PLOD1_MOUSE
ID PLOD1_MOUSE Reviewed; 728 AA.
AC Q9R0E2;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1;
DE EC=1.14.11.4 {ECO:0000250|UniProtKB:P24802};
DE AltName: Full=Lysyl hydroxylase 1;
DE Short=LH1;
DE Flags: Precursor;
GN Name=Plod1; Synonyms=Plod;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10429951; DOI=10.1016/s0945-053x(99)00016-5;
RA Ruotsalainen H., Sipila L., Kerkela E., Pospiech H., Myllylae R.;
RT "Characterization of cDNAs for mouse lysyl hydroxylase 1, 2 and 3, their
RT phylogenetic analysis and tissue-specific expression in the mouse.";
RL Matrix Biol. 18:325-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH P3H3 AND P3H4.
RX PubMed=27119146; DOI=10.1371/journal.pgen.1006002;
RA Heard M.E., Besio R., Weis M., Rai J., Hudson D.M., Dimori M.,
RA Zimmerman S.M., Kamykowski J.A., Hogue W.R., Swain F.L., Burdine M.S.,
RA Mackintosh S.G., Tackett A.J., Suva L.J., Eyre D.R., Morello R.;
RT "Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex
RT Regulating Collagen Lysyl Hydroxylation.";
RL PLoS Genet. 12:E1006002-E1006002(2016).
CC -!- FUNCTION: Part of a complex composed of PLOD1, P3H3 and P3H4 that
CC catalyzes hydroxylation of lysine residues in collagen alpha chains and
CC is required for normal assembly and cross-linkling of collagen fibrils
CC (PubMed:27119146). Forms hydroxylysine residues in -Xaa-Lys-
CC Gly- sequences in collagens (By similarity). These hydroxylysines serve
CC as sites of attachment for carbohydrate units and are essential for the
CC stability of the intermolecular collagen cross-links (PubMed:27119146).
CC {ECO:0000250|UniProtKB:P24802, ECO:0000269|PubMed:27119146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-
CC lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-
CC COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:P24802};
CC -!- SUBUNIT: Homodimer (By similarity). Identified in a complex with P3H3
CC and P3H4 (PubMed:27119146). {ECO:0000250|UniProtKB:P24802,
CC ECO:0000269|PubMed:27119146}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral
CC membrane protein; Lumenal side.
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, heart, lung,
CC skeletal muscle and kidney. {ECO:0000269|PubMed:10429951}.
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DR EMBL; AF046782; AAD54617.1; -; mRNA.
DR EMBL; BC006599; AAH06599.1; -; mRNA.
DR CCDS; CCDS18924.1; -.
DR RefSeq; NP_035252.1; NM_011122.3.
DR AlphaFoldDB; Q9R0E2; -.
DR SMR; Q9R0E2; -.
DR BioGRID; 202253; 6.
DR STRING; 10090.ENSMUSP00000019199; -.
DR GlyConnect; 2607; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9R0E2; 3 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9R0E2; -.
DR PhosphoSitePlus; Q9R0E2; -.
DR jPOST; Q9R0E2; -.
DR MaxQB; Q9R0E2; -.
DR PaxDb; Q9R0E2; -.
DR PeptideAtlas; Q9R0E2; -.
DR PRIDE; Q9R0E2; -.
DR ProteomicsDB; 289448; -.
DR Antibodypedia; 28331; 144 antibodies from 25 providers.
DR DNASU; 18822; -.
DR Ensembl; ENSMUST00000019199; ENSMUSP00000019199; ENSMUSG00000019055.
DR GeneID; 18822; -.
DR KEGG; mmu:18822; -.
DR UCSC; uc008vtk.2; mouse.
DR CTD; 5351; -.
DR MGI; MGI:99907; Plod1.
DR VEuPathDB; HostDB:ENSMUSG00000019055; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_022320_1_0_1; -.
DR InParanoid; Q9R0E2; -.
DR OMA; CTYYFSM; -.
DR OrthoDB; 194164at2759; -.
DR PhylomeDB; Q9R0E2; -.
DR TreeFam; TF313826; -.
DR BRENDA; 1.14.11.4; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 18822; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Plod1; mouse.
DR PRO; PR:Q9R0E2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R0E2; protein.
DR Bgee; ENSMUSG00000019055; Expressed in stroma of bone marrow and 238 other tissues.
DR ExpressionAtlas; Q9R0E2; baseline and differential.
DR Genevisible; Q9R0E2; MM.
DR GO; GO:1902494; C:catalytic complex; IMP:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
DR GO; GO:0031418; F:L-ascorbic acid binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISO:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
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 Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal; Vitamin C.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..728
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1"
FT /id="PRO_0000024679"
FT DOMAIN 637..728
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 719
FT /evidence="ECO:0000255"
FT BINDING 657
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 659
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 709
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 83595 MW; 339C2D71976ED985 CRC64;
MRSLLLLAPL AWLLLVQAKD DAKLEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQSLGL
GEDWSVDGGP AAAGGGQKVR LLKKALEKHA DKEDLVILFV DSYDVVFASG PRELLKKFQQ
AKSQVVFSAE EHIYPDRRLE AKYPTVPDGK RFLGSGGFIG YAPSLSKLVA EWEGQDSDSD
QLFYTKIFLN PEKREQINIS LDHRCRIFQN LDGALDEVVL KFEMGHVRAR NLAYDTLPVV
VHGNGPTKLQ LNYLGNYIPR FWTFETGCTV CDEGLRSLKG IGDEALPTVL VGVFIEQPTP
FLSLFFLRLL RLRYPQKQMR LFIHNQERHH KLQVEQFLAE HGSEYQSVKL VGPEVRMANA
DARNMGADLC RQDQTCTYYF SVDADVALTE PNSLRLLIEQ NKNVIAPLMT RHGRLWSNFW
GGLSADGYYA RSEDYVDIVQ GRRVGVWNVP YISNIYLIKG SALRAELQNV DLFHYSKLDS
DMSFCANVRQ QEVFMFLTNR HTFGHLLSLD NYQTTHLHND LWEVFSNPED WKEKYIHENY
TKALAGKLVE TPCPDVYWFP IFTEAACDEL VEEMEHYGQW SLGDNKDNRI QGGYENVPTI
DIHMNQITFE REWHKFLVEY IAPMTEKLYP GYYTRAQFDL AFVVRYKPDE QPSLMPHHDA
STFTVNIALN RVGEDYEGGG CRFLRYNCSV RAPRKGWALL HPGRLTHYHE GLPTTKGTRY
IAVSFVDP
