Reviewed, UniProtKB/Swiss-Prot Q20679 (PLOD_CAEEL)

Names and origin

Protein names

Recommended name:
    Procollagen-lysine,2-oxoglutarate 5-dioxygenase
    EC=1.14.11.4
Alternative name(s):
    Lysyl hydroxylase
      Short name=LH
    Lethal protein 268

Gene names

Name:	let-268
ORF Names:	F52H3.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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 collagen type IV. Ref.2
Catalytic activity	Procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
Cofactor	Iron By similarity. Ascorbate By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.
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	Complete proteome
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase embryonic development ending in birth or egg hatching Ref.2 Inferred from mutant phenotype. Source: WormBase morphogenesis of an epithelium Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase 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 – 16	16	Potential
	Chain	17 – 730	714	Procollagen-lysine,2-oxoglutarate 5-dioxygenase		PRO_0000024689
Regions
	Domain	555 – 730	176	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	689	1	N-linked (GlcNAc...) Ref.3 Ref.4
Experimental info
	Mutagenesis	668	1	D → R in let-268(mn189); lethal effect. Ref.2
	Mutagenesis	682	1	G → D in let-268(mn198); lethal effect. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q20679-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 884F3EFE1A0A86FF	FASTA	730	84,425
	10 20 30 40 50 60 MRVLPFLLPL IPVLLATTIT DLPELVVVTV ATENTDGLKR LLESAKAFDI NIEVLGLGEK 70 80 90 100 110 120 WNGGDTRIEQ GGGQKIRILS DWIEKYKDAS DTMIMFVDAY DVVFNADSTT ILRKFFEHYS 130 140 150 160 170 180 EKRLLFGAEP FCWPDQSLAP EYPIVEFGKR FLNSGLFMGY GPEMHKILKL KSVEDKDDDQ 190 200 210 220 230 240 LYYTMIYLDE KLRKELNMDL DSMSKIFQNL NGVIEDVELQ FKEDGTPEAY NAAYNTKPLI 250 260 270 280 290 300 VHGNGPSKSH LNYLGNYLGN RWNSQLGCRT CGLEVKESEE VPLIALNLFI SKPIPFIEEV 310 320 330 340 350 360 LQKIAEFDYP KEKIALYIYN NQPFSIKNIQ DFLQKHGKSY YTKRVINGVT EIGDREARNE 370 380 390 400 410 420 AIEWNKARNV EFAFLMDGDA YFSEPKVIKD LIQYSKTYDV GIIAPMIGQP GKLFTNFWGA 430 440 450 460 470 480 IAANGYYARS EDYMAIVKGN RVGYWNVPFI TSAVLFNKEK LEAMKDAYSY NKNLDPDMSM 490 500 510 520 530 540 CKFARDNGHF LYIDNEKYYG FLIVSDEYAE TVTEGKWHPE MWQIFENREL WEARYIHPGY 550 560 570 580 590 600 HKIMEPEHVV DQACPDVYDF PLMSERFCEE LIEEMEGFGR WSDGSNNDKR LAGGYENVPT 610 620 630 640 650 660 RDIHMNQVGF ERQWLYFMDT YVRPVQEKTF IGYYHQPVES NMMFVVRYKP EEQPSLRPHH 670 680 690 700 710 720 DASTFSIDIA LNKKGRDYEG GGVRYIRYNC TVPADEVGYA MMFPGRLTHL HEGLATTKGT 730 RYIMVSFINP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion." Norman K.R., Moerman D.G. Dev. Biol. 227:690-705(2000) [PubMed: 11071784] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-668 AND GLY-682. Strain: Bristol N2.
[3]	"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-689, MASS SPECTROMETRY.
[4]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-689, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z66512 Genomic DNA. Translation: CAA91321.1.
PIR	T22517.
RefSeq	NP_496170.1.
UniGene	Cel.14738
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	F52H3.1. Caenorhabditis elegans. [Contig view]
GeneID	174564.
KEGG	cel:F52H3.1.
Organism-specific databases
WormBase	WBGene00002497. let-268.
WormPep	F52H3.1. CE03397. [WorfDB]
Phylogenomic databases
OMA	Q20679. SAEFFNY.
Enzyme and pathway databases
BRENDA	1.14.11.4. 672.
Gene expression databases
ArrayExpress	Q20679.
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...
Other Resources
NextBio	884580.

Entry information

Entry name

PLOD_CAEEL

Accession

Primary (citable) accession number: Q20679

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
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)

Annotation project

Caenorhabditis annotation project