Protein Information

General Information
MoonProt ID129
First appeared in release1.0
Name(s)Lysyl hydroxylase 3 Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 LH3 lysine hydroxylase Lysine,2-oxoglutarate 5-dioxygenase Gene Name: PLOD3
UniProt IDO60568 (PLOD3_HUMAN) Reviewed
GO termsGO:0001701 in utero embryonic development GO:0001886 endothelial cell morphogenesis GO:0006464 cellular protein modification process GO:0008104 protein localization GO:0021915 neural tube development GO:0030198 extracellular matrix organization GO:0030199 collagen fibril organization GO:0032870 cellular response to hormone stimulus GO:0042311 vasodilation GO:0048730 epidermis morphogenesis GO:0055114 oxidation-reduction process GO:0060425 lung morphogenesis GO:0070831 basement membrane assembly GO:0005506 iron ion binding GO:0005515 protein binding GO:0008475 procollagen-lysine 5-dioxygenase activity GO:0016491 oxidoreductase activity GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen GO:0016706 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors GO:0031418 L-ascorbic acid binding GO:0033823 procollagen glucosyltransferase activity GO:0046872 metal ion binding GO:0050211 procollagen galactosyltransferase activity GO:0051213 dioxygenase activity GO:0005783 endoplasmic reticulum GO:0005789 endoplasmic reticulum membrane GO:0016020 membrane GO:0030867 rough endoplasmic reticulum membrane GO:0070062 extracellular vesicular exosome GO:0032963 collagen metabolic process GO:0033823 procollagen glucosyltransferase activity
Organisms for which functions have been demonstratedHomo sapiens
Sequence length738
FASTA sequence>sp|O60568|PLOD3_HUMAN Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 OS=Homo sapiens GN=PLOD3 PE=1 SV=1 MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
Structure Information
PDB ID
Quaternary structure
Function 1
Function descriptionLysyl hydroxylase isoform 3, enzyme L-lysine-[procollagen] + 2-oxoglutarate + O(2) <=> (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2) Important for formation of intermolecular cross-links in collagen, helps provide strength to collagen acts at -Xaa-Lys-Gly- sequences
References for functionValtavaara M, Szpirer C, Szpirer J, Myllyl? R. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3. J Biol Chem. 1998 May 22. PMID: 9582318
E.C. number1.14.11.4
Location of functional site(s)Active site:729 Metal binding site:719,669,667
Cellular location of functionEndoplasmic Reticulum, Cytoplasmic membrane
Comments
Function 2
Function descriptionCollagen glucosyltransferase UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen = UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
References for functionHeikkinen J, Risteli M, Wang C, Latvala J, Rossi M, Valtavaara M, Myllyl? R. Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J Biol Chem. 2000 Nov 17. PMID: 10934207
E.C. number2.4.1.66
Location of functional site(s)
Cellular location of functionPlasma membrane
Comments