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'''Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3''' is an [[enzyme]] that in humans is encoded by the ''PLOD3'' [[gene]].<ref name="pmid9724729">{{cite journal | vauthors = Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI | title = Cloning and characterization of a third human lysyl hydroxylase isoform | journal = Proc Natl Acad Sci U S A | volume = 95 | issue = 18 | pages = 10482–6 |date=Sep 1998 | pmid = 9724729 | pmc = 27920 | doi =10.1073/pnas.95.18.10482  }}</ref><ref name="pmid9582318">{{cite journal | vauthors = Valtavaara M, Szpirer C, Szpirer J, Myllyla R | title = Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) | journal = J Biol Chem | volume = 273 | issue = 21 | pages = 12881–6 |date=Jun 1998 | pmid = 9582318 | pmc =  | doi =10.1074/jbc.273.21.12881 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8985| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3
| HGNCid = 9083
| Symbol = PLOD3
| AltSymbols =; LH3
| OMIM = 603066
| ECnumber = 
| Homologene = 843
| MGIid = 1347008
| GeneAtlas_image1 = PBB_GE_PLOD3_202185_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008475 |text = procollagen-lysine 5-dioxygenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016702 |text = oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen}} {{GNF_GO|id=GO:0031418 |text = L-ascorbic acid binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}}  
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0019538 |text = protein metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8985
    | Hs_Ensembl = ENSG00000106397
    | Hs_RefseqProtein = NP_001075
    | Hs_RefseqmRNA = NM_001084
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 100635979
    | Hs_GenLoc_end = 100647731
    | Hs_Uniprot = O60568
    | Mm_EntrezGene = 26433
    | Mm_Ensembl = ENSMUSG00000004846
    | Mm_RefseqmRNA = NM_011962
    | Mm_RefseqProtein = NP_036092
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 137271646
    | Mm_GenLoc_end = 137281164
    | Mm_Uniprot = Q9R0E1
  }}
}}
'''Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3''', also known as '''PLOD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8985| accessdate = }}</ref>


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| section_title =  
| summary_text = The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.<ref name="entrez">{{cite web | title = Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8985| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Salo AM, Wang C, Sipilä L, ''et al.'' |title=Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. |journal=J. Cell. Physiol. |volume=207 |issue= 3 |pages= 644-53 |year= 2006 |pmid= 16447251 |doi= 10.1002/jcp.20596 }}
*{{cite journal   |vauthors=Salo AM, Wang C, Sipilä L, etal |title=Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. |journal=J. Cell. Physiol. |volume=207 |issue= 3 |pages= 644–53 |year= 2006 |pmid= 16447251 |doi= 10.1002/jcp.20596 }}
*{{cite journal | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal   |vauthors=Otsuki T, Ota T, Nishikawa T, etal |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal   |vauthors=Hillier LW, Fulton RS, Fulton LA, etal |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Wang C, Luosujärvi H, Heikkinen J, ''et al.'' |title=The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. |journal=Matrix Biol. |volume=21 |issue= 7 |pages= 559-66 |year= 2003 |pmid= 12475640 |doi=  }}
*{{cite journal   |vauthors=Wang C, Luosujärvi H, Heikkinen J, etal |title=The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. |journal=Matrix Biol. |volume=21 |issue= 7 |pages= 559–66 |year= 2003 |pmid= 12475640 |doi=10.1016/S0945-053X(02)00071-9 }}
*{{cite journal | author=Rautavuoma K, Takaluoma K, Passoja K, ''et al.'' |title=Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 23084-91 |year= 2002 |pmid= 11956192 |doi= 10.1074/jbc.M112077200 }}
*{{cite journal   |vauthors=Rautavuoma K, Takaluoma K, Passoja K, etal |title=Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 23084–91 |year= 2002 |pmid= 11956192 |doi= 10.1074/jbc.M112077200 }}
*{{cite journal | author=Ruotsalainen H, Vanhatupa S, Tampio M, ''et al.'' |title=Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. |journal=Matrix Biol. |volume=20 |issue= 2 |pages= 137-46 |year= 2001 |pmid= 11334715 |doi=  }}
*{{cite journal   |vauthors=Ruotsalainen H, Vanhatupa S, Tampio M, etal |title=Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. |journal=Matrix Biol. |volume=20 |issue= 2 |pages= 137–46 |year= 2001 |pmid= 11334715 |doi=10.1016/S0945-053X(01)00130-5 }}
*{{cite journal | author=Heikkinen J, Risteli M, Wang C, ''et al.'' |title=Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36158-63 |year= 2000 |pmid= 10934207 |doi= 10.1074/jbc.M006203200 }}
*{{cite journal   |vauthors=Heikkinen J, Risteli M, Wang C, etal |title=Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36158–63 |year= 2000 |pmid= 10934207 |doi= 10.1074/jbc.M006203200 }}
*{{cite journal  | author=Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI |title=Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). |journal=Matrix Biol. |volume=19 |issue= 1 |pages= 73-9 |year= 2000 |pmid= 10686427 |doi= }}
*{{cite journal  | vauthors=Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI |title=Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). |journal=Matrix Biol. |volume=19 |issue= 1 |pages= 73–9 |year= 2000 |pmid= 10686427 |doi=10.1016/S0945-053X(99)00058-X }}
*{{cite journal  | author=Passoja K, Rautavuoma K, Ala-Kokko L, ''et al.'' |title=Cloning and characterization of a third human lysyl hydroxylase isoform. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10482-6 |year= 1998 |pmid= 9724729 |doi=  }}
*{{cite journal  | author=Valtavaara M, Szpirer C, Szpirer J, Myllylä R |title=Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 12881-6 |year= 1998 |pmid= 9582318 |doi= }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:18, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 is an enzyme that in humans is encoded by the PLOD3 gene.[1][2][3]

The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity.[3]

References

  1. ↑ Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI (Sep 1998). "Cloning and characterization of a third human lysyl hydroxylase isoform". Proc Natl Acad Sci U S A. 95 (18): 10482–6. doi:10.1073/pnas.95.18.10482. PMC 27920. PMID 9724729.
  2. ↑ Valtavaara M, Szpirer C, Szpirer J, Myllyla R (Jun 1998). "Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3)". J Biol Chem. 273 (21): 12881–6. doi:10.1074/jbc.273.21.12881. PMID 9582318.
  3. ↑ 3.0 3.1 "Entrez Gene: PLOD3 procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3".

Further reading



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