PLOD3_MOUSE
ID PLOD3_MOUSE Reviewed; 741 AA.
AC Q9R0E1; Q542E0; Q9CYY9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3;
DE Includes:
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3;
DE EC=1.14.11.4 {ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571};
DE AltName: Full=Lysyl hydroxylase 3;
DE Short=LH3;
DE Includes:
DE RecName: Full=Procollagen glycosyltransferase;
DE EC=2.4.1.50 {ECO:0000250|UniProtKB:O60568};
DE EC=2.4.1.66 {ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571, ECO:0000269|PubMed:21220425};
DE AltName: Full=Galactosylhydroxylysine-glucosyltransferase;
DE AltName: Full=Procollagen galactosyltransferase;
DE AltName: Full=Procollagen glucosyltransferase;
DE Flags: Precursor;
GN Name=Plod3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10429951; DOI=10.1016/s0945-053x(99)00016-5;
RA Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.;
RT "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their
RT phylogenetic analysis and tissue-specific expression in the mouse.";
RL Matrix Biol. 18:325-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11334715; DOI=10.1016/s0945-053x(01)00130-5;
RA Ruotsalainen H., Vanhatupa S., Tampio M., Sipila L., Valtavaara M.,
RA Myllylae R.;
RT "Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl
RT hydroxylase 3/collagen glucosyltransferase.";
RL Matrix Biol. 20:137-146(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15377789; DOI=10.1073/pnas.0404966101;
RA Rautavuoma K., Takaluoma K., Sormunen R., Myllyharju J., Kivirikko K.I.,
RA Soininen R.;
RT "Premature aggregation of type IV collagen and early lethality in lysyl
RT hydroxylase 3 null mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14120-14125(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RX PubMed=16447251; DOI=10.1002/jcp.20596;
RA Salo A.M., Wang C., Sipilae L., Sormunen R., Vapola M., Kervinen P.,
RA Ruotsalainen H., Heikkinen J., Myllylae R.;
RT "Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a
RT novel mechanism for matrix remodeling.";
RL J. Cell. Physiol. 207:644-653(2006).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-672,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16467571; DOI=10.1242/jcs.02780;
RA Ruotsalainen H., Sipilae L., Vapola M., Sormunen R., Salo A.M., Uitto L.,
RA Mercer D.K., Robins S.P., Risteli M., Aszodi A., Faessler R., Myllylae R.;
RT "Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement
RT membranes.";
RL J. Cell Sci. 119:625-635(2006).
RN [8]
RP FUNCTION.
RX PubMed=17873278; DOI=10.1074/jbc.m704198200;
RA Sipilae L., Ruotsalainen H., Sormunen R., Baker N.L., Lamande S.R.,
RA Vapola M., Wang C., Sado Y., Aszodi A., Myllylae R.;
RT "Secretion and assembly of type IV and VI collagens depend on glycosylation
RT of hydroxylysines.";
RL J. Biol. Chem. 282:33381-33388(2007).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21220425; DOI=10.1074/jbc.m110.178509;
RA Sricholpech M., Perdivara I., Nagaoka H., Yokoyama M., Tomer K.B.,
RA Yamauchi M.;
RT "Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type
RT I collagen in osteoblast culture.";
RL J. Biol. Chem. 286:8846-8856(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=21465473; DOI=10.1002/jcp.22774;
RA Wang C., Ristiluoma M.M., Salo A.M., Eskelinen S., Myllylae R.;
RT "Lysyl hydroxylase 3 is secreted from cells by two pathways.";
RL J. Cell. Physiol. 227:668-675(2012).
RN [13]
RP FUNCTION.
RX PubMed=23209641; DOI=10.1371/journal.pone.0050045;
RA Ruotsalainen H., Risteli M., Wang C., Wang Y., Karppinen M., Bergmann U.,
RA Kvist A.P., Pospiech H., Herzig K.H., Myllylae R.;
RT "The activities of lysyl hydroxylase 3 (LH3) regulate the amount and
RT oligomerization status of adiponectin.";
RL PLoS ONE 7:E50045-E50045(2012).
RN [14]
RP FUNCTION.
RX PubMed=25419660; DOI=10.1371/journal.pone.0113498;
RA Risteli M., Ruotsalainen H., Bergmann U., Venkatraman Girija U., Wallis R.,
RA Myllylae R.;
RT "Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization
RT of mannan-binding lectin.";
RL PLoS ONE 9:E113498-E113498(2014).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes a series of post-
CC translational modifications on Lys residues in procollagen
CC (PubMed:16447251). Plays a redundant role in catalyzing the formation
CC of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens
CC (PubMed:16447251). Plays a redundant role in catalyzing the transfer of
CC galactose onto hydroxylysine groups, giving rise to galactosyl 5-
CC hydroxylysine (By similarity). Has an essential role by catalyzing the
CC subsequent transfer of glucose moieties, giving rise to 1,2-
CC glucosylgalactosyl-5-hydroxylysine residues (PubMed:16447251,
CC PubMed:16467571, PubMed:21220425). Catalyzes hydroxylation and
CC glycosylation of Lys residues in the MBL1 collagen-like domain, giving
CC rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine
CC residues (PubMed:25419660). Catalyzes hydroxylation and glycosylation
CC of Lys residues in the ADIPOQ collagen-like domain, giving rise to
CC hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues
CC (PubMed:23209641). Essential for normal biosynthesis and secretion of
CC type IV collagens (PubMed:15377789, PubMed:16467571, PubMed:17873278).
