Q07418 (PEX19_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal membrane protein import receptor PEX19

Alternative name(s):
Peroxin-19

Gene names

Name:	PEX19
Synonyms:	PAS12
Ordered Locus Names:	YDL065C
ORF Names:	D2528

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs. Ref.1 Ref.4 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16
Subunit structure	Interacts (farnesylated) with PEX3; farnesylation is required for this interaction. Interacts with PEX2, PEX5, PEX10, PEX11, PEX12, PEX13, PEX14, PEX17, PEX22, PEX25, PEX30 and PEX32; the interaction requires well-defined PEX19-binging sites within the peroxisomal membrane protein targeting signal (mPTS) of the PMPs and is independent on the presence of PEX3. Interacts with VPS1. Ref.1 Ref.5 Ref.10 Ref.14 Ref.15 Ref.16
Subcellular location	Cytoplasm. Peroxisome membrane; Lipid-anchor; Cytoplasmic side. Endoplasmic reticulum membrane. Note: Predominantly cytoplasmic. Concentrates in a PEX3-dependent manner to defined foci on the endoplasmic reticulum membrane, which then bud off to form newly sythesized peroxisomes. Ref.1 Ref.7 Ref.11
Induction	By oleic acid (at protein level). Ref.1
Miscellaneous	Present with 5350 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the peroxin-19 family.
Sequence caution	The sequence CAA98630.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Peroxisome biogenesis
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Peroxisome
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER-dependent peroxisome organization Inferred from mutant phenotype. Source: SGD protein exit from endoplasmic reticulum Inferred from mutant phenotype Ref.11. Source: SGD protein import into peroxisome membrane Inferred from mutant phenotype Ref.4. Source: SGD protein stabilization Inferred from physical interaction Ref.16. Source: SGD
Cellular component	cytosol Inferred from direct assay Ref.1. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisomal membrane Inferred from direct assay Ref.1. Source: SGD
Molecular function	peroxisome membrane targeting sequence binding Inferred from physical interaction Ref.16. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
INP2	Q03824	3	EBI-292,EBI-27354

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Peroxisomal membrane protein import receptor PEX19		PRO_0000218763
	Propeptide	340 – 342	3	Removed in mature form Probable		PRO_0000396705
Regions
	Compositional bias	311 – 314	4	Poly-Glu
Amino acid modifications
	Modified residue	36	1	Phosphoserine Ref.18
	Modified residue	62	1	Phosphoserine Ref.18
	Modified residue	304	1	Phosphoserine Ref.17 Ref.18
	Modified residue	339	1	Cysteine methyl ester Probable
	Lipidation	339	1	S-farnesyl cysteine Ref.1
Experimental info
	Mutagenesis	339	1	C → S or R: Prevents farnesylation. Ref.1 Ref.13

