PLOD3_RAT
ID PLOD3_RAT Reviewed; 741 AA.
AC Q5U367; Q811A5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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:12878181};
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:0000250|UniProtKB:O60568};
DE AltName: Full=Galactosylhydroxylysine-glucosyltransferase;
DE AltName: Full=Procollagen galactosyltransferase;
DE AltName: Full=Procollagen glucosyltransferase;
DE Flags: Precursor;
GN Name=Plod3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=12878181; DOI=10.1016/s0006-291x(03)01262-2;
RA Mercer D.K., Nicol P.F., Wright M.C., Robins S.P.;
RT "Identification, expression, and tissue distribution of the three rat lysyl
RT hydroxylase isoforms.";
RL Biochem. Biophys. Res. Commun. 307:803-809(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes a series of post-
CC translational modifications on Lys residues in procollagen. Plays a
CC redundant role in catalyzing the formation of hydroxylysine residues in
CC -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant
CC role in catalyzing the transfer of galactose onto hydroxylysine groups,
CC giving rise to galactosyl 5-hydroxylysine (By similarity). Has an
CC essential role by catalyzing the subsequent transfer of glucose
CC moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine
CC residues. Catalyzes hydroxylation and glycosylation of Lys residues in
CC the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-
CC glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation
CC and glycosylation of Lys residues in the ADIPOQ collagen-like domain,
CC giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine
CC residues. Essential for normal biosynthesis and secretion of type IV
CC collagens. Essential for normal formation of basement membranes (By
CC similarity). {ECO:0000250|UniProtKB:O60568,
CC ECO:0000250|UniProtKB:Q9R0E1}.
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:12878181};
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:0000250|UniProtKB:O60568};
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:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side
CC {ECO:0000250|UniProtKB:Q9R0E1}. Secreted
CC {ECO:0000250|UniProtKB:O60568}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted
CC protein is associated with the extracellular matrix.
CC {ECO:0000250|UniProtKB:Q9R0E1}.
CC -!- TISSUE SPECIFICITY: Detected in heart and bone.
CC {ECO:0000269|PubMed:12878181}.
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}.
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DR EMBL; AJ430859; CAD23628.1; -; mRNA.
DR EMBL; BC085683; AAH85683.1; -; mRNA.
DR RefSeq; NP_835202.2; NM_178101.3.
DR AlphaFoldDB; Q5U367; -.
DR SMR; Q5U367; -.
DR IntAct; Q5U367; 9.
DR STRING; 10116.ENSRNOP00000001921; -.
DR GlyGen; Q5U367; 2 sites.
DR jPOST; Q5U367; -.
DR PaxDb; Q5U367; -.
DR PRIDE; Q5U367; -.
DR Ensembl; ENSRNOT00000001921; ENSRNOP00000001921; ENSRNOG00000001417.
DR GeneID; 288583; -.
DR KEGG; rno:288583; -.
DR UCSC; RGD:631339; rat.
DR CTD; 8985; -.
DR RGD; 631339; Plod3.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_022320_1_0_1; -.
DR InParanoid; Q5U367; -.
DR OMA; NLFPGYH; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; Q5U367; -.
DR TreeFam; TF313826; -.
DR BRENDA; 1.14.11.4; 5301.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q5U367; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001417; Expressed in ovary and 20 other tissues.
DR Genevisible; Q5U367; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS: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; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0070831; P:basement membrane assembly; ISO:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0048730; P:epidermis morphogenesis; ISO:RGD.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR GO; GO:0021915; P:neural tube development; ISO:RGD.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; ISO:RGD.
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 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_0000041774"
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: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 CONFLICT 4..10
FT /note="SVPEPRL -> ISPGTPA (in Ref. 1; CAD23628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 85060 MW; E14883A4D2522767 CRC64;
MAASVPEPRL LLLLLLLLPP LPPVTSASDR PRGANPVNPD KLLVITVATA ETEGYRRFLQ
SAEFFNYTVR TLGLGQEWRG GDVARTVGGG QKVRWLKKEM EKYASQEDMI IMFVDSYDVI
LASSPTELLK KFVQSGSHLL FSAESFCWPD WGLAEQYPEV GVGKRFLNSG GFIGFAPTIH
RIVRQWKYKD DDDDQLFYTQ LYLDPGLREK LKLSLDHKSR IFQNLNGALD EVVLKFDQNR
VRIRNVAYDT LPVVVHGNGP TKLQLNYLGN YVPNGWTPQG GCGFCNLNRR TLPGGQPPPR
VLLAVFVEQP TPFLPRFLQR LLLLDYPPDR ISLFLHNNEV YHEPHIADAW PQLQDHFSAV
KLVGPEEALS SGEARDMAMD SCRQNPECEF YFSLDADAVL TNPETLRILI EQNRKVIAPM
LSRHGKLWSN FWGALSPDEY YARSEDYVEL VQRKRVGLWN VPYISQAYVI RGETLRTELP
EKEVFSSSDT DPDMAFCRSV RDKGIFLHLS NQHEFGRLLS TSHYDTDHLH PDLWQIFDNP
VDWREQYIHE NYSRALDGEG LVEQPCPDVY WFPLLTEQMC DELVEEMEHY GQWSGGRHED
SRLAGGYENV PTVDIHMKQV GYEDQWLQLL RTYVGPMTEH LFPGYHTKTR AVMNFVVRYR
PDEQPSLRPH HDSSTFTLNV ALNHKGVDYE GGGCRFLRYD CRVSSPRKGW ALLHPGRLTH
YHEGLPTTRG TRYIMVSFVD P