CC Essential for normal formation of basement membranes (PubMed:15377789,
CC PubMed:16467571). {ECO:0000250|UniProtKB:O60568,
CC ECO:0000269|PubMed:15377789, ECO:0000269|PubMed:16447251,
CC ECO:0000269|PubMed:16467571, ECO:0000269|PubMed:17873278,
CC ECO:0000269|PubMed:21220425, ECO:0000269|PubMed:23209641,
CC ECO:0000269|PubMed:25419660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC Evidence={ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose =
CC (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H(+) +
CC UDP; Xref=Rhea:RHEA:12637, Rhea:RHEA-COMP:12752, Rhea:RHEA-
CC COMP:12753, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133442, ChEBI:CHEBI:133443; EC=2.4.1.50;
CC Evidence={ECO:0000250|UniProtKB:O60568};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] +
CC UDP-alpha-D-glucose = (5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-
CC galactosyl]-5-hydroxy-L-lysyl-[collagen] + H(+) + UDP;
CC Xref=Rhea:RHEA:12576, Rhea:RHEA-COMP:12753, Rhea:RHEA-COMP:12754,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:133443, ChEBI:CHEBI:133452; EC=2.4.1.66;
CC Evidence={ECO:0000269|PubMed:16447251, ECO:0000269|PubMed:16467571,
CC ECO:0000269|PubMed:21220425};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O60568};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:O60568};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O60568};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O60568}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:O60568}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16447251}; Peripheral membrane protein
CC {ECO:0000305|PubMed:16447251}; Lumenal side
CC {ECO:0000305|PubMed:16447251}. Secreted {ECO:0000269|PubMed:21465473}.
CC Secreted, extracellular space {ECO:0000269|PubMed:16447251}. Note=The
CC majority of the secreted protein is associated with the extracellular
CC matrix. {ECO:0000269|PubMed:16447251}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum, heart, brain, liver,
CC kidney, lung, spleen, muscle and testis (at protein level)
CC (PubMed:16447251). Highly expressed in the heart, lung, liver and
CC testis (PubMed:10429951). Detected in the walls of blood vessels in
CC placenta and embryos. Detected in chondrocytes in embryos at 14.5 dpc
CC and in adults, in adult kidney mesangium and vascular poles of kidney
CC glomeruli (PubMed:15377789). Detected around nerves and in the adrenal
CC gland (PubMed:15377789). {ECO:0000269|PubMed:10429951,
CC ECO:0000269|PubMed:15377789, ECO:0000269|PubMed:16447251}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos (at protein level)
CC (PubMed:16467571). Ubiquitous and strongly expressed in embryos at 8.5
CC to 9.5 dpc. Expression becomes more restricted during embryonic
CC development. Highly expressed in head, eye lens and developing bones at
CC 12.5 dpc. Expression in the eye is decreased by 14.5 dpc. Detected in
CC capillaries and in the photoreceptor layer in the adult eye
CC (PubMed:15377789). {ECO:0000269|PubMed:15377789,
CC ECO:0000269|PubMed:16467571}.
CC -!- DOMAIN: The N-terminal domain mediates glycosyltransferase activity.
CC {ECO:0000250|UniProtKB:O60568}.
CC -!- DOMAIN: The C-terminal domain that mediates lysyl hydroxylase activity
CC is also important for homodimerization. {ECO:0000250|UniProtKB:O60568}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16447251}.
CC -!- DISRUPTION PHENOTYPE: Full embryonic lethality. Mutant embryos are much
CC smaller than wild-type by 9.5 dpc, and the majority are dead by 10.5
CC dpc. At 9.5 dpc, mutant embryos display fragmentation of basement
CC membranes (PubMed:15377789, PubMed:16467571). The majority of the
CC mutant embryos display dilated blood vessels, particularly in the
CC region of the sinus venosus (PubMed:16467571). Mutant embryos display
CC no decrease in global lysyl hydroxylase activity, due to the expression
CC of other lysyl hydroxylases (PubMed:15377789). Mutant embryos display a
CC nearly complete loss of procollagen glucosyltransferase activity
CC (PubMed:15377789, PubMed:16467571). {ECO:0000269|PubMed:15377789,
CC ECO:0000269|PubMed:16467571}.
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DR EMBL; AF046783; AAD54618.1; -; mRNA.
