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Database: UniProt/SWISS-PROT
Entry: PLOD1_CHICK
LinkDB: PLOD1_CHICK
Original site: 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   10-MAY-2017, entry version 114.
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;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-40; 412-417;
RP   508-515 AND 550-573.
RX   PubMed=1704364;
RA   Kivirikko K.I., Turpeenniemi-Hujanen T., Pajunen L., Pihlajaniemi T.,
RA   Myllylae R.;
RT   "Molecular cloning of chick lysyl hydroxylase. Little homology in
RT   primary structure to the two types of subunit of prolyl 4-
RT   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
RT   kinetics and related aspects.";
RL   Biochim. Biophys. Acta 611:40-50(1980).
CC   -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences
CC       in collagens. These hydroxylysines serve as sites of attachment
CC       for carbohydrate units and are essential for the stability of the
CC       intermolecular collagen cross-links. {ECO:0000269|PubMed:6779811}.
CC   -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2)
CC       = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2).
CC       {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;
CC       Peripheral membrane protein; Lumenal side.
DR   EMBL; M59183; AAA48945.1; -; mRNA.
DR   PIR; A23742; A23742.
DR   RefSeq; NP_001005618.1; NM_001005618.1.
DR   UniGene; Gga.4726; -.
DR   ProteinModelPortal; P24802; -.
DR   STRING; 9031.ENSGALP00000007204; -.
DR   PaxDb; P24802; -.
DR   PRIDE; P24802; -.
DR   GeneID; 419485; -.
DR   KEGG; gga:419485; -.
DR   CTD; 5351; -.
DR   eggNOG; KOG1971; Eukaryota.
DR   eggNOG; ENOG410Y4QU; LUCA.
DR   HOGENOM; HOG000231099; -.
DR   HOVERGEN; HBG053618; -.
DR   InParanoid; P24802; -.
DR   KO; K00473; -.
DR   PhylomeDB; P24802; -.
DR   PRO; PR:P24802; -.
DR   Proteomes; UP000000539; 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; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.550.10; -; 1.
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   Complete proteome; Dioxygenase; Direct protein sequencing;
KW   Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Reference proteome; Signal; Vitamin C.
FT   SIGNAL        1     20       {ECO:0000269|PubMed:1704364}.
FT   CHAIN        21    730       Procollagen-lysine,2-oxoglutarate 5-
FT                                dioxygenase 1.
FT                                /FTId=PRO_0000024682.
FT   DOMAIN      639    730       Fe2OG dioxygenase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   ACT_SITE    721    721       {ECO:0000255}.
FT   METAL       659    659       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       661    661       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       711    711       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    403    403       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    689    689       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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