Plod3
entrez
26433
canonical
uniprot
Q9R0E1
canonical
ensembl
ENSMUSG00000004846
resolver
ensp
ENSMUSP00000004968
resolver
enst
ENSMUST00000004968
resolver
genesymbol
Plod3
resolver
uniprot
Q542E0
resolver
uniprot
Q9CYY9
resolver
uniprot_entry
PLOD3_MOUSE
resolver
uniprot_sec
Q542E0
resolver
uniprot_sec
Q9CYY9
resolver
amino_acid_sequence
MAAAGPEPRLLLLLLLLLPPLPPVTSASDRPRGANAVNPDKLLVITVATAETEGYRRFLQSAEFFNYTVRTLGLGQEWRGGDVARTVGGGQKVRWLKKEMEKYADQKDMIIMFVDSYDVILASSPTELLKKFVQSGSHLLFSAESFCWPEWGLAEQYPEVGMGKRFLNSGGFIGFAPTIHQIVRQWNYKDDDDDQLFYTQLYLDPGLREKLKLSLDHKSRIFQNLNGALDEVILKFDQNRVRIRNVAYDTLPVVVHGNGPTKLQLNYLGNYVPNGWTPQGGCGFCNQTLRTLPGGQPPPRVLLAVFVEQPTPFLPRFLQRLLLLDYPPDRISLFLHNSEVYHEPHIADAWPQLQDHFSAVKLVGPEEALSAGEARDMAMDSCRQNPECEFYFSLDADAVLTNPETLRVLIEQNRKVIAPMLSRHGKLWSNFWGALSPNEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGETLRTELPQKEVFSSSDTDPDMAFCKSVRDKGIFLHLSNQHEFGRLLATSRYDTDHLHPDLWQIFDNPVDWREQYIHENYSRALDGEGLVEQPCPDVYWFPLLTEQMCDELVEEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTEYLFPGYHTKTRAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGVDYEGGGCRFLRYDCRISSPRKGWALLHPGRLTHYHEGLPTTRGTRYIMVSFVDP
uniprot
proteins
ec_number
1.14.11.4
uniprot
proteins
ec_number
2.4.1.50
uniprot
proteins
ec_number
2.4.1.66
uniprot
proteins
function
FUNCTION: Multifunctional enzyme that catalyzes a series of post-translational modifications on Lys residues in procollagen (PubMed:16447251). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:16447251). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:16447251, PubMed:16467571, PubMed:21220425). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:25419660). Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:23209641). Essential for normal biosynthesis and secretion of type IV collagens (PubMed:15377789, PubMed:16467571, PubMed:17873278). Essential for normal formation of basement membranes (PubMed:15377789, PubMed:16467571). {ECO:0000250|UniProtKB:O60568, ECO:0000269|PubMed:15377789, ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571, ECO:0000269|PubMed:17873278, ECO:0000269|PubMed:21220425, ECO:0000269|PubMed:23209641, ECO:0000269|PubMed:25419660}.
uniprot
proteins
mass_dalton
84922
uniprot
proteins
mutagenesis
MUTAGEN 672; /note="D->A: Loss of lysyl hydroxylase activity. No effect on glycosyltransferase activity. Mutant mice are born at the expected Mendelian rate and have no visible phenotype, excepting decreased hydroxylysine modifications in type IV collagens in the skin."; /evidence="ECO:0000269|PubMed:16467571
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:16447251}.
uniprot
proteins
pubmed
10429951
uniprot
proteins
pubmed
11334715
uniprot
proteins
pubmed
15377789
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16447251
uniprot
proteins
pubmed
16467571
uniprot
proteins
pubmed
17873278
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21220425
uniprot
proteins
pubmed
21465473
uniprot
proteins
pubmed
23209641
uniprot
proteins
pubmed
25419660
uniprot
proteins
sequence_length
741
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16447251}; Peripheral membrane protein {ECO:0000305|PubMed:16447251}; Lumenal side {ECO:0000305|PubMed:16447251}. Secreted {ECO:0000269|PubMed:21465473}. Secreted, extracellular space {ECO:0000269|PubMed:16447251}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000269|PubMed:16447251}.
uniprot
proteins