PLOD1_RAT
ID PLOD1_RAT Reviewed; 728 AA.
AC Q63321;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE EC=1.14.11.4 {ECO:0000269|PubMed:7578263};
DE AltName: Full=Lysyl hydroxylase 1;
DE Short=LH1;
DE Flags: Precursor;
GN Name=Plod1; Synonyms=Plod;
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 FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=7578263; DOI=10.1016/0167-4781(95)00130-9;
RA Armstrong L.C., Last J.A.;
RT "Rat lysyl hydroxylase: molecular cloning, mRNA distribution and expression
RT in a baculovirus system.";
RL Biochim. Biophys. Acta 1264:93-102(1995).
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 (PubMed:7578263). These hydroxylysines
CC serve as sites of attachment for carbohydrate units and are essential
CC for the stability of the intermolecular collagen cross-links (By
CC similarity). {ECO:0000250|UniProtKB:P24802,
CC ECO:0000250|UniProtKB:Q9R0E2, ECO:0000269|PubMed:7578263}.
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:7578263};
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; Peripheral
CC membrane protein; Lumenal side.
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DR EMBL; L25331; AAA41550.1; -; mRNA.
DR PIR; S59964; S59964.
DR AlphaFoldDB; Q63321; -.
DR SMR; Q63321; -.
DR IntAct; Q63321; 1.
DR STRING; 10116.ENSRNOP00000010433; -.
DR GlyGen; Q63321; 4 sites.
DR jPOST; Q63321; -.
DR PaxDb; Q63321; -.
DR PRIDE; Q63321; -.
DR UCSC; RGD:621382; rat.
DR RGD; 621382; Plod1.
DR eggNOG; KOG1971; Eukaryota.
DR InParanoid; Q63321; -.
DR PhylomeDB; Q63321; -.
DR BRENDA; 1.14.11.4; 5301.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q63321; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902494; C:catalytic complex; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008198; F:ferrous iron binding; IMP:RGD.
DR GO; GO:0031418; F:L-ascorbic acid binding; IMP:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
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; 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..728
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1"
FT /id="PRO_0000024681"
FT DOMAIN 637..728
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 719
FT /evidence="ECO:0000255"
FT BINDING 657
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 659
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 709
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 83612 MW; 3CAE198EB0742DF1 CRC64;
MRSLLLLASL AWLLLAQAKD DAKLEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQSLGL
GEDWSAAGGP SAAGGGQKVR LLKKALKKYA DKEDLVILFV DSYDVVFASG PRELLKKFQQ
AKSRVVFSAE ELIYPDRRLE AKYPTVPDGK RFLGSGGFIG YAPSLSKLVA EWEGQDNDSD
QLFYTKIFLD PEKREQINIS LDHRCRIFQN LDGALDEVVL KFEMGHVRAR NLAYDTLPVV
IHGNGPTKLQ VNYLGNYIPR FWTFETGCTV CDEGLRSLKG IGDEALPTVL VGVFIEQPTP
FLSLFFRRLL HLRYPQKQMR LFIHNQEQHH KLQVEQFLAE HGGEYQSVKL VGPEVRMANA
DARNMGADLC RQDQTCTYYF SVDADVALTE PNSLRLLIEQ NKNVIAPLMT RHGRLWSNFW
GALSADGYYA RSEDYVDIVQ GRRVGVWNVP YISNIYLIKG SALRAELRHV DLFHYSKLDP
DMSFCANVRQ QEVFMFLTNR HTFGHLLSLD NYQTTHLHND LWEVFSNPQD WKEKYIHENY
TKALAGKLVE TPCPDVYWFP IFTEVACDEL VEEMEHYGQW SLGDNKDNRI QGGYENVPTI
DIHMNQITFE REWHKFLVEY IAPLTEKLYP GYYTKAQFDL AFVVRYKPDE QPSLMPHHDA
STFTINIALN RVGEDYEGGG CRFLRYNCSV RAPRKGWALM HPGRLTHYHE GLPTTKGTRY
IAVSFVDP
