PLOD3

From Wikipedia, the free encyclopedia

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3

Identifiers

External IDs

OMIM: 603066 MGI: 1347008 HomoloGene: 843

Gene ontology
Molecular Function:	• iron ion binding • protein binding • procollagen-lysine 5-dioxygenase activity • oxidoreductase activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • L-ascorbic acid binding • metal ion binding
Cellular Component:	• endoplasmic reticulum • membrane
Biological Process:	• protein modification process • protein metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001084 (mRNA)
NP_001075 (protein)

NM_011962 (mRNA)
NP_036092 (protein)

Location

Chr 7: 100.64 - 100.65 Mb

Chr 5: 137.27 - 137.28 Mb

Pubmed search

[1]

[2]

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3, also known as PLOD3, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3.

[edit] 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. 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. 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. 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. 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. PMID 10686427.
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.
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.