Reviewed, UniProtKB/Swiss-Prot P24802 (PLOD1_CHICK)

Names and origin

Protein names

Recommended name:
    Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
    EC=1.14.11.4
Alternative name(s):
    Lysyl hydroxylase 1
      Short name=LH1

Gene names

Name:	PLOD1
Synonyms:	PLOD

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	730 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Catalytic activity	Procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Cofactor	Iron. Ascorbate.
Subunit structure	Homodimer.
Subcellular location	Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
Sequence similarities	Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal
Ligand	Iron Metal-binding Vitamin C
Molecular function	Dioxygenase Oxidoreductase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW procollagen-lysine 5-dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Ref.1
	Chain	21 – 730	710	Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1		PRO_0000024682
Regions
	Domain	556 – 730	175	PKHD
Sites
	Active site	721	1	Potential
	Metal binding	659	1	Iron By similarity
	Metal binding	661	1	Iron By similarity
	Metal binding	711	1	Iron By similarity
Amino acid modifications
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	403	1	N-linked (GlcNAc...) Potential
	Glycosylation	541	1	N-linked (GlcNAc...) Potential
	Glycosylation	689	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P24802-1 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: CE588F720D4F98E3	FASTA	730	84,318
	10 20 30 40 50 60 MVPPAVLLPW VVLPLLGVQG GSGSKQEENL LVLTVATKQT EGFRRFRRSA QFFNYKIQVL 70 80 90 100 110 120 GLDEEWKGGD DKKPAGGGQK VRLLKSALKQ HADKEDLVIL FIESYDVLFA SGPTELLKKF 130 140 150 160 170 180 KQAKSKVVFS AENYIYPDRK LEAKYPPVRD GKRFLGSGGF IGYAPNLKKL VEEWKGKDDD 190 200 210 220 230 240 SDQLFYTKIF LDPEKRENIN ISLDHRSRIF QNLNGALDEV VLKFENARVR ARNLLYDTLP 250 260 270 280 290 300 VIIHGNGPTK LQLNYLGNYI PQIWTFETGC TVCDEGLRSL TGIKDEALPM ILIGIFIEQP 310 320 330 340 350 360 TPFLSQFFLR LRNLHYPKQR IQIFIHNHEE HHSMQVDSFV KEHSKEYLAM KVIGPDDEVE 370 380 390 400 410 420 NAEARNLGMD LCRKDPDCDY YFSLDAEVVL KNTETLRILI EQNKSVIAPL VSRHEKLWSN 430 440 450 460 470 480 FWGALSPDGY YARSEDYVDI VQRRRVGLWN VPYISSVYMV KGKVLRSELD EGDLFHGGKL 490 500 510 520 530 540 DADMAFCHNV RNQGVFMYLT NRHQFGHILS LENYQTTHLH NDLWQIFSNP EDWREKYIHE 550 560 570 580 590 600 NYTAALKGKL VEMPCPDVYW FPIFTDTACD ELVEEMEHYG KWSTGDNTDS RIQGGYENVP 610 620 630 640 650 660 TIDIHMNQIG FEREWYKFLL DYIAPITEKL YPGYYTKTQF ELAFVVRYKP DEQPSLMPHH 670 680 690 700 710 720 DASTFTINIA LNRVGIDYEG GGCRFLRYNC SIRAPRKGWT LMHPGRLTHY HEGLPTTKGT 730 RYIAVSFIDP

References

[1]

"Molecular cloning of chick lysyl hydroxylase. Little homology in primary structure to the two types of subunit of prolyl 4-hydroxylase." Kivirikko K.I., Turpeenniemi-Hujanen T., Pajunen L., Pihlajaniemi T., Myllylae R. J. Biol. Chem. 266:2805-2810(1991) [PubMed: 1704364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-40; 412-417; 508-515 AND 550-573.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M59183 mRNA. Translation: AAA48945.1.
IPI	IPI00574055.
PIR	A23742.
RefSeq	NP_001005618.1.
UniGene	Gga.4726
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSGALG00000004531. Gallus gallus. [Contig view]
GeneID	419485.
KEGG	gga:419485.
Phylogenomic databases
HOGENOM	P24802.
HOVERGEN	P24802.
Enzyme and pathway databases
BRENDA	1.14.11.4. 4.
Family and domain databases
InterPro	IPR005123. Oxoglutarate/Fe-dep_Oase. IPR006620. Pro_4_hyd_alph. IPR001006. Procol_lys_dOase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view]
ProDom	PD011578. ProcolLys_dioxy. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00702. P4Hc. 1 hit. [Graphical view]
PROSITE	PS01325. LYS_HYDROXYLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLOD1_CHICK

Accession

Primary (citable) accession number: P24802

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)