PLOD3
entrez
8985
canonical
uniprot
O60568
canonical
ensembl
ENSG00000106397
resolver
ensp
ENSP00000223127
resolver
ensp
ENSP00000560328
resolver
ensp
ENSP00000560329
resolver
ensp
ENSP00000560330
resolver
enst
ENST00000223127
resolver
enst
ENST00000890269
resolver
enst
ENST00000890270
resolver
enst
ENST00000890271
resolver
genesymbol
PLOD3
resolver
hgnc
HGNC:9083
resolver
uniprot
B2R6W6
resolver
uniprot
Q540C3
resolver
uniprot_entry
PLOD3_HUMAN
resolver
uniprot_sec
B2R6W6
resolver
uniprot_sec
Q540C3
resolver
activity_regulation
ACTIVITY REGULATION: Lysyl hydroxylase activity is strongly inhibited by imidazole. {ECO:0000269|PubMed:10934207}.
uniprot
proteins
amino_acid_sequence
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
uniprot
proteins
disease_involvement
DISEASE: BCARD syndrome (BCARD) [MIM:612394]: An autosomal recessive connective tissue disorder, secondary to lysyl hydroxylase 3 deficiency. It is characterized by congenital malformations severely affecting multiple tissues and organs. Clinical features include growth retardation, craniofacial dysmorphism, popliteal and cerebral aneurysm, cerebral arterial hemorrhage, skin blistering and easy bruisability, and osteopenia. {ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:30237576}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 essential post-translational modifications on Lys residues in procollagen (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812, PubMed:9582318, PubMed:9724729). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:10934207, PubMed:11896059, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). 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). Essential for normal biosynthesis and secretion of type IV collagens (Probable) (PubMed:18834968). Essential for normal formation of basement membranes (By similarity). {ECO:0000250|UniProtKB:Q9R0E1, ECO:0000269|PubMed:10934207, ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:11956192, ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658, ECO:0000269|PubMed:18834968, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:30089812, ECO:0000269|PubMed:9582318, ECO:0000269|PubMed:9724729, ECO:0000305}.
uniprot
proteins
mass_dalton
84785
uniprot
proteins
mutagenesis
MUTAGEN 75; /note="W->A: Decreased lysyl hydroxylase activity and loss of glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812"; MUTAGEN 114; /note="Y->A: Decreased lysyl hydroxylase and glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812"; MUTAGEN 144; /note="C->I: Strongly reduced glucosyltransferase activity. Strongly reduced galactosyltransferase activity."; /evidence="ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:12475640"; MUTAGEN 187..191; /note="DDDDD->ADAAA: Loss of glucosyltransferase activity. Loss of galactosyltransferase activity."; /evidence="ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:12475640, ECO:0000269|PubMed:18298658"; MUTAGEN 187..189; /note="DDD->ADA: Nearly abolishes glucosyltransferase activity. Nearly abolishes galactosyltransferase activity."; /evidence="ECO:0000269|PubMed:11896059, ECO:0000269|PubMed:12475640"; MUTAGEN 208; /note="L->I: Reduced glucosyltransferase activity."; /evidence="ECO:0000269|PubMed:11896059"; MUTAGEN 669; /note="D->A: Strongly decreased lysyl hydroxylase activity. No effect on glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:10934207, ECO:0000269|PubMed:18298658"; MUTAGEN 672; /note="T->N: Loss of dimerization. Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812"; MUTAGEN 714; /note="R->N: Loss of dimerization. Loss of lysyl hydroxylase activity and no effect on glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812"; MUTAGEN 715; /note="L->D: No effect on dimerization, lysyl hydroxylase and glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812"; MUTAGEN 715; /note="L->R: Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity."; /evidence="ECO:0000269|PubMed:30089812
uniprot
proteins
pubmed
10686427
uniprot
proteins
pubmed
10934207
uniprot
proteins
pubmed
11896059
uniprot
proteins
pubmed
11956192
uniprot
proteins
pubmed
12475640
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18298658
uniprot
proteins
pubmed
18834968
uniprot
proteins
pubmed
20470363
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21465473
uniprot
proteins
pubmed
25419660
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
30089812
uniprot
proteins
pubmed
30237576
uniprot
proteins
pubmed
9582318
uniprot
proteins
pubmed
9724729
uniprot
proteins
sequence_length
738
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000269|PubMed:10934207}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:20470363}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side {ECO:0000250|UniProtKB:Q9R0E1}. Secreted {ECO:0000269|PubMed:21465473}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000250|UniProtKB:Q9R0E1}.
uniprot
proteins