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9.A.17.1.1
The Pex3/Pex16/Pex19 peroxisomal protein importer (for insertion of integral membranes from the cytosol to the peroxisomal membrane) (Matsuzono and Fujiki, 2006).  Pex3 promotes formation of peroxisome-peroxisome and peroxisome-lipid droplet contact sites (Amado et al. 2025).  Pex3 is a conserved multifunctional peroxisomal transmembrane protein that is involved in the insertion of peroxisomal membrane proteins, in pexophagy, and in the formation of membrane contact sites. High Pex3 levels in Saccharomyces cerevisiae induce the formation of peroxisome clusters surrounded by lipid droplets, mediated by peroxisome-peroxisome and peroxisome-lipid droplet contact sites (Amado et al. 2025).

Accession Number:Q07418
Protein Name:Pex19 aka Peroxin-19
Length:342
Molecular Weight:38706.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Location1 / Topology2 / Orientation3: Cytoplasm1 / Lipid-anchor2 / Cytoplasmic side3
Substrate protein polypeptide chain

Cross database links:

DIP: DIP-1563N
RefSeq: NP_010218.2   
Entrez Gene ID: 851494   
Pfam: PF04614   
KEGG: sce:YDL065C   

Gene Ontology

GO:0005829 C:cytosol
GO:0005789 C:endoplasmic reticulum membrane
GO:0005778 C:peroxisomal membrane
GO:0033328 F:peroxisome membrane targeting sequence binding
GO:0005515 F:protein binding
GO:0032527 P:protein exit from endoplasmic reticulum
GO:0045046 P:protein import into peroxisome membrane
GO:0050821 P:protein stabilization

References (17)

[1] “Pex19p, a farnesylated protein essential for peroxisome biogenesis.”  Goette K.et.al.   9418908
[2] “The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.”  Jacq C.et.al.   9169867
[3] “Saccharomyces cerevisiae Pex3p and Pex19p are required for proper localization and stability of peroxisomal membrane proteins.”  Hettema E.H.et.al.   10637226
[4] “Pex10p links the ubiquitin conjugating enzyme Pex4p to the protein import machinery of the peroxisome.”  Eckert J.H.et.al.   12876220
[5] “Sequencing and comparison of yeast species to identify genes and regulatory elements.”  Kellis M.et.al.   12748633
[6] “Global analysis of protein localization in budding yeast.”  Huh W.-K.et.al.   14562095
[7] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[8] “Finding functional features in Saccharomyces genomes by phylogenetic footprinting.”  Cliften P.F.et.al.   12775844
[9] “Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals.”  Rottensteiner H.et.al.   15133130
[10] “Contribution of the endoplasmic reticulum to peroxisome formation.”  Hoepfner D.et.al.   16009135
[11] “Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae.”  Tam Y.Y.C.et.al.   16087670
[12] “Farnesylation of Pex19p is not essential for peroxisome biogenesis in yeast and mammalian cells.”  Vastiau I.M.K.et.al.   16791427
[13] “The dynamin-like protein Vps1p of the yeast Saccharomyces cerevisiae associates with peroxisomes in a Pex19p-dependent manner.”  Vizeacoumar F.J.et.al.   16520372
[14] “Pex19p binds Pex30p and Pex32p at regions required for their peroxisomal localization but separate from their peroxisomal targeting signals.”  Vizeacoumar F.J.et.al.   16551610
[15] “Pex19p-dependent targeting of Pex17p, a peripheral component of the peroxisomal protein import machinery.”  Girzalsky W.et.al.   16679311
[16] “Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.”  Li X.et.al.   17330950
[17] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNENEYDNFD DLDDLLDEDP TKLDEAEPDD VQAKGSVYND SENKEKNAES KDSDGVQVAN 
61:	ESEEDPELKE MMVDLQNEFA NLMKNNGNEN NVKTEDFNKL ISALEEAAKV PHQQMEQGCS 
121:	SLKSNSTDKG TVNGSNPGFK NIVSNTLDRL KENGNKVDTS LAEETKESQR SGQNNNIDDI 
181:	LSQLLDQMVA SGGKESAENQ FDLKDGEMDD AITKILDQMT SKEVLYEPMK EMRSEFGVWF 
241:	QENGENEEHK EKIGTYKRQF NIVDEIVNIY ELKDYDELKH KDRVTELLDE LEQLGDSPIR 
301:	SANSPLKHGN EEEELMKMLE IDGNDPNLGN LDKELTDGCK QQ