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Identification
HMDB Protein ID HMDBP00462
Secondary Accession Numbers
  • 5701
  • HMDBP03684
Name Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
Synonyms
  1. LH3
  2. Lysyl hydroxylase 3
Gene Name PLOD3
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Pathways
  • Lysine degradation
  • Other types of O-glycan biosynthesis
Reactions
L-lysine-[procollagen] + Oxoglutaric acid + Oxygen → (2S,5R)-5-hydroxy-L-lysine-[procollagen] + Succinic acid + CO(2) details
Protein lysine + Oxoglutaric acid + Oxygen → Procollagen 5-hydroxy-L-lysine + Succinic acid + Carbon dioxide + Water details
Uridine diphosphategalactose + Procollagen 5-hydroxy-L-lysine → Uridine 5'-diphosphate + 5-(D-Galactosyloxy)-L-lysine-procollagen details
Uridine diphosphate glucose + 5-(D-Galactosyloxy)-L-lysine-procollagen → Uridine 5'-diphosphate + 1,2-D-Glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen details
GO Classification
Biological Process
extracellular matrix organization
cellular response to hormone stimulus
cellular protein modification process
in utero embryonic development
vasodilation
protein localization
basement membrane assembly
endothelial cell morphogenesis
epidermis morphogenesis
lung morphogenesis
collagen fibril organization
neural tube development
Cellular Component
endoplasmic reticulum membrane
rough endoplasmic reticulum membrane
Component
endoplasmic reticulum
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
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
l-ascorbic acid binding
iron ion binding
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
vitamin binding
oxidoreductase activity
peptidyl-lysine 5-dioxygenase activity
procollagen-lysine 5-dioxygenase activity
Molecular Function
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
procollagen galactosyltransferase activity
L-ascorbic acid binding
iron ion binding
procollagen-lysine 5-dioxygenase activity
procollagen glucosyltransferase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Peripheral membrane protein
  2. Lumenal side
  3. Rough endoplasmic reticulum membrane
Gene Properties
Chromosome Location 7
Locus 7q22
SNPs PLOD3
Gene Sequence
>2217 bp
ATGACCTCCTCGGGGCCTGGACCCCGGTTCCTGCTGCTGCTGCCGCTGCTGCTGCCCCCT
GCGGCCTCAGCCTCCGACCGGCCCCGGGGCCGAGACCCGGTCAACCCAGAGAAGCTGCTG
GTGATCACTGTGGCCACAGCTGAAACCGAGGGGTACCTGCGTTTCCTGCGCTCTGCGGAG
TTCTTCAACTACACTGTGCGGACCCTGGGCCTGGGAGAGGAGTGGCGAGGGGGTGATGTG
GCTCGAACAGTTGGTGGAGGACAGAAGGTCCGGTGGTTAAAGAAGGAAATGGAGAAATAC
GCTGACCGGGAGGATATGATCATCATGTTTGTGGATAGCTACGACGTGATTCTGGCCGGC
AGCCCCACAGAGCTGCTGAAGAAGTTCGTCCAGAGTGGCAGCCGCCTGCTCTTCTCTGCA
GAGAGCTTCTGCTGGCCCGAGTGGGGGCTGGCGGAGCAGTACCCTGAGGTGGGCACGGGG
AAGCGCTTCCTCAATTCTGGTGGATTCATCGGTTTTGCCACCACCATCCACCAAATCGTG
