Overview
| Uniprot ID | O60568 |
| Protein Name | Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 |
| Gene Name | PLOD3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 128 |
SPTELLKKFVQSGSR |
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)
Protein Sequence
10
MTSSGPGPRF
20
LLLLPLLLPP
30
AASASDRPRG
40
RDPVNPEKLL
50
VITVATAETE
60
GYLRFLRSAE
70
FFNYTVRTLG
80
LGEEWRGGDV
90
ARTVGGGQKV
100
RWLKKEMEKY
110
ADREDMIIMF
120
VDSYDVILAG
130
SPTELLKKFV
140
QSGSRLLFSA
150
ESFCWPEWGL
160
AEQYPEVGTG
170
KRFLNSGGFI
180
GFATTIHQIV
190
RQWKYKDDDD
200
DQLFYTRLYL
210
DPGLREKLSL
220
NLDHKSRIFQ
230
NLNGALDEVV
240
LKFDRNRVRI
250
RNVAYDTLPI
260
VVHGNGPTKL
270
QLNYLGNYVP
280
NGWTPEGGCG
290
FCNQDRRTLP
300
GGQPPPRVFL
310
AVFVEQPTPF
320
LPRFLQRLLL
330
LDYPPDRVTL
340
FLHNNEVFHE
350
PHIADSWPQL
360
QDHFSAVKLV
370
GPEEALSPGE
380
ARDMAMDLCR
390
QDPECEFYFS
400
LDADAVLTNL
410
QTLRILIEEN
420
RKVIAPMLSR
430
HGKLWSNFWG
440
ALSPDEYYAR
450
SEDYVELVQR
460
KRVGVWNVPY
470
ISQAYVIRGD
480
TLRMELPQRD
490
VFSGSDTDPD
500
MAFCKSFRDK
510
GIFLHLSNQH
520
EFGRLLATSR
530
YDTEHLHPDL
540
WQIFDNPVDW
550
KEQYIHENYS
560
RALEGEGIVE
570
QPCPDVYWFP
580
LLSEQMCDEL
590
VAEMEHYGQW
600
SGGRHEDSRL
610
AGGYENVPTV
620
DIHMKQVGYE
630
DQWLQLLRTY
640
VGPMTESLFP
650
GYHTKARAVM
660
NFVVRYRPDE
670
QPSLRPHHDS
680
STFTLNVALN
690
HKGLDYEGGG
700
CRFLRYDCVI
710
SSPRKGWALL
720
HPGRLTHYHE
730
GLPTTWGTRY
IMVSFVDP
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005788 |
endoplasmic reticulum lumen |
| Cellular Component |
GO:0005789 |
endoplasmic reticulum membrane |
| Cellular Component |
GO:0070062 |
extracellular exosome |
| Cellular Component |
GO:0031012 |
extracellular matrix |
| Cellular Component |
GO:0005615 |
extracellular space |
| Cellular Component |
GO:0005794 |
Golgi apparatus |
| Cellular Component |
GO:0005791 |
rough endoplasmic reticulum |
| Cellular Component |
GO:0005802 |
trans-Golgi network |
| Molecular Function |
GO:0005506 |
iron ion binding |
| Molecular Function |
GO:0031418 |
L-ascorbic acid binding |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0050211 |
procollagen galactosyltransferase activity |
| Molecular Function |
GO:0033823 |
procollagen glucosyltransferase activity |
| Molecular Function |
GO:0008475 |
procollagen-lysine 5-dioxygenase activity |
| Molecular Function |
GO:0036094 |
small molecule binding |
| Biological Process |
GO:0032964 |
collagen biosynthetic process |
| Biological Process |
GO:0030199 |
collagen fibril organization |
| Biological Process |
GO:0046947 |
hydroxylysine biosynthetic process |
| Biological Process |
GO:0180062 |
protein O-linked glycosylation via galactose |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.