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-APR-2013, entry version 95.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE EC=1.14.11.4;
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 Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; 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).
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.
CC -!- CATALYTIC ACTIVITY: L-lysine-[procollagen] + 2-oxoglutarate + O(2)
CC = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO(2).
CC -!- COFACTOR: Iron.
CC -!- COFACTOR: Ascorbate.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC Peripheral membrane protein; Lumenal side.
CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
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DR EMBL; M59183; AAA48945.1; -; mRNA.
DR IPI; IPI00574055; -.
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 GeneID; 419485; -.
DR KEGG; gga:419485; -.
DR CTD; 5351; -.
DR eggNOG; NOG311199; -.
DR HOGENOM; HOG000231099; -.
DR HOVERGEN; HBG053618; -.
DR InParanoid; P24802; -.
DR KO; K00473; -.
DR OrthoDB; EOG4K0QMV; -.
DR NextBio; 20822534; -.
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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:EC.
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 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
FT CHAIN 21 730 Procollagen-lysine,2-oxoglutarate 5-
FT dioxygenase 1.
FT /FTId=PRO_0000024682.
FT DOMAIN 639 730 Fe2OG dioxygenase.
FT ACT_SITE 721 721 Potential.
FT METAL 659 659 Iron (By similarity).
FT METAL 661 661 Iron (By similarity).
FT METAL 711 711 Iron (By similarity).
FT CARBOHYD 200 200 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 541 541 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 689 689 N-linked (GlcNAc...) (Potential).
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
//
