PEX15_YEAST
ID PEX15_YEAST Reviewed; 383 AA.
AC Q08215; D6W222;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Peroxisomal membrane protein PEX15;
DE AltName: Full=Peroxin-15;
DE AltName: Full=Peroxisome biosynthesis protein PAS21;
GN Name=PEX15; Synonyms=PAS21; OrderedLocusNames=YOL044W;
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 [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND TOPOLOGY.
RX PubMed=9405362; DOI=10.1093/emboj/16.24.7326;
RA Elgersma Y., Kwast L., van den Berg M., Snyder W.B., Distel B.,
RA Subramani S., Tabak H.F.;
RT "Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane
RT protein required for peroxisome assembly in S.cerevisiae, causes
RT proliferation of the endoplasmic reticulum membrane.";
RL EMBO J. 16:7326-7341(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH PEX6, AND MUTAGENESIS OF LEU-22; GLN-47 AND
RP VAL-50.
RX PubMed=12808025; DOI=10.1091/mbc.e02-11-0752;
RA Birschmann I., Stroobants A.K., van den Berg M., Schaefer A.,
RA Rosenkranz K., Kunau W.-H., Tabak H.F.;
RT "Pex15p of Saccharomyces cerevisiae provides a molecular basis for
RT recruitment of the AAA peroxin Pex6p to peroxisomal membranes.";
RL Mol. Biol. Cell 14:2226-2236(2003).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH PEX19, AND PEROXISOMAL SUBCELLULAR LOCATION.
RX PubMed=16763195; DOI=10.1242/jcs.02979;
RA Halbach A., Landgraf C., Lorenzen S., Rosenkranz K., Volkmer-Engert R.,
RA Erdmann R., Rottensteiner H.;
RT "Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and
RT PEX15 occurs through C-terminal PEX19-binding sites.";
RL J. Cell Sci. 119:2508-2517(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=24821790; DOI=10.1073/pnas.1405755111;
RA Okreglak V., Walter P.;
RT "The conserved AAA-ATPase Msp1 confers organelle specificity to tail-
RT anchored proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8019-8024(2014).
CC -!- FUNCTION: Essential for the biogenesis of peroxisomes. Has a role in
CC anchoring PEX6 onto the peroxisomal membrane.
CC {ECO:0000269|PubMed:12808025, ECO:0000269|PubMed:9405362}.
CC -!- SUBUNIT: Interacts with PEX6 and PEX19. Interaction with PEX19 targets
CC PEX15 to the peroxisome. {ECO:0000269|PubMed:12808025,
CC ECO:0000269|PubMed:16763195}.
CC -!- INTERACTION:
CC Q08215; P33760: PEX6; NbExp=14; IntAct=EBI-31849, EBI-13178;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:24821790}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9405362}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74786; CAA99046.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10738.1; -; Genomic_DNA.
DR PIR; S66729; S66729.
DR RefSeq; NP_014598.1; NM_001183298.1.
DR PDB; 5VXV; X-ray; 1.55 A; A=43-253.
DR PDBsum; 5VXV; -.
DR AlphaFoldDB; Q08215; -.
DR SMR; Q08215; -.
DR BioGRID; 34358; 204.
DR ComplexPortal; CPX-1901; Peroxisomal receptor export module complex.
DR DIP; DIP-4159N; -.
DR IntAct; Q08215; 13.
DR MINT; Q08215; -.
DR STRING; 4932.YOL044W; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q08215; -.
DR PaxDb; Q08215; -.
DR PRIDE; Q08215; -.
DR EnsemblFungi; YOL044W_mRNA; YOL044W; YOL044W.
DR GeneID; 854113; -.
DR KEGG; sce:YOL044W; -.
DR SGD; S000005404; PEX15.
DR VEuPathDB; FungiDB:YOL044W; -.
DR eggNOG; ENOG502S7IW; Eukaryota.
DR HOGENOM; CLU_057737_0_0_1; -.
DR InParanoid; Q08215; -.
DR OMA; VSACDIM; -.
DR BioCyc; YEAST:G3O-33458-MON; -.
DR PRO; PR:Q08215; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08215; protein.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IMP:SGD.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Peroxisome;
KW Peroxisome biogenesis; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..383
FT /note="Peroxisomal membrane protein PEX15"
FT /id="PRO_0000270567"
FT TOPO_DOM 1..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..383
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MUTAGEN 22
FT /note="L->F,S: No interaction with PEX6."
FT /evidence="ECO:0000269|PubMed:12808025"
FT MUTAGEN 47
FT /note="Q->L: No interaction with PEX6."
FT /evidence="ECO:0000269|PubMed:12808025"
FT MUTAGEN 50
FT /note="V->A: No interaction with PEX6."
FT /evidence="ECO:0000269|PubMed:12808025"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 153..177
FT /evidence="ECO:0007829|PDB:5VXV"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:5VXV"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5VXV"
FT HELIX 237..253
FT /evidence="ECO:0007829|PDB:5VXV"
SQ SEQUENCE 383 AA; 43676 MW; B575A8D4B0DAC0B8 CRC64;
MAASEIMNNL PMHSLDSSLR DLLNDDLFIE SDESTKSVND QRSEVFQECV NLFIKRDIKD
CLEKMSEVGF IDITVFKSNP MILDLFVSAC DIMPSFTKLG LTLQSEILNI FTLDTPQCIE
TRKIILGDLS KLLVINKFFR CCIKVIQFNL TDHTEQEEKT LELESIMSDF IFVYITKMRT
TIDVVGLQEL IEIFIFQVKV KLHHKKPSPN MYWALCKTLP KLSPTLKGLY LSKDVSIEDA
ILNSIDNKIQ KDKAKSKGKQ RGVKQKIHHF HEPMLHNSSE EQVKVEDAFN QRTSTDSRLQ
STGTAPRKKN NDITVLAGSF WAVLKHHFTR SVLNKNGLLL TGLLLLLCLK KYKSLMAIFK
HVPAAFHTVY PQIVGLLKLL ASI
