PEX5

From Wikipedia, the free encyclopedia

Peroxisomal biogenesis factor 5

PDB rendering based on 1fch.

Available structures: 1fch, 2c0l, 2c0m, 2j9q

Identifiers

Symbol(s)

PEX5; PTS1R; PXR1

External IDs

OMIM: 600414 MGI: 1098808 HomoloGene: 270

Gene ontology
Molecular Function:	• peroxisome matrix targeting signal-1 binding • binding • protein binding
Cellular Component:	• peroxisome • peroxisomal membrane
Biological Process:	• protein transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000319 (mRNA)
NP_000310 (protein)

NM_008995 (mRNA)
NP_033021 (protein)

Location

Chr 12: 7.23 - 7.26 Mb

Chr 6: 124.36 - 124.38 Mb

Pubmed search

[1]

[2]

Peroxisomal biogenesis factor 5, also known as PEX5, is a human gene.^[1]

[edit] References

^ Entrez Gene: PEX5 Peroxisomal biogenesis factor 5.

[edit] Further reading

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. 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. 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. 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. 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. 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. 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. 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. 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): 367–71. 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. 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. 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. 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. 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.