PLOD1_PONAB
ID PLOD1_PONAB Reviewed; 727 AA.
AC Q5R9N3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE EC=1.14.11.4 {ECO:0000250|UniProtKB:P24802};
DE AltName: Full=Lysyl hydroxylase 1;
DE Short=LH1;
DE Flags: Precursor;
GN Name=PLOD1;
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: Part of a complex composed of PLOD1, P3H3 and P3H4 that
CC catalyzes hydroxylation of lysine residues in collagen alpha chains and
CC is required for normal assembly and cross-linkling of collagen fibrils
CC (By similarity). Forms hydroxylysine residues in -Xaa-Lys-
CC Gly- sequences in collagens (By similarity). These hydroxylysines serve
CC as sites of attachment for carbohydrate units and are essential for the
CC stability of the intermolecular collagen cross-links (By similarity).
CC {ECO:0000250|UniProtKB:P24802, ECO:0000250|UniProtKB:Q9R0E2}.
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:P24802};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- SUBUNIT: Homodimer (By similarity). Identified in a complex with P3H3
CC and P3H4 (By similarity). {ECO:0000250|UniProtKB:P24802,
CC ECO:0000250|UniProtKB:Q9R0E2}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side
CC {ECO:0000250}.
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DR EMBL; CR859353; CAH91527.1; -; mRNA.
DR RefSeq; NP_001127428.1; NM_001133956.1.
DR AlphaFoldDB; Q5R9N3; -.
DR SMR; Q5R9N3; -.
DR STRING; 9601.ENSPPYP00000002169; -.
DR GeneID; 100174498; -.
DR KEGG; pon:100174498; -.
DR CTD; 5351; -.
DR eggNOG; KOG1971; Eukaryota.
DR InParanoid; Q5R9N3; -.
DR OrthoDB; 194164at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0008475; F:procollagen-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
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; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal; Vitamin C.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..727
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1"
FT /id="PRO_0000024680"
FT DOMAIN 636..727
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 718
FT /evidence="ECO:0000255"
FT BINDING 656
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 658
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 708
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 727 AA; 83563 MW; 33BFA74BCAF650EF CRC64;
MRPLLLLAPL GWLLLAEAKG DAKPEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQALGL
GEDWNVEKGT SAGGGQKVRL LKKALEKHAD KEDLVILFTD SYDVLFASGP RELLKKFRQA
RSQVVFSAEE LIYPDRRLET KYPVVSDGKR FLGSGGFIGY APNLSKLVAE WEGQDSDSDQ
LFYTRIFLDP EKREQINITL DHRCRIFQNL DGALDEVVLK FEMGHVRARN LAYDTLPVLI
HGNGPTKLQL NYLGNYIPRF WTFETGCTVC DEGLRSLKGI GDEALPTVLV GVFIEQPTPF
VSLFFQRLLR LHYPQKHMRL FIHNHEQHHK AQVEEFLAEH GSEYQSVKLV GPEVRMANAD
ARNMGADLCR QDRSCTYYFS VDADVALTEP SSLRLLIQQN KNVIAPLMTR HGRLWSNFWG
ALSADGYYAR SEDYVDIVQG RRVGVWNVPY ISNIYLIKGS ALRGELQSPD LFHHSKLDPD
MAFCANVRQQ DVFMFLTNRH TLGHLLSLDS YRTTHLHNDL WEVFSNPEDW KEKYIHQNYT
KALAGKLVET PCPDVYWFPI FTEVACDELV EEMEHFGQWS LGDNKDNRIQ GGYENVPTID
IHMNQIGFER EWHKFLLEYI APMTEKLYPG YYTRAQFDLA FVVRYKPDEQ PSLMPHHDAS
TFTINIALNR VGVDYEGGGC RFLRYNCSIR APRKGWTLMH PGRLTHYHEG LPTTRGTRYI
AVSFVDP