Sequences

	Sequence		Length	Mass (Da)
	Q07418 [UniParc]. Last modified July 1, 2008. Version 2. Checksum: B2FDE24970443D2A	FASTA	342	38,706
	10 20 30 40 50 60 MNENEYDNFD DLDDLLDEDP TKLDEAEPDD VQAKGSVYND SENKEKNAES KDSDGVQVAN 70 80 90 100 110 120 ESEEDPELKE MMVDLQNEFA NLMKNNGNEN NVKTEDFNKL ISALEEAAKV PHQQMEQGCS 130 140 150 160 170 180 SLKSNSTDKG TVNGSNPGFK NIVSNTLDRL KENGNKVDTS LAEETKESQR SGQNNNIDDI 190 200 210 220 230 240 LSQLLDQMVA SGGKESAENQ FDLKDGEMDD AITKILDQMT SKEVLYEPMK EMRSEFGVWF 250 260 270 280 290 300 QENGENEEHK EKIGTYKRQF NIVDEIVNIY ELKDYDELKH KDRVTELLDE LEQLGDSPIR 310 320 330 340 SANSPLKHGN EEEELMKMLE IDGNDPNLGN LDKELTDGCK QQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pex19p, a farnesylated protein essential for peroxisome biogenesis." Goette K., Girzalsky W., Linkert M., Baumgart E., Kammerer S., Kunau W.-H., Erdmann R. Mol. Cell. Biol. 18:616-628(1998) [PubMed: 9418908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH PEX3, INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-339, ISOPRENYLATION AT CYS-339.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins." Hettema E.H., Girzalsky W., van den Berg M., Erdmann R., Distel B. EMBO J. 19:223-233(2000) [PubMed: 10637226] [Abstract] Cited for: FUNCTION.
[5]	"Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome." Eckert J.H., Johnsson N. J. Cell Sci. 116:3623-3634(2003) [PubMed: 12876220] [Abstract] Cited for: INTERACTION WITH PEROXISOMAL MEMBRANE PROTEINS.
[6]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Finding functional features in Saccharomyces genomes by phylogenetic footprinting." Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M. Science 301:71-76(2003) [PubMed: 12775844] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[10]	"Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals." Rottensteiner H., Kramer A., Lorenzen S., Stein K., Landgraf C., Volkmer-Engert R., Erdmann R. Mol. Biol. Cell 15:3406-3417(2004) [PubMed: 15133130] [Abstract] Cited for: FUNCTION, INTERACTION WITH PEX11; PEX13 AND PEX25.
[11]	"Contribution of the endoplasmic reticulum to peroxisome formation." Hoepfner D., Schildknegt D., Braakman I., Philippsen P., Tabak H.F. Cell 122:85-95(2005) [PubMed: 16009135] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae." Tam Y.Y.C., Fagarasanu A., Fagarasanu M., Rachubinski R.A. J. Biol. Chem. 280:34933-34939(2005) [PubMed: 16087670] [Abstract] Cited for: FUNCTION.
[13]	"Farnesylation of Pex19p is not essential for peroxisome biogenesis in yeast and mammalian cells." Vastiau I.M.K., Anthonio E.A., Brams M., Brees C., Young S.G., Van de Velde S., Wanders R.J.A., Mannaerts G.P., Baes M., Van Veldhoven P.P., Fransen M. Cell. Mol. Life Sci. 63:1686-1699(2006) [PubMed: 16791427] [Abstract] Cited for: MUTAGENESIS OF CYS-339.
[14]	"The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner." Vizeacoumar F.J., Vreden W.N., Fagarasanu M., Eitzen G.A., Aitchison J.D., Rachubinski R.A. J. Biol. Chem. 281:12817-12823(2006) [PubMed: 16520372] [Abstract] Cited for: FUNCTION, INTERACTION WITH VPS1.
[15]	"Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals." Vizeacoumar F.J., Vreden W.N., Aitchison J.D., Rachubinski R.A. J. Biol. Chem. 281:14805-14812(2006) [PubMed: 16551610] [Abstract] Cited for: FUNCTION, INTERACTION WITH PEX11; PEX30 AND PEX32.
[16]	"Pex19p-dependent targeting of Pex17p, a peripheral component of the peroxisomal protein import machinery." Girzalsky W., Hoffmann L.S., Schemenewitz A., Nolte A., Kunau W.-H., Erdmann R. J. Biol. Chem. 281:19417-19425(2006) [PubMed: 16679311] [Abstract] Cited for: FUNCTION, INTERACTION WITH PEX17.
[17]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY. Strain: ADR376.
[18]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-62 AND SER-304, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74113 Genomic DNA. Translation: CAA98630.1. Different initiation. BK006938 Genomic DNA. Translation: DAA11792.1.
PIR	S67600.
RefSeq	NP_010218.2. NM_001180124.1.
3D structure databases
ProteinModelPortal	Q07418.
SMR	Q07418. Positions 208-313.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1563N.
IntAct	Q07418. 15 interactions.
MINT	MINT-383941.
STRING	Q07418.
Protein family/group databases
TCDB	9.A.17.1.1. integral membrane peroxisomal protein importer-2 (PPI2) family.
Proteomic databases
PeptideAtlas	Q07418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL065C; YDL065C; YDL065C.
GeneID	851494.
KEGG	sce:YDL065C.
NMPDR	fig|4932.3.peg.958.
Organism-specific databases
SGD	S000002223. PEX19.
Phylogenomic databases
eggNOG	fuNOG11412.
GeneTree	EFGT00050000005381.
HOGENOM	HBG203092.
OMA	LDFNDKD.
OrthoDB	EOG4GJ2ZH.
Gene expression databases
ArrayExpress	Q07418.
Genevestigator	Q07418.
GermOnline	YDL065C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006708. Pex19. [Graphical view]
KO	K13337.
PANTHER	PTHR12774. Pex19. 1 hit.
Pfam	PF04614. Pex19. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968828.

Entry information

Entry name

PEX19_YEAST

Accession

Primary (citable) accession number: Q07418
Secondary accession number(s): D6VRT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 2008
Last modified:	December 14, 2011
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program