PLOD3

PLOD3
Identifiers
Aliases	PLOD3, LH3, procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
External IDs	MGI: 1347008 HomoloGene: 843 GeneCards: PLOD3
Gene ontology Molecular function • iron ion binding • L-ascorbic acid binding • dioxygenase activity • metal ion binding • procollagen-lysine 5-dioxygenase activity • protein binding • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen • procollagen galactosyltransferase activity • procollagen glucosyltransferase activity • oxidoreductase activity Cellular component • rough endoplasmic reticulum membrane • endoplasmic reticulum membrane • membrane • extracellular exosome • endoplasmic reticulum Biological process • protein localization • lung morphogenesis • collagen fibril organization • epidermis morphogenesis • endothelial cell morphogenesis • vasodilation • in utero embryonic development • basement membrane assembly • cellular response to hormone stimulus • neural tube development • oxidation-reduction process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8985	26433
Ensembl	ENSG00000106397	ENSMUSG00000004846
UniProt	O60568	Q9R0E1
RefSeq (mRNA)	NM_001084	NM_011962
RefSeq (protein)	NP_001075.1	NP_036092.1
Location (UCSC)	Chr 7: 101.21 – 101.22 Mb	Chr 5: 136.99 – 137 Mb
PubMed search	[1]	[2]
Wikidata

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Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.^[3][4][5]

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.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI (Sep 1998). "Cloning and characterization of a third human lysyl hydroxylase isoform". Proc Natl Acad Sci U S A. 95 (18): 10482–6. doi:10.1073/pnas.95.18.10482. PMC 27920. PMID 9724729.
4. Valtavaara M, Szpirer C, Szpirer J, Myllyla R (Jun 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. doi:10.1074/jbc.273.21.12881. PMID 9582318.
5. "Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3".

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.
• 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.
• 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.
• 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. PMC 528928. PMID 15489334.
• 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.
• 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. PMC 139241. PMID 12477932.
• 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. doi:10.1016/S0945-053X(02)00071-9. PMID 12475640.
• 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.
• 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. doi:10.1016/S0945-053X(01)00130-5. PMID 11334715.
• 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.
• 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. doi:10.1016/S0945-053X(99)00058-X. PMID 10686427.