PLOD1_CHICK
ID PLOD1_CHICK Reviewed; 730 AA.
AC P24802;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE EC=1.14.11.4 {ECO:0000269|PubMed:6766066, ECO:0000269|PubMed:6779811};
DE AltName: Full=Lysyl hydroxylase 1;
DE Short=LH1;
DE Flags: Precursor;
GN Name=PLOD1; Synonyms=PLOD;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-40; 412-417; 508-515
RP AND 550-573.
RX PubMed=1704364; DOI=10.1016/s0021-9258(18)49918-8;
RA Kivirikko K.I., Turpeenniemi-Hujanen T., Pajunen L., Pihlajaniemi T.,
RA Myllylae R.;
RT "Molecular cloning of chick lysyl hydroxylase. Little homology in primary
RT structure to the two types of subunit of prolyl 4-hydroxylase.";
RL J. Biol. Chem. 266:2805-2810(1991).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=6779811; DOI=10.1042/bj1890247;
RA Turpeenniemi-Hujanen T.M., Puistola U., Kivirikko K.I.;
RT "Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from
RT chick embryos as a homogeneous protein.";
RL Biochem. J. 189:247-253(1980).
RN [3]
RP CATALYTIC ACTIVITY, COFACTOR, ENZYME KINETICS, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=6766066; DOI=10.1016/0005-2744(80)90040-6;
RA Puistola U., Turpeenniemi-Hujanen T.M., Myllylae R., Kivirikko K.I.;
RT "Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics
RT and related aspects.";
RL Biochim. Biophys. Acta 611:40-50(1980).
CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in
CC collagens. These hydroxylysines serve as sites of attachment for
CC carbohydrate units and are essential for the stability of the
CC intermolecular collagen cross-links. {ECO:0000269|PubMed:6779811}.
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:6766066, ECO:0000269|PubMed:6779811};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:6766066};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:6766066};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for 2-oxoglutarate {ECO:0000269|PubMed:6766066};
CC KM=40 uM for O(2) {ECO:0000269|PubMed:6766066};
CC KM=190 uM for ascorbate {ECO:0000269|PubMed:6766066};
CC KM=400 uM for peptide substrate {ECO:0000269|PubMed:6766066};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6779811}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral
CC membrane protein; Lumenal side.
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DR EMBL; M59183; AAA48945.1; -; mRNA.
DR PIR; A23742; A23742.
DR RefSeq; NP_001005618.1; NM_001005618.1.
DR AlphaFoldDB; P24802; -.
DR SMR; P24802; -.
DR STRING; 9031.ENSGALP00000007204; -.
DR PaxDb; P24802; -.
DR GeneID; 419485; -.
DR KEGG; gga:419485; -.
DR CTD; 5351; -.
DR VEuPathDB; HostDB:geneid_419485; -.
DR eggNOG; KOG1971; Eukaryota.
DR InParanoid; P24802; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; P24802; -.
DR PRO; PR:P24802; -.
DR Proteomes; UP000000539; Unplaced.
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: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 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Signal; Vitamin C.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1704364"
FT CHAIN 21..730
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1"
FT /id="PRO_0000024682"
FT DOMAIN 639..730
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 721
FT /evidence="ECO:0000255"
FT BINDING 659
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 661
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 711
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 730 AA; 84318 MW; CE588F720D4F98E3 CRC64;
MVPPAVLLPW VVLPLLGVQG GSGSKQEENL LVLTVATKQT EGFRRFRRSA QFFNYKIQVL
GLDEEWKGGD DKKPAGGGQK VRLLKSALKQ HADKEDLVIL FIESYDVLFA SGPTELLKKF
KQAKSKVVFS AENYIYPDRK LEAKYPPVRD GKRFLGSGGF IGYAPNLKKL VEEWKGKDDD
SDQLFYTKIF LDPEKRENIN ISLDHRSRIF QNLNGALDEV VLKFENARVR ARNLLYDTLP
VIIHGNGPTK LQLNYLGNYI PQIWTFETGC TVCDEGLRSL TGIKDEALPM ILIGIFIEQP
TPFLSQFFLR LRNLHYPKQR IQIFIHNHEE HHSMQVDSFV KEHSKEYLAM KVIGPDDEVE
NAEARNLGMD LCRKDPDCDY YFSLDAEVVL KNTETLRILI EQNKSVIAPL VSRHEKLWSN
FWGALSPDGY YARSEDYVDI VQRRRVGLWN VPYISSVYMV KGKVLRSELD EGDLFHGGKL
DADMAFCHNV RNQGVFMYLT NRHQFGHILS LENYQTTHLH NDLWQIFSNP EDWREKYIHE
NYTAALKGKL VEMPCPDVYW FPIFTDTACD ELVEEMEHYG KWSTGDNTDS RIQGGYENVP
TIDIHMNQIG FEREWYKFLL DYIAPITEKL YPGYYTKTQF ELAFVVRYKP DEQPSLMPHH
DASTFTINIA LNRVGIDYEG GGCRFLRYNC SIRAPRKGWT LMHPGRLTHY HEGLPTTKGT
RYIAVSFIDP
