PEX5

From Wikipedia, the free encyclopedia

Peroxisomal biogenesis factor 5

PDB rendering based on 1fch.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1FCH, 2C0L, 2C0M, 2J9Q, 2W84, 3R9A

Identifiers

Symbols

PEX5; PBD2A; PBD2B; PTS1-BP; PTS1R; PXR1

External IDs

OMIM: 600414 MGI: 1098808 HomoloGene: 270 GeneCards: PEX5 Gene

Gene Ontology
Molecular function	• peroxisome targeting sequence binding • peroxisome matrix targeting signal-1 binding • protein binding • protein C-terminus binding • enzyme binding • small GTPase binding • protein N-terminus binding
Cellular component	• cytoplasm • mitochondrion • peroxisome • peroxisomal membrane • peroxisomal matrix • Golgi apparatus • cytosol • membrane • protein complex
Biological process	• very long-chain fatty acid metabolic process • neuron migration • protein targeting to peroxisome • fatty acid beta-oxidation • mitochondrial membrane organization • endoplasmic reticulum organization • protein import into peroxisome matrix • protein import into peroxisome matrix, docking • protein import into peroxisome matrix, translocation • cerebral cortex cell migration • cerebral cortex neuron differentiation • positive regulation of multicellular organism growth • protein import into peroxisome membrane • cell development • neuromuscular process • protein tetramerization • negative regulation of protein homotetramerization
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
7.34 – 7.37 Mb

Chr 6:
124.4 – 124.42 Mb

PubMed search

Peroxisomal targeting signal 1 receptor is a protein that in humans is encoded by the PEX5 gene.^[1]

Interactions

PEX5 has been shown to interact with PEX12,^[2]^[3] PEX13^[4]^[5] and PEX14.^[3]^[5]^[6]

References

↑ "Entrez Gene: PEX5 Peroxisomal biogenesis factor 5".
↑ Chang, C C; Warren D S, Sacksteder K A, Gould S J (November 1999). "Pex12 Interacts with Pex5 and Pex10 and Acts Downstream of Receptor Docking in Peroxisomal Matrix Protein Import". J. Cell Biol. (UNITED STATES) 147 (4): 761–74. doi:10.1083/jcb.147.4.761. ISSN 0021-9525. PMC 2156163. PMID 10562279. Cite uses deprecated parameters (help)
↑ 3.0 3.1 Okumoto, K; Abe I, Fujiki Y (August 2000). "Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p". J. Biol. Chem. (UNITED STATES) 275 (33): 25700–10. doi:10.1074/jbc.M003303200. ISSN 0021-9258. PMID 10837480. Cite uses deprecated parameters (help)
↑ Gould, S J; Kalish J E, Morrell J C, Bjorkman J, Urquhart A J, Crane D I (October 1996). "Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor". J. Cell Biol. (UNITED STATES) 135 (1): 85–95. doi:10.1083/jcb.135.1.85. ISSN 0021-9525. PMC 2121023. PMID 8858165. Cite uses deprecated parameters (help)
↑ 5.0 5.1 Otera, Hidenori; Setoguchi Kiyoko, Hamasaki Maho, Kumashiro Toshitaka, Shimizu Nobuhiro, Fujiki Yukio (March 2002). "Peroxisomal Targeting Signal Receptor Pex5p Interacts with Cargoes and Import Machinery Components in a Spatiotemporally Differentiated Manner: Conserved Pex5p WXXXF/Y Motifs Are Critical for Matrix Protein Import". Mol. Cell. Biol. (United States) 22 (6): 1639–55. doi:10.1128/MCB.22.6.1639-1655.2002. ISSN 0270-7306. PMC 135613. PMID 11865044. Cite uses deprecated parameters (help)
↑ Shimizu, N; Itoh R, Hirono Y, Otera H, Ghaedi K, Tateishi K, Tamura S, Okumoto K, Harano T, Mukai S, Fujiki Y (April 1999). "The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis". J. Biol. Chem. (UNITED STATES) 274 (18): 12593–604. doi:10.1074/jbc.274.18.12593. ISSN 0021-9258. PMID 10212238. Cite uses deprecated parameters (help)

