PLOD2_MOUSE
ID PLOD2_MOUSE Reviewed; 737 AA.
AC Q9R0B9; E9QM54; Q8VDT4;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2;
DE EC=1.14.11.4 {ECO:0000250|UniProtKB:P24802};
DE AltName: Full=Lysyl hydroxylase 2;
DE Short=LH2;
DE Flags: Precursor;
GN Name=Plod2;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-704, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in
CC collagens. These hydroxylysines serve as sites of attachment for
CC carbohydrate units and are essential for the stability of the
CC intermolecular collagen cross-links. {ECO:0000250|UniProtKB:P24802}.
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. {ECO:0000250|UniProtKB:P24802}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral
CC membrane protein; Lumenal side.
CC -!- TISSUE SPECIFICITY: Is highly expressed in the heart, lung, kidney,
CC eye, ovary and placenta. {ECO:0000269|PubMed:10429951}.
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DR EMBL; AF080572; AAD53987.1; -; mRNA.
DR EMBL; AC165156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021352; AAH21352.1; -; mRNA.
DR CCDS; CCDS23408.1; -.
DR RefSeq; NP_001136388.1; NM_001142916.1.
DR RefSeq; NP_036091.2; NM_011961.3.
DR AlphaFoldDB; Q9R0B9; -.
DR SMR; Q9R0B9; -.
DR BioGRID; 204984; 11.
DR CORUM; Q9R0B9; -.
DR STRING; 10090.ENSMUSP00000125373; -.
DR GlyConnect; 2608; 1 N-Linked glycan (1 site).
DR GlyGen; Q9R0B9; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9R0B9; -.
DR PhosphoSitePlus; Q9R0B9; -.
DR EPD; Q9R0B9; -.
DR jPOST; Q9R0B9; -.
DR MaxQB; Q9R0B9; -.
DR PaxDb; Q9R0B9; -.
DR PeptideAtlas; Q9R0B9; -.
DR PRIDE; Q9R0B9; -.
DR ProteomicsDB; 288255; -.
DR Antibodypedia; 33520; 249 antibodies from 28 providers.
DR DNASU; 26432; -.
DR Ensembl; ENSMUST00000070522; ENSMUSP00000068611; ENSMUSG00000032374.
DR GeneID; 26432; -.
DR KEGG; mmu:26432; -.
DR UCSC; uc009rau.2; mouse.
DR CTD; 5352; -.
DR MGI; MGI:1347007; Plod2.
DR VEuPathDB; HostDB:ENSMUSG00000032374; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR InParanoid; Q9R0B9; -.
DR OMA; WDLQDND; -.
DR OrthoDB; 194164at2759; -.
DR BRENDA; 1.14.11.4; 3474.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR BioGRID-ORCS; 26432; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Plod2; mouse.
DR PRO; PR:Q9R0B9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9R0B9; protein.
DR Bgee; ENSMUSG00000032374; Expressed in molar tooth and 244 other tissues.
DR ExpressionAtlas; Q9R0B9; baseline and differential.
DR Genevisible; Q9R0B9; MM.
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:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0008475; F:procollagen-lysine 5-dioxygenase activity; ISO:MGI.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; ISO:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISO:MGI.
DR Gene3D; 3.90.550.10; -; 1.
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; Phosphoprotein; Reference proteome; Signal;
KW Vitamin C.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..737
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2"
FT /id="PRO_0000024684"
FT DOMAIN 644..737
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 728
FT /evidence="ECO:0000255"
FT BINDING 666
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 668
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 718
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00469"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O00469"
FT MOD_RES 704
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 2
FT /note="G -> E (in Ref. 1; AAD53987)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="F -> I (in Ref. 3; AAH21352)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="I -> T (in Ref. 1; AAD53987 and 3; AAH21352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 84488 MW; 0FF2880E5FEEA084 CRC64;
MGDRGARPGR LMPMLALLSW AAGLGVAEET PGRIPADKLL VITVATKEND GFHRFMNSAK
YFNYTVKVLG QGQEWRGGDG MNSIGGGQKV RLLKEAMEHY ASQEDLVILF TECFDVVFAG
GPEEVLKKFQ KTNHKIVFAA DGLLWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYISRLV
QQWNLQDNDD DQLFYTKVYI DPLKREAFNI TLDHKCKIFQ ALNGATDEVV LKFENGKSRV
KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQENGCA LCDVDTIDLS TVDVPPKVTL
GVFIEQPTPF LPRFLNLLLT LDYPKEALQL FIHNKEVYHE KDIKVFVDKA KHDISSIKIV
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKFLIEQN RKIIAPLVTR
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGIWNVPY MANVYLIQGK TLRSEMNERN
YFVRDKLDPD MALCRNARDM GVFMYISNRH EFGRLISTAN YNTSHLNNDF WQIFENPVDW
KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSERACDELV EEMEHYGKWS GGKHHDSRIS
GGYENVPTDD IHMKQIGLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ
RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG
LPVKNGTRYI AVSFIDP
