PLOD1_BOVIN
ID PLOD1_BOVIN Reviewed; 726 AA.
AC O77588; Q1JPK0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Knight M.A., Drinkwater R.D.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P24802, ECO:0000250|UniProtKB:Q9R0E2}.
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 (By similarity). {ECO:0000250|UniProtKB:P24802,
CC ECO:0000250|UniProtKB:Q9R0E2}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral
CC membrane protein; Lumenal side.
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DR EMBL; AF054274; AAC25107.1; -; mRNA.
DR EMBL; BT025353; ABF57309.1; -; mRNA.
DR RefSeq; NP_776573.1; NM_174148.1.
DR AlphaFoldDB; O77588; -.
DR SMR; O77588; -.
DR IntAct; O77588; 1.
DR STRING; 9913.ENSBTAP00000002658; -.
DR PeptideAtlas; O77588; -.
DR PRIDE; O77588; -.
DR GeneID; 281409; -.
DR KEGG; bta:281409; -.
DR CTD; 5351; -.
DR eggNOG; KOG1971; Eukaryota.
DR InParanoid; O77588; -.
DR OrthoDB; 194164at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISS:UniProtKB.
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 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..726
FT /note="Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1"
FT /id="PRO_0000024677"
FT DOMAIN 635..726
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT ACT_SITE 717
FT /evidence="ECO:0000255"
FT BINDING 655
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 657
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 707
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 140
FT /note="K -> N (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> I (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="LD -> FH (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="R -> L (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="L -> F (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="A -> T (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="F -> Y (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="A -> G (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="L -> V (in Ref. 1; AAC25107)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 83487 MW; D215F7E093CCADE9 CRC64;
MRLLLLLAPL GWLLLAETKG DAKPEDNLLV LTVATKETEG FRRFKRSAQF FNYKIQALGL
GEDWPGEAML AGGGLKVRLL KKALEKHADK ENLVILFTDS YDVVFASGPR ELLKKFRQAR
SQVVFSAEEL IYPDRRLEAK YPVVSDGKRF LGSGGFIGYA PNLSKLVAEW EGQDSDSDQL
FYTKIFLDPE KREQINITLD HRCRIFQNLD GALDEVVLKF EMGQVRARNL AYDTLPVLIH
GNGPTKLQLN YLGNYIPRFW TFETGCAVCD EGLRSLKGIG DEALPAVLVG VFIEQPTPFL
SLFFQRLLRL HYPQKRLRLF IHNHEQHHKA QVEQFLAEHG DEYQSVKLVG PEVRVANADA
RNMGADLCRQ DRGCTYYFSV DADVALTEPK TLRLLIEQNK NVIAPLMTRH GRLWSNFWGA
LSADGYYARS EDYVDIVQGR RVGVWNVPYI SNIYLIKGSA LRAELQETDL FHHSKLDPDM
AFCANIRQQD VFMFLTNRHS FGHLLSLDSY QTTHLHNDLW EVFSNPEDWK EKYIHENYTK
ALAGKMVEMP CPDVYWFPIF TETACDELVE EMEHYGQWSL GDNKDNRIQG GYENVPTIDI
HMNQINFERE WHKFLVEYIA PMTEKLYPGY YTRAQFDLAF VVRYKPDEQP SLVPHHDAST
FTINIALNRV GVDYEGGGCR FLRYNCSIRA PRKGWTLMHP GRLTHYHEGL PTTKGTRYIA
VSFVDP
