PLOD3_PONAB
ID PLOD3_PONAB Reviewed; 738 AA.
AC Q5R6K5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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:0000250|UniProtKB:O60568};
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O60568};
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 -!- 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; CR860483; CAH92605.1; -; mRNA.
DR RefSeq; NP_001128871.1; NM_001135399.1.
DR AlphaFoldDB; Q5R6K5; -.
DR SMR; Q5R6K5; -.
DR STRING; 9601.ENSPPYP00000019555; -.
DR PRIDE; Q5R6K5; -.
DR Ensembl; ENSPPYT00000020326; ENSPPYP00000019555; ENSPPYG00000017444.
DR GeneID; 100189797; -.
DR KEGG; pon:100189797; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR InParanoid; Q5R6K5; -.
DR OrthoDB; 194164at2759; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
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:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0048730; P:epidermis morphogenesis; IEA:Ensembl.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:Ensembl.
DR GO; GO:0042311; P:vasodilation; IEA:Ensembl.
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 2: Evidence at transcript 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..738
FT /note="Multifunctional procollagen lysine hydroxylase and
FT glycosyltransferase LH3"
FT /id="PRO_0000024688"
FT DOMAIN 647..738
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 25..290
FT /note="Required for glycosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT REGION 295..520
FT /note="Accessory region"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT REGION 672..715
FT /note="Important for dimerization"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 44..46
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 112..114
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 256..259
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 599
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 656
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 667
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 669
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 676
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT BINDING 719
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 729
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 279..282
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT DISULFID 379..385
FT /evidence="ECO:0000250|UniProtKB:O60568"
FT DISULFID 563..698
FT /evidence="ECO:0000250|UniProtKB:O60568"
SQ SEQUENCE 738 AA; 84785 MW; 5161767653568B5D CRC64;
MTSSGPGPRF LLLLPLLLPP AASASDRPRG RDPVNPEKLL VITVATAETE GYLRFLRSAE
FFNYTVRTLG LGEEWRGGDV ARTVGGGQKV RWLKKEMEKY ADREDMIIMF VDSYDVILAG
SPTELLKKFV QSGSRLLFSA ESFCWPEWGL AEQYPEVGTG KRFLNSGGFI GFATTIHQIV
RQWKYKDDDD DQLFYTRLYL DPGLREKLSL NLDHKSRIFQ NLNGALDEVV LKFDRNRVRI
RNVAYDTLPV VVHGNGPTKL QLNYLGNYVP KGWTPEGGCG FCNQDRRTLP GGQPPPRVFL
AVFVEQPTPF LPRFLQRLLL LDYPPDRVTL FLHNNEVFHE PHIADSWPQL QDHFSAVKLV
GPEEALSPGE ARDMAMDLCR QDPECEFYFS LDADTVLTNL QTLRILIEEN RKVIAPMLSR
HGKLWSNFWG ALSPDEYYAR SEDYVELVQR KRVGVWNVPY ISQAYVIRGD TLRTELPQRD
VFSGSDTDPD MAFCKSFRDK GIFLHLSNQH EFGRLLATSR YDTEHLHPDL WQIFDNPVDW
KEQYIHENYS RALEGEGIVE QPCPDVYWFP LLSEQMCDEL VAEMEHYGQW SGGRHEDSRL
AGGYENVPTV DIHMKQVGYE DQWLQLLRTY VGPMTESLFP GYHTKARAVM NFVVRYRPDE
QPSLRPHHDS STFTLNVALN HKGLDYEGGG CRFLRYDCVI SSPRKGWALL HPGRLTHYHE
GLPTTWGTRY IMVSFVDP
