ID A0A452RMR1_URSAM Unreviewed; 732 AA.
AC A0A452RMR1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=procollagen-lysine 5-dioxygenase {ECO:0000256|ARBA:ARBA00012264};
DE EC=1.14.11.4 {ECO:0000256|ARBA:ARBA00012264};
GN Name=PLOD3 {ECO:0000313|Ensembl:ENSUAMP00000020444.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000020444.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000020444.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024166};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004367}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004367}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004367}.
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DR AlphaFoldDB; A0A452RMR1; -.
DR Ensembl; ENSUAMT00000022850.1; ENSUAMP00000020444.1; ENSUAMG00000013690.1.
DR GeneTree; ENSGT01030000234558; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005789; C: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; IEA:UniProtKB-EC.
DR CDD; cd23002; GT_LH3; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 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 PANTHER; PTHR10730:SF7; MULTIFUNCTIONAL PROCOLLAGEN LYSINE HYDROXYLASE AND GLYCOSYLTRANSFERASE LH3; 1.
DR PANTHER; PTHR10730; PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-DIOXYGENASE/GLYCOSYLTRANSFERASE 25 FAMILY MEMBER; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..732
FT /note="procollagen-lysine 5-dioxygenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019503511"
FT DOMAIN 641..732
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 732 AA; 83524 MW; 116ECDA22A666705 CRC64;
MASSGPGLRL LLGLLMLLPP APATSASDRP RGSDPVNPEK LLVITVATAE TEGYRRFLRS
AEFFNYTVRT LGLGEEWRGG DVARTVGGGQ KVRWLKKEME KYADREDMVI MFVDSYDVIL
AGSPSELLKK FVQSGSHLLF SAEGFCWPEW GLAEQYPEVG TGKRFLNSGG FIGFAPTVHQ
VVRQWKYKDD DDDQLFYTRL YLDPGLREKL SLSLDHKSRI FQNLNGALDE VVLKFDRNRV
RIRNVAYDTL PVVVHGNGPT KLQLNYLGNY VPNGWTPQGG CGFCGQDRRT LPGGQTPSYT
FLLTTVPLLS LGHYLFSPLY PRLSAPHLQE VYHEPHVADS WPQLQDHFSA VKLVGPEEAL
TPGEARDMAM DTCRQDPECE FYFSLDADAV ITNQQTLRIL IEENRKVIAP MLSRHGKLWS
NFWGALSPDE YYARSEDYVE LVQRKRVGVW NVPYISQAYV IRGETLRTEL PQREVFSGSD
TDPDMAFCKS LRDKGIFLHL SNQHEFGRLL ATSRYDTDHL HPDLWQIFDN PLDWKEQYIH
ENYSRALEGE GLVEQPCPDV YWFPLLSDQM CDELVEEMEL YGQWSGGRHE DSRLAGGYEN
VPTVDIHMKQ VGYEDQWLQL LRTYVGPMTE SLFPGYHTKT RAVMNFVVRY RPDEQPSLRP
HHDSSTFTLN VALNHKGLDY EGGGCRFLRY DCIVSSPRKG WGLLHPGRLT HYHEGLPTTR
GTRYIMVSFV DP
//
