB; Q02969; -.
DR PaxDb; Q02969; -.
DR PRIDE; Q02969; -.
DR EnsemblFungi; YPL112C_mRNA; YPL112C; YPL112C.
DR GeneID; 855991; -.
DR KEGG; sce:YPL112C; -.
DR SGD; S000006033; PEX25.
DR VEuPathDB; FungiDB:YPL112C; -.
DR eggNOG; ENOG502R7FJ; Eukaryota.
DR HOGENOM; CLU_043324_0_0_1; -.
DR InParanoid; Q02969; -.
DR OMA; IDLYYGI; -.
DR BioCyc; YEAST:G3O-34013-MON; -.
DR PRO; PR:Q02969; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02969; protein.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IEA:InterPro.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:SGD.
DR GO; GO:0044375; P:regulation of peroxisome size; IDA:UniProtKB.
DR InterPro; IPR008733; PEX11.
DR Pfam; PF05648; PEX11; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Peroxisome; Peroxisome biogenesis;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..394
FT /note="Peroxisomal membrane protein PEX25"
FT /id="PRO_0000270568"
FT TOPO_DOM 1..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..394
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 8
FT /note="D -> N (in Ref. 3; AAT92840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 44911 MW; A453AF4B5E41DB68 CRC64;
MSQFGTTDIV SGSETPPYSG ASYQDAQDDN THPHSSDAGA EKFSAGSGSE SHTESSRSDD
EDSQAKTKMV DNITILKYIL DSLSGRDKLA KIIKYALDIL KLFIEKSKRN LTVLDPSVLT
YYTKILKNLT VKVALRHPIT VIKVLLLSLL RNFDKKIDFI SQQLSTFRYI LRFGGTPFRV
CSFLGKFNKT RKCNFQIDQI KKIWFNEASL REFLDLYYGI FDELDLLYKL KIWTNKSFYS
FVSRQESLAW QYDILLSLKD HWLNLQSLQK RQLELEVQLK VQNNALLLSP ILMHQAHKDD
GSQSPIRKQL LNDLNVNNDA EVLIHKQLKA IKDEKTLVYL DIARLSFDCM ANTSDILNLK
TPKGTYAVLS LGSGLTGLVK LWITTKRSLC SSKD