Fransen M, Brees C, Baumgart E, et al. (1995). "Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor". J. Biol. Chem. 270 (13): 7731–6. doi:10.1074/jbc.270.13.7731. PMID 7706321.
Dodt G, Braverman N, Wong C, et al. (1995). "Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders". Nat. Genet. 9 (2): 115–25. doi:10.1038/ng0295-115. PMID 7719337.
Wiemer EA, Nuttley WM, Bertolaet BL, et al. (1995). "Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders". J. Cell Biol. 130 (1): 51–65. doi:10.1083/jcb.130.1.51. PMC 2120514. PMID 7790377.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Marynen P, Fransen M, Raeymaekers P, et al. (1996). "The gene for the peroxisomal targeting signal import receptor (PXR1) is located on human chromosome 12p13, flanked by TPI1 and D12S1089". Genomics 30 (2): 366–8. doi:10.1006/geno.1995.0032. PMID 8586442.
Gould SJ, Kalish JE, Morrell JC, et al. (1996). "Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTs1 receptor". J. Cell Biol. 135 (1): 85–95. doi:10.1083/jcb.135.1.85. PMC 2121023. PMID 8858165.
Dodt G, Gould SJ (1997). "Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor". J. Cell Biol. 135 (6 Pt 2): 1763–74. doi:10.1083/jcb.135.6.1763. PMC 2133940. PMID 8991089.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Reuber BE, Germain-Lee E, Collins CS, et al. (1997). "Mutations in PEX1 are the most common cause of peroxisome biogenesis disorders". Nat. Genet. 17 (4): 445–8. doi:10.1038/ng1297-445. PMID 9398847.
Otera H, Okumoto K, Tateishi K, et al. (1998). "Peroxisome Targeting Signal Type 1 (PTS1) Receptor Is Involved in Import of Both PTS1 and PTS2: Studies with PEX5-Defective CHO Cell Mutants". Mol. Cell. Biol. 18 (1): 388–99. PMC 121509. PMID 9418886.
Fransen M, Terlecky SR, Subramani S (1998). "Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8087–92. doi:10.1073/pnas.95.14.8087. PMC 20933. PMID 9653144.
Amery L, Brees C, Baes M, et al. (1999). "C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal". Biochem. J. 336 ( Pt 2) (Pt 2): 367–71. PMC 1219880. PMID 9820813.
Shimizu N, Itoh R, Hirono Y, et al. (1999). "The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis". J. Biol. Chem. 274 (18): 12593–604. doi:10.1074/jbc.274.18.12593. PMID 10212238.
Shimozawa N, Zhang Z, Suzuki Y, et al. (1999). "Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients". Biochem. Biophys. Res. Commun. 262 (2): 504–8. doi:10.1006/bbrc.1999.1232. PMID 10462504.
Chang CC, Warren DS, Sacksteder KA, Gould SJ (1999). "Pex12 Interacts with Pex5 and Pex10 and Acts Downstream of Receptor Docking in Peroxisomal Matrix Protein Import". J. Cell Biol. 147 (4): 761–74. doi:10.1083/jcb.147.4.761. PMC 2156163. PMID 10562279.
Watters D, Kedar P, Spring K, et al. (1999). "Localization of a portion of extranuclear ATM to peroxisomes". J. Biol. Chem. 274 (48): 34277–82. doi:10.1074/jbc.274.48.34277. PMID 10567403.
Okumoto K, Abe I, Fujiki Y (2000). "Molecular anatomy of the peroxin Pex12p: ring finger domain is essential for Pex12p function and interacts with the peroxisome-targeting signal type 1-receptor Pex5p and a ring peroxin, Pex10p". J. Biol. Chem. 275 (33): 25700–10. doi:10.1074/jbc.M003303200. PMID 10837480.
Gatto GJ, Geisbrecht BV, Gould SJ, Berg JM (2001). "Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5". Nat. Struct. Biol. 7 (12): 1091–5. doi:10.1038/81930. PMID 11101887.
Harano T, Nose S, Uezu R, et al. (2001). "Hsp70 regulates the interaction between the peroxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1". Biochem. J. 357 (Pt 1): 157–65. doi:10.1042/0264-6021:3570157. PMC 1221938. PMID 11415446.
Saidowsky J, Dodt G, Kirchberg K, et al. (2001). "The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14". J. Biol. Chem. 276 (37): 34524–9. doi:10.1074/jbc.M104647200. PMID 11438541.
Stanley W, Filipp F, Kursula P, et al. (2006). "Recognition of a Functional Peroxisome Type 1 Target by the Dynamic Import Receptor Pex5p". Mol. Cell 24 (5): 653–63. doi:10.1016/j.molcel.2006.10.024. PMID 17157249.

External links

PDB gallery

1fch: CRYSTAL STRUCTURE OF THE PTS1 COMPLEXED TO THE TPR REGION OF HUMAN PEX5

2c0l: TPR DOMAIN OF HUMAN PEX5P IN COMPLEX WITH HUMAN MSCP2

2c0m: APO FORM OF THE TPR DOMAIN OF THE PEX5P RECEPTOR

2j9q: A NOVEL CONFORMATION FOR THE TPR DOMAIN OF PEX5P

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PEX5

Interactions

References

Further reading

External links