DR EMBL; AY014830; AAK00576.1; -; Genomic_DNA.
DR EMBL; AK013195; BAB28704.1; -; mRNA.
DR EMBL; AK033360; BAC28246.1; -; mRNA.
DR EMBL; AK088948; BAC40669.1; -; mRNA.
DR EMBL; BC043047; AAH43047.1; -; mRNA.
DR EMBL; BC054734; AAH54734.1; -; mRNA.
DR CCDS; CCDS19759.1; -.
DR RefSeq; NP_036092.1; NM_011962.3.
DR AlphaFoldDB; Q9R0E1; -.
DR SMR; Q9R0E1; -.
DR BioGRID; 204985; 22.
DR IntAct; Q9R0E1; 1.
DR MINT; Q9R0E1; -.
DR STRING; 10090.ENSMUSP00000004968; -.
DR GlyConnect; 2609; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9R0E1; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9R0E1; -.
DR PhosphoSitePlus; Q9R0E1; -.
DR EPD; Q9R0E1; -.
DR MaxQB; Q9R0E1; -.
DR PaxDb; Q9R0E1; -.
DR PeptideAtlas; Q9R0E1; -.
DR PRIDE; Q9R0E1; -.
DR ProteomicsDB; 289449; -.
DR Antibodypedia; 16729; 190 antibodies from 26 providers.
DR DNASU; 26433; -.
DR Ensembl; ENSMUST00000004968; ENSMUSP00000004968; ENSMUSG00000004846.
DR GeneID; 26433; -.
DR KEGG; mmu:26433; -.
DR UCSC; uc009abj.2; mouse.
DR CTD; 8985; -.
DR MGI; MGI:1347008; Plod3.
DR VEuPathDB; HostDB:ENSMUSG00000004846; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_022320_1_0_1; -.
DR InParanoid; Q9R0E1; -.
DR OMA; NLFPGYH; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; Q9R0E1; -.
DR TreeFam; TF313826; -.
DR BRENDA; 1.14.11.4; 3474.
DR BRENDA; 2.4.1.66; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 26433; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Plod3; mouse.
DR PRO; PR:Q9R0E1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R0E1; protein.
DR Bgee; ENSMUSG00000004846; Expressed in granulocyte and 227 other tissues.
DR ExpressionAtlas; Q9R0E1; baseline and differential.
DR Genevisible; Q9R0E1; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0050211; F:procollagen galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0033823; F:procollagen glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0070831; P:basement membrane assembly; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR001006; Procol_lys_dOase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Iron; Manganese; Membrane; Metal-binding;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome; Secreted;
KW Signal; Transferase; Vitamin C.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..741
FT /note="Multifunctional procollagen lysine hydroxylase and
FT glycosyltransferase LH3"
FT /id="PRO_0000024687"
FT DOMAIN 650..741
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 28..293
FT /note="Required for glycosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT REGION 298..523
FT /note="Accessory region"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT REGION 675..718
FT /note="Important for dimerization"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 47..49
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 115..117
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 259..262
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 602
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 659
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 670
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 672
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 679
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 722
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 732
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 282..285
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT DISULFID 382..388
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT DISULFID 566..701
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT MUTAGEN 672
FT /note="D->A: Loss of lysyl hydroxylase activity. No effect
FT on glycosyltransferase activity. Mutant mice are born at
FT the expected Mendelian rate and have no visible phenotype,
FT excepting decreased hydroxylysine modifications in type IV
FT collagens in the skin."
FT /evidence="ECO:0000269|PubMed:16467571"
FT CONFLICT 8
FT /note="P -> H (in Ref. 3; BAB28704)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 84922 MW; D1B79B386339D9F4 CRC64;
MAAAGPEPRL LLLLLLLLPP LPPVTSASDR PRGANAVNPD KLLVITVATA ETEGYRRFLQ
SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM EKYADQKDMI IMFVDSYDVI
LASSPTELLK KFVQSGSHLL FSAESFCWPE WGLAEQYPEV GMGKRFLNSG GFIGFAPTIH
QIVRQWNYKD DDDDQLFYTQ LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVILKFDQNR
VRIRNVAYDT LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNQTLR TLPGGQPPPR
VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNSEV YHEPHIADAW PQLQDHFSAV
KLVGPEEALS AGEARDMAMD SCRQNPECEF YFSLDADAVL TNPETLRVLI EQNRKVIAPM
LSRHGKLWSN FWGALSPNEY YARSEDYVEL VQRKRVGVWN VPYISQAYVI RGETLRTELP
QKEVFSSSDT DPDMAFCKSV RDKGIFLHLS NQHEFGRLLA TSRYDTDHLH PDLWQIFDNP
VDWREQYIHE NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED
SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEY LFPGYHTKTR AVMNFVVRYR
PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD CRISSPRKGW ALLHPGRLTH
YHEGLPTTRG TRYIMVSFVD P
