ID PLOD_CAEEL Reviewed; 730 AA. AC Q20679; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 71. DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase; DE EC=1.14.11.4; DE AltName: Full=Lysyl hydroxylase; DE Short=LH; DE AltName: Full=Lethal protein 268; DE Flags: Precursor; GN Name=let-268; ORFNames=F52H3.1; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP FUNCTION, AND MUTAGENESIS OF ASP-668 AND GLY-682. RC STRAIN=Bristol N2; RX MEDLINE=20525610; PubMed=11071784; DOI=10.1006/dbio.2000.9897; RA Norman K.R., Moerman D.G.; RT "The let-268 locus of Caenorhabditis elegans encodes a procollagen RT lysyl hydroxylase that is essential for type IV collagen secretion."; RL Dev. Biol. 227:690-705(2000). RN [3] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-689, AND MASS RP SPECTROMETRY. RX PubMed=12754521; DOI=10.1038/nbt829; RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., RA Kasai K., Takahashi N., Isobe T.; RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry RT to identify N-linked glycoproteins."; RL Nat. Biotechnol. 21:667-672(2003). RN [4] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-689, AND MASS RP SPECTROMETRY. RX PubMed=17761667; DOI=10.1074/mcp.M600392-MCP200; RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., RA Taoka M., Takahashi N., Isobe T.; RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis RT elegans and suggests an atypical translocation mechanism for integral RT membrane proteins."; RL Mol. Cell. Proteomics 6:2100-2109(2007). CC -!- FUNCTION: Forms hydroxylysine residues in collagen type IV. CC -!- CATALYTIC ACTIVITY: Procollagen L-lysine + 2-oxoglutarate + O(2) = CC procollagen 5-hydroxy-L-lysine + succinate + CO(2). CC -!- COFACTOR: Iron (By similarity). CC -!- COFACTOR: Ascorbate (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; CC Peripheral membrane protein; Lumenal side (By similarity). CC -!- SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z66512; CAA91321.1; -; Genomic_DNA. DR PIR; T22517; T22517. DR RefSeq; NP_496170.1; -. DR UniGene; Cel.14738; -. DR Ensembl; F52H3.1; Caenorhabditis elegans. DR GeneID; 174564; -. DR KEGG; cel:F52H3.1; -. DR WormBase; WBGene00002497; let-268. DR WormPep; F52H3.1; CE03397. DR OMA; Q20679; SAEFFNY. DR BRENDA; 1.14.11.4; 672. DR NextBio; 884580; -. DR ArrayExpress; Q20679; -. DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; IEA:EC. DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase. DR GO; GO:0002119; P:nematode larval development; IMP:WormBase. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR005123; Oxoglutarate/Fe-dep_Oase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR001006; Procol_lys_dOase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR ProDom; PD011578; ProcolLys_dioxy; 1. DR SMART; SM00702; P4Hc; 1. DR PROSITE; PS01325; LYS_HYDROXYLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Dioxygenase; Endoplasmic reticulum; Glycoprotein; KW Iron; Membrane; Metal-binding; Oxidoreductase; Signal; Vitamin C. FT SIGNAL 1 16 Potential. FT CHAIN 17 730 Procollagen-lysine,2-oxoglutarate 5- FT dioxygenase. FT /FTId=PRO_0000024689. FT DOMAIN 555 730 PKHD. 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 689 689 N-linked (GlcNAc...). FT MUTAGEN 668 668 D->R: In let-268(mn189); lethal effect. FT MUTAGEN 682 682 G->D: In let-268(mn198); lethal effect. SQ SEQUENCE 730 AA; 84425 MW; 884F3EFE1A0A86FF CRC64; MRVLPFLLPL IPVLLATTIT DLPELVVVTV ATENTDGLKR LLESAKAFDI NIEVLGLGEK WNGGDTRIEQ GGGQKIRILS DWIEKYKDAS DTMIMFVDAY DVVFNADSTT ILRKFFEHYS EKRLLFGAEP FCWPDQSLAP EYPIVEFGKR FLNSGLFMGY GPEMHKILKL KSVEDKDDDQ LYYTMIYLDE KLRKELNMDL DSMSKIFQNL NGVIEDVELQ FKEDGTPEAY NAAYNTKPLI VHGNGPSKSH LNYLGNYLGN RWNSQLGCRT CGLEVKESEE VPLIALNLFI SKPIPFIEEV LQKIAEFDYP KEKIALYIYN NQPFSIKNIQ DFLQKHGKSY YTKRVINGVT EIGDREARNE AIEWNKARNV EFAFLMDGDA YFSEPKVIKD LIQYSKTYDV GIIAPMIGQP GKLFTNFWGA IAANGYYARS EDYMAIVKGN RVGYWNVPFI TSAVLFNKEK LEAMKDAYSY NKNLDPDMSM CKFARDNGHF LYIDNEKYYG FLIVSDEYAE TVTEGKWHPE MWQIFENREL WEARYIHPGY HKIMEPEHVV DQACPDVYDF PLMSERFCEE LIEEMEGFGR WSDGSNNDKR LAGGYENVPT RDIHMNQVGF ERQWLYFMDT YVRPVQEKTF IGYYHQPVES NMMFVVRYKP EEQPSLRPHH DASTFSIDIA LNKKGRDYEG GGVRYIRYNC TVPADEVGYA MMFPGRLTHL HEGLATTKGT RYIMVSFINP //