CGCCAGTGGAAGTACAAGGATGATGACGACGACCAGCTGTTCTACACACGGCTCTACCTG
GACCCAGGACTGAGGGAGAAACTCAGCCTTAATCTGGATCATAAGTCTCGGATCTTTCAG
AACCTCAACGGGGCTTTAGATGAAGTGGTTTTAAAGTTTGATCGGAACCGTGTGCGTATC
CGGAACGTGGCCTACGACACGCTCCCCATTGTGGTCCATGGAAACGGTCCCACTAAGCTG
CAGCTCAACTACCTGGGAAACTACGTCCCCAATGGCTGGACTCCTGAGGGAGGCTGTGGC
TTCTGCAACCAGGACCGGAGGACACTCCCGGGGGGGCAGCCTCCCCCCCGGGTGTTTCTG
GCCGTGTTTGTGGAACAGCCTACTCCGTTTCTGCCCCGCTTCCTGCAGCGGCTGCTACTC
CTGGACTATCCCCCCGACAGGGTCACCCTTTTCCTGCACAACAACGAGGTCTTCCATGAA
CCCCACATCGCTGACTCCTGGCCGCAGCTCCAGGACCACTTCTCAGCTGTGAAGCTCGTG
GGGCCGGAGGAGGCTCTGAGCCCAGGCGAGGCCAGGGACATGGCCATGGACCTGTGTCGG
CAGGACCCCGAGTGTGAGTTCTACTTCAGCCTGGACGCCGACGCTGTCCTCACCAACCTG
CAGACCCTGCGTATCCTCATTGAGGAGAACAGGAAGGTGATCGCCCCCATGCTGTCCCGC
CACGGCAAGCTGTGGTCCAACTTCTGGGGCGCCCTGAGCCCCGATGAGTACTACGCCCGC
TCCGAGGACTACGTGGAGCTGGTGCAGCGGAAGCGAGTGGGTGTGTGGAATGTACCATAC
ATCTCCCAGGCCTATGTGATCCGGGGTGATACCCTGCGGATGGAGCTGCCCCAGAGGGAT
GTGTTCTCGGGCAGTGACACAGACCCGGACATGGCCTTCTGTAAGAGCTTTCGAGACAAG
GGCATCTTCCTCCATCTGAGCAATCAGCATGAATTTGGCCGGCTCCTGGCCACTTCCAGA
TACGACACGGAGCACCTGCACCCCGACCTCTGGCAGATCTTCGACAACCCCGTCGACTGG
AAGGAGCAGTACATCCACGAGAACTACAGCCGGGCCCTGGAAGGGGAAGGAATCGTGGAG
CAGCCATGCCCGGACGTGTACTGGTTCCCACTGCTGTCAGAACAAATGTGTGATGAGCTG
GTGGCAGAGATGGAGCACTACGGCCAGTGGTCAGGCGGCCGGCATGAGGATTCAAGGCTG
GCTGGAGGCTACGAGAATGTGCCCACCGTGGACATCCACATGAAGCAGGTGGGGTACGAG
GACCAGTGGCTGCAGCTGCTGCGGACGTATGTGGGCCCCATGACCGAGAGCCTGTTTCCC
GGTTACCACACCAAGGCGCGGGCGGTGATGAACTTTGTGGTTCGCTACCGGCCAGACGAG
CAGCCGTCTCTGCGGCCACACCACGACTCATCCACCTTCACCCTCAACGTTGCCCTCAAC
CACAAGGGCCTGGACTATGAGGGAGGTGGCTGCCGCTTCCTGCGCTACGACTGTGTGATC
TCCTCCCCGAGGAAGGGCTGGGCACTCCTGCACCCCGGCCGCCTCACCCACTACCACGAG
GGGCTGCCAACGACCTGGGGCACACGCTACATCATGGTGTCCTTTGTCGACCCCTGA
Protein Properties
Number of Residues 738
Molecular Weight 84784.505
Theoretical pI 6.055
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
GenBank ID Protein 3153235
UniProtKB/Swiss-Prot ID O60568
UniProtKB/Swiss-Prot Entry Name PLOD3_HUMAN
PDB IDs Not Available
GenBank Gene ID AF046889
GeneCard ID PLOD3
GenAtlas ID PLOD3
HGNC ID HGNC:9083
References
General References
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  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed:12853948 ]
  4. Valtavaara M, Szpirer C, Szpirer J, Myllyla R: Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) J Biol Chem. 1998 May 22;273(21):12881-6. [PubMed:9582318 ]
  5. Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10482-6. [PubMed:9724729 ]
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  7. Salo AM, Cox H, Farndon P, Moss C, Grindulis H, Risteli M, Robins SP, Myllyla R: A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene. Am J Hum Genet. 2008 Oct;83(4):495-503. doi: 10.1016/j.ajhg.2008.09.004. Epub 2008 Oct 2. [PubMed:18834968 ]