PLOD3

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3
Identifiers
Symbols	PLOD3 ; LH3
External IDs	Template:OMIM5 Template:MGI HomoloGene: 843
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PLOD3 202185 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3, also known as PLOD3, is a human gene.

The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.

Further reading

• Salo AM, Wang C, Sipilä L; et al. (2006). "Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling". J. Cell. Physiol. 207 (3): 644–53. doi:10.1002/jcp.20596. PMID 16447251.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Otsuki T, Ota T, Nishikawa T; et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hillier LW, Fulton RS, Fulton LA; et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang C, Luosujärvi H, Heikkinen J; et al. (2003). "The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro". Matrix Biol. 21 (7): 559–66. PMID 12475640.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rautavuoma K, Takaluoma K, Passoja K; et al. (2002). "Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity". J. Biol. Chem. 277 (25): 23084–91. doi:10.1074/jbc.M112077200. PMID 11956192.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ruotsalainen H, Vanhatupa S, Tampio M; et al. (2001). "Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase". Matrix Biol. 20 (2): 137–46. PMID 11334715.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Heikkinen J, Risteli M, Wang C; et al. (2000). "Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity". J. Biol. Chem. 275 (46): 36158–63. doi:10.1074/jbc.M006203200. PMID 10934207.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI (2000). "Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3)". Matrix Biol. 19 (1): 73–9. PMID 10686427.CS1 maint: Multiple names: authors list (link)
• Passoja K, Rautavuoma K, Ala-Kokko L; et al. (1998). "Cloning and characterization of a third human lysyl hydroxylase isoform". Proc. Natl. Acad. Sci. U.S.A. 95 (18): 10482–6. PMID 9724729.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Valtavaara M, Szpirer C, Szpirer J, Myllylä R (1998). "Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)". J. Biol. Chem. 273 (21): 12881–6. PMID 9582318.CS1 maint: Multiple names: authors list (link)