PLOD3

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

PLOD3
Identifiers
Aliases	PLOD3, LH3, procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
External IDs	OMIM: 603066 MGI: 1347008 HomoloGene: 843 GeneCards: PLOD3
Gene location (Human) Chr. Chromosome 7 (human) Band 7q22.1 Start 101,205,977 bp End 101,218,420 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 G2|5 76.09 cM Start 137,015,873 bp End 137,025,502 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium pancreatic ductal cell tibial nerve upper lobe of left lung right lobe of liver sural nerve left coronary artery left uterine tube canal of the cervix right coronary artery Top expressed in calvaria yolk sac ankle joint lip sternocleidomastoid muscle belly cord superior frontal gyrus lens white adipose tissue temporal muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function iron ion binding L-ascorbic acid binding dioxygenase activity metal ion binding protein binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen procollagen galactosyltransferase activity oxidoreductase activity procollagen-lysine 5-dioxygenase activity procollagen glucosyltransferase activity catalytic activity transferase activity glycosyltransferase activity Cellular component rough endoplasmic reticulum membrane endoplasmic reticulum membrane membrane extracellular exosome endoplasmic reticulum Golgi apparatus trans-Golgi network extracellular matrix extracellular region extracellular space endoplasmic reticulum lumen rough endoplasmic reticulum collagen-containing extracellular matrix 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 protein O-linked glycosylation hydroxylysine biosynthetic process peptidyl-lysine hydroxylation collagen metabolic process metabolism Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8985 26433 Ensembl ENSG00000106397 ENSMUSG00000004846 UniProt O60568 Q9R0E1 RefSeq (mRNA) NM_001084 NM_011962 RefSeq (protein) NP_001075 NP_036092 Location (UCSC) Chr 7: 101.21 – 101.22 Mb Chr 5: 137.02 – 137.03 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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): 644–653. doi:10.1002/jcp.20596. PMID 16447251. S2CID 19594208.
• 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): 117–126. 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): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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): 2121–2127. 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): 157–164. Bibcode:2003Natur.424..157H. 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): 16899–16903. Bibcode:2002PNAS...9916899M. 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): 559–566. 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): 23084–23091. 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): 137–146. 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): 36158–36163. 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): 73–79. doi:10.1016/S0945-053X(99)00058-X. PMID 10686427.