PLOD2_RAT
ID PLOD2_RAT Reviewed; 737 AA.
AC Q811A3; Q811A4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Mercer D.K., Nicol P.F., Wright M.C., Robins S.P.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Short;
CC IsoId=Q811A3-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q811A3-2; Sequence=VSP_013468;
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DR EMBL; AJ430860; CAD23629.1; -; mRNA.
DR EMBL; AJ430861; CAD23630.1; -; mRNA.
DR AlphaFoldDB; Q811A3; -.
DR SMR; Q811A3; -.
DR STRING; 10116.ENSRNOP00000053546; -.
DR CarbonylDB; Q811A3; -.
DR GlyGen; Q811A3; 6 sites.
DR PhosphoSitePlus; Q811A3; -.
DR jPOST; Q811A3; -.
DR PaxDb; Q811A3; -.
DR UCSC; RGD:3353; rat. [Q811A3-1]
DR RGD; 3353; Plod2.
DR eggNOG; KOG1971; Eukaryota.
DR InParanoid; Q811A3; -.
DR BRENDA; 1.14.11.4; 5301.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR PRO; PR:Q811A3; -.
DR Proteomes; UP000002494; Unplaced.
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:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0046947; P:hydroxylysine biosynthetic process; ISO:RGD.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Dioxygenase; Endoplasmic reticulum; Glycoprotein;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Signal; 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_0000024685"
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:0000250|UniProtKB:Q9R0B9"
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 VAR_SEQ 500
FT /note="M -> MTLQREKDSPTPETFQMLSPPK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_013468"
SQ SEQUENCE 737 AA; 84542 MW; FB49A6C360E25D9D CRC64;
MGDRGVRLGL LMPMLALLSW AASLGVAEET PSRIPADKLL VITVATKEND GFHRFMNSAK
YFNYTVKVLG QGQEWRGGDG MNSIGGGQKV RLMKEAMEHY AGQDDLVILF TECFDVIFAG
GPEELLKKFQ KTNHKIVFAA DALLWPDKRL ADKYPGVHIG KRYLNSGGFI GYAPYISRLV
QQWNLQDNDD DQLFYTKVYI DPLKREALNI TLDHRCKIFQ ALNGATDEVV LKFENGKSRV
KNTFYETLPV AINGNGPSKI LLNYFGNYVP NSWTQENGCA LCDFDASDLS TVDVYPKVTL
GVFIEQPTPF QPRFLDLLLT LDYPKEALRL FVHNKEVYHE KDIKAFVDKA KHDISSIKIV
GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR
HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGIWNVPY MANVYLIQGK TLRSEMSERN
YFVRDKLDPD MSLCRNARDM GVFMYISNRH EFGRLISTAN YNTSHLNNDL WQIFENPVDW
KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSERACDELV EEMEHYGKWS GGKHHDSRIS
GGYENVPTDD IHMKQIDLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ
RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG
LPVKNGTRYI AVSFIDP
