LYOX_PIG
ID LYOX_PIG Reviewed; 249 AA.
AC P45845; Q7M3F0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein-lysine 6-oxidase {ECO:0000250|UniProtKB:P28300};
DE EC=1.4.3.13 {ECO:0000250|UniProtKB:P28300};
DE AltName: Full=Lysyl oxidase;
DE Contains:
DE RecName: Full=Protein-lysine 6-oxidase, long form {ECO:0000250|UniProtKB:P28300};
DE Contains:
DE RecName: Full=Protein-lysine 6-oxidase, short form {ECO:0000250|UniProtKB:P28300};
GN Name=LOX {ECO:0000250|UniProtKB:P28300};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RA Cronshaw A.D., Hulmes D.J.S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE OF 1-19; 23-44; 49-121 AND 131-184, AND MASS SPECTROMETRY.
RC TISSUE=Skin;
RX PubMed=7864821; DOI=10.1042/bj3060279;
RA Cronshaw A.D., Fothergill-Gilmore L.A., Hulmes D.J.S.;
RT "The proteolytic processing site of the precursor of lysyl oxidase.";
RL Biochem. J. 306:279-284(1995).
RN [3]
RP PROTEIN SEQUENCE OF 131-166.
RC TISSUE=Skin;
RX PubMed=8100985; DOI=10.1016/s0934-8832(11)80009-0;
RA Cronshaw A.D., Macbeath J.R.E., Shackleton D.R., Collins J.F.,
RA Fothergill-Gilmore L.A., Hulmes D.J.S.;
RT "TRAMP (tyrosine rich acidic matrix protein), a protein that co-purifies
RT with lysyl oxidase from porcine skin. Identification of TRAMP as the
RT dermatan sulphate proteoglycan-associated 22K extracellular matrix
RT protein.";
RL Matrix 13:255-266(1993).
CC -!- FUNCTION: Responsible for the post-translational oxidative deamination
CC of peptidyl lysine residues in precursors to fibrous collagen and
CC elastin. Regulator of Ras expression. May play a role in tumor
CC suppression. Plays a role in the aortic wall architecture (By
CC similarity). {ECO:0000250|UniProtKB:P28301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-
CC [protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131803; EC=1.4.3.13;
CC Evidence={ECO:0000250|UniProtKB:P28301};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P16636};
CC -!- COFACTOR:
CC Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489;
CC Evidence={ECO:0000250|UniProtKB:P33072};
CC Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072};
CC -!- SUBUNIT: Interacts with MFAP4. Interacts (via propeptide) with EFEMP2;
CC this interaction is strong and facilitates formation of ternary
CC complexes with ELN during elastic fiber assembly; this interaction
CC limits interaction of EFEMP2 with FBLN5.
CC {ECO:0000250|UniProtKB:P28300}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28301}.
CC Secreted, extracellular space.
CC -!- PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by
CC condensation of the epsilon-amino group of a lysine with a topaquinone
CC produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:P33072}.
CC -!- PTM: Proteolytically cleaved by BMP1 which removes the propeptide (By
CC similarity). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but
CC not by ADAMTS3, at an additional cleavage site downstream of the BMP1
CC cleavage site (By similarity). The propeptide plays a role in directing
CC the deposition of this enzyme to elastic fibers, via interaction with
CC tropoelastin (By similarity). Cleavage by BMP1 to remove the propeptide
CC does not increase enzymatic activity but increases binding to collagen
CC (By similarity). Cleavage by ADAMTS2 produces a form with reduced
CC collagen-binding activity (By similarity).
CC {ECO:0000250|UniProtKB:P28300, ECO:0000250|UniProtKB:P28301}.
CC -!- PTM: Sulfated at Tyr-19 and also at either Tyr-15 or Tyr-16 which
CC enhances binding to collagen. {ECO:0000250|UniProtKB:P28300}.
CC -!- MASS SPECTROMETRY: [Protein-lysine 6-oxidase, long form]: Mass=29377;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:7864821};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR PIR; S54337; S54337.
DR STRING; 9823.ENSSSCP00000015138; -.
DR BindingDB; P45845; -.
DR ChEMBL; CHEMBL3112375; -.
DR PaxDb; P45845; -.
DR PeptideAtlas; P45845; -.
DR PRIDE; P45845; -.
DR eggNOG; ENOG502QWQR; Eukaryota.
DR InParanoid; P45845; -.
DR BRENDA; 1.4.3.13; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; ISS:UniProtKB.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; LTQ; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Sulfation; TPQ.
FT CHAIN 1..249
FT /note="Protein-lysine 6-oxidase, long form"
FT /evidence="ECO:0000250|UniProtKB:P16636"
FT /id="PRO_0000156409"
FT CHAIN 51..249
FT /note="Protein-lysine 6-oxidase, short form"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT /id="PRO_0000447887"
FT REGION 45..249
FT /note="Lysyl-oxidase like"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 128
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT SITE 50..51
FT /note="Cleavage; by ADAMTS2 and ADAMTS14"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT MOD_RES 19
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT MOD_RES 187
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 70..76
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 123..172
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 156..162
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 183..193
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 230..244
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CROSSLNK 152..187
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CONFLICT 121
FT /note="H -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 29073 MW; C2E71087CD799111 CRC64;
DDPYNPYKYS DDNPYYNYYX XXERPRPGSR YRPGYGTGYF QYGLPDLVPD PYYIQASTYV
QKMSMYNLRC AAEENCLAST AYRADVRDYD HRVLLRFPQR VKNQGTSDFL PSRPRYSWEW
HSCHQHYHSM DEFSHYDLLD ASTQRRVAEG HKASFCLEDT SCDYGYHRRF ACTAHTQGLS
PGCYDTYNAD IDCQWIDITD VKPGNYILKV SVNPSYLVPE SDYSNNVVRC EIRYTGHHAY
ASGCTISPY
