PEX19_YEAST
ID PEX19_YEAST Reviewed; 342 AA.
AC Q07418; D6VRT2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Peroxisomal membrane protein import receptor PEX19;
DE AltName: Full=Peroxin-19;
DE Flags: Precursor;
GN Name=PEX19; Synonyms=PAS12; OrderedLocusNames=YDL065C; ORFNames=D2528;
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, INTERACTION WITH PEX3,
RP INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-339, AND ISOPRENYLATION
RP AT CYS-339.
RX PubMed=9418908; DOI=10.1128/mcb.18.1.616;
RA Goette K., Girzalsky W., Linkert M., Baumgart E., Kammerer S., Kunau W.-H.,
RA Erdmann R.;
RT "Pex19p, a farnesylated protein essential for peroxisome biogenesis.";
RL Mol. Cell. Biol. 18:616-628(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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.
RX PubMed=10637226; DOI=10.1093/emboj/19.2.223;
RA Hettema E.H., Girzalsky W., van den Berg M., Erdmann R., Distel B.;
RT "Saccharomyces cerevisiae Pex3p and Pex19p are required for proper
RT localization and stability of peroxisomal membrane proteins.";
RL EMBO J. 19:223-233(2000).
RN [5]
RP INTERACTION WITH PEROXISOMAL MEMBRANE PROTEINS.
RX PubMed=12876220; DOI=10.1242/jcs.00678;
RA Eckert J.H., Johnsson N.;
RT "Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import
RT machinery of the peroxisome.";
RL J. Cell Sci. 116:3623-3634(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH PEX11; PEX13 AND PEX25.
RX PubMed=15133130; DOI=10.1091/mbc.e04-03-0188;
RA Rottensteiner H., Kramer A., Lorenzen S., Stein K., Landgraf C.,
RA Volkmer-Engert R., Erdmann R.;
RT "Peroxisomal membrane proteins contain common Pex19p-binding sites that are
RT an integral part of their targeting signals.";
RL Mol. Biol. Cell 15:3406-3417(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16009135; DOI=10.1016/j.cell.2005.04.025;
RA Hoepfner D., Schildknegt D., Braakman I., Philippsen P., Tabak H.F.;
RT "Contribution of the endoplasmic reticulum to peroxisome formation.";
RL Cell 122:85-95(2005).
RN [13]
RP FUNCTION.
RX PubMed=16087670; DOI=10.1074/jbc.m506208200;
RA Tam Y.Y.C., Fagarasanu A., Fagarasanu M., Rachubinski R.A.;
RT "Pex3p initiates the formation of a preperoxisomal compartment from a
RT subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:34933-34939(2005).
RN [14]
RP MUTAGENESIS OF CYS-339.
RX PubMed=16791427; DOI=10.1007/s00018-006-6110-y;
RA Vastiau I.M.K., Anthonio E.A., Brams M., Brees C., Young S.G.,
RA Van de Velde S., Wanders R.J.A., Mannaerts G.P., Baes M.,
RA Van Veldhoven P.P., Fransen M.;
RT "Farnesylation of Pex19p is not essential for peroxisome biogenesis in
RT yeast and mammalian cells.";
RL Cell. Mol. Life Sci. 63:1686-1699(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH VPS1.
RX PubMed=16520372; DOI=10.1074/jbc.m600365200;
RA Vizeacoumar F.J., Vreden W.N., Fagarasanu M., Eitzen G.A., Aitchison J.D.,
RA Rachubinski R.A.;
RT "The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae
RT associates with peroxisomes in a Pex19p-dependent manner.";
RL J. Biol. Chem. 281:12817-12823(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH PEX11; PEX30 AND PEX32.
RX PubMed=16551610; DOI=10.1074/jbc.m601808200;
RA Vizeacoumar F.J., Vreden W.N., Aitchison J.D., Rachubinski R.A.;
RT "Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal
RT localization but separate from their peroxisomal targeting signals.";
RL J. Biol. Chem. 281:14805-14812(2006).
RN [17]
RP FUNCTION, AND INTERACTION WITH PEX17.
RX PubMed=16679311; DOI=10.1074/jbc.m603344200;
RA Girzalsky W., Hoffmann L.S., Schemenewitz A., Nolte A., Kunau W.-H.,
RA Erdmann R.;
RT "Pex19p-dependent targeting of Pex17p, a peripheral component of the
RT peroxisomal protein import machinery.";
RL J. Biol. Chem. 281:19417-19425(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-304, AND
RP IDENTIFICATION BY 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Required for proper post-translational import and
CC stabilization of peroxisomal membrane proteins (PMPs). Acts as a
CC cytosolic import receptor for PMPs and delivers them to the docking
CC factor PEX3 at the peroxisomal membrane for subsequent insertion into
CC the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in
CC the lipid bilayer. Directs PEX17, a peripheral component of the
CC peroxisomal matrix protein translocation machinery, to peroxisomes.
CC Stabilizes VPS1, a protein required for peroxisomal fission, at the
CC peroxisomal membrane. Also acts in conjunction with PEX3 in the
CC formation of peroxisomes from preperoxisomal compartments at the
CC endoplasmic reticulum during de novo peroxisome synthesis, probably via
CC the import of additional PMPs. {ECO:0000269|PubMed:10637226,
CC ECO:0000269|PubMed:15133130, ECO:0000269|PubMed:16087670,
CC ECO:0000269|PubMed:16520372, ECO:0000269|PubMed:16551610,
CC ECO:0000269|PubMed:16679311, ECO:0000269|PubMed:9418908}.
CC -!- SUBUNIT: Interacts (farnesylated) with PEX3; farnesylation is required
CC for this interaction. Interacts with PEX2, PEX5, PEX10, PEX11, PEX12,
CC PEX13, PEX14, PEX17, PEX22, PEX25, PEX30 and PEX32; the interaction
CC requires well-defined PEX19-binding sites within the peroxisomal
CC membrane protein targeting signal (mPTS) of the PMPs and is independent
CC on the presence of PEX3. Interacts with VPS1.
CC {ECO:0000269|PubMed:12876220, ECO:0000269|PubMed:15133130,
CC ECO:0000269|PubMed:16520372, ECO:0000269|PubMed:16551610,
CC ECO:0000269|PubMed:16679311, ECO:0000269|PubMed:9418908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16009135, ECO:0000269|PubMed:9418908}. Peroxisome
CC membrane {ECO:0000269|PubMed:16009135}; Lipid-anchor {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16009135}. Note=Predominantly cytoplasmic
CC (PubMed:9418908). Concentrates in a PEX3-dependent manner to defined
CC foci on the endoplasmic reticulum membrane, which then bud off to form
CC newly sythesized peroxisomes (PubMed:16009135).
CC {ECO:0000269|PubMed:16009135, ECO:0000269|PubMed:9418908}.
CC -!- INDUCTION: By oleic acid (at protein level).
CC {ECO:0000269|PubMed:9418908}.
CC -!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxin-19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA98630.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z74113; CAA98630.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006938; DAA11792.1; -; Genomic_DNA.
DR PIR; S67600; S67600.
DR RefSeq; NP_010218.2; NM_001180124.1.
DR AlphaFoldDB; Q07418; -.
DR SMR; Q07418; -.
DR BioGRID; 31994; 390.
DR DIP; DIP-1563N; -.
DR IntAct; Q07418; 18.
DR MINT; Q07418; -.
DR STRING; 4932.YDL065C; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR TCDB; 9.A.17.1.1; the integral membrane peroxisomal protein importer-2 (ppi2) family.
DR iPTMnet; Q07418; -.
DR MaxQB; Q07418; -.
DR PaxDb; Q07418; -.
DR PRIDE; Q07418; -.
DR EnsemblFungi; YDL065C_mRNA; YDL065C; YDL065C.
DR GeneID; 851494; -.
DR KEGG; sce:YDL065C; -.
DR SGD; S000002223; PEX19.
DR VEuPathDB; FungiDB:YDL065C; -.
DR eggNOG; KOG3133; Eukaryota.
DR GeneTree; ENSGT00390000010993; -.
DR HOGENOM; CLU_863835_0_0_1; -.
DR InParanoid; Q07418; -.
DR OMA; NPQCPTM; -.
DR BioCyc; YEAST:G3O-29480-MON; -.
DR Reactome; R-SCE-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:Q07418; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07418; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990429; C:peroxisomal importomer complex; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IPI:SGD.
DR GO; GO:0032581; P:ER-dependent peroxisome organization; IMP:SGD.
DR GO; GO:0045033; P:peroxisome inheritance; IPI:SGD.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IMP:SGD.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IPI:SGD.
DR Gene3D; 1.20.120.900; -; 1.
DR InterPro; IPR006708; Pex19.
DR InterPro; IPR038322; Pex19_C_sf.
DR PANTHER; PTHR12774; PTHR12774; 1.
DR Pfam; PF04614; Pex19; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Lipoprotein; Membrane; Methylation;
KW Peroxisome; Peroxisome biogenesis; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Peroxisomal membrane protein import receptor PEX19"
FT /id="PRO_0000218763"
FT PROPEP 340..342
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396705"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 339
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 339
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:9418908"
FT MUTAGEN 339
FT /note="C->S,R: Prevents farnesylation."
FT /evidence="ECO:0000269|PubMed:16791427,
FT ECO:0000269|PubMed:9418908"
SQ SEQUENCE 342 AA; 38706 MW; B2FDE24970443D2A CRC64;
MNENEYDNFD DLDDLLDEDP TKLDEAEPDD VQAKGSVYND SENKEKNAES KDSDGVQVAN
ESEEDPELKE MMVDLQNEFA NLMKNNGNEN NVKTEDFNKL ISALEEAAKV PHQQMEQGCS
SLKSNSTDKG TVNGSNPGFK NIVSNTLDRL KENGNKVDTS LAEETKESQR SGQNNNIDDI
LSQLLDQMVA SGGKESAENQ FDLKDGEMDD AITKILDQMT SKEVLYEPMK EMRSEFGVWF
QENGENEEHK EKIGTYKRQF NIVDEIVNIY ELKDYDELKH KDRVTELLDE LEQLGDSPIR
SANSPLKHGN EEEELMKMLE IDGNDPNLGN LDKELTDGCK QQ
