LYOX_CHICK
ID LYOX_CHICK Reviewed; 420 AA.
AC Q05063;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein-lysine 6-oxidase;
DE EC=1.4.3.13 {ECO:0000269|PubMed:1360009};
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};
DE Flags: Precursor;
GN Name=LOX;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC TISSUE=Embryo;
RX PubMed=1360009; DOI=10.1016/s0021-9258(18)35750-8;
RA Wu Y., Rich C.B., Lincecum J., Trackman P.C., Kagan H.M., Foster J.A.;
RT "Characterization and developmental expression of chick aortic lysyl
RT oxidase.";
RL J. Biol. Chem. 267:24199-24206(1992).
CC -!- FUNCTION: Responsible for the post-translational oxidative deamination
CC of peptidyl lysine residues in precursors to fibrous collagen and
CC elastin.
CC -!- FUNCTION: In addition to cross linking of extracellular matrix
CC proteins, it may have a direct role in tumor suppression.
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:0000269|PubMed:1360009};
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DEVELOPMENTAL STAGE: Increases between day 8 and 16 of embryonic
CC development, during aortic embryogenesis, in direct proportion to total
CC protein synthesis.
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-190 and also at either Tyr-186 or Tyr-187 which
CC enhances binding to collagen. {ECO:0000250|UniProtKB:P28300}.
CC -!- SIMILARITY: Belongs to the lysyl oxidase family. {ECO:0000305}.
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DR EMBL; M97881; AAA48942.1; -; mRNA.
DR PIR; A45166; A45166.
DR RefSeq; NP_990812.2; NM_205481.2.
DR AlphaFoldDB; Q05063; -.
DR SMR; Q05063; -.
DR STRING; 9031.ENSGALP00000040869; -.
DR GeneID; 396474; -.
DR KEGG; gga:396474; -.
DR CTD; 4015; -.
DR VEuPathDB; HostDB:geneid_396474; -.
DR eggNOG; ENOG502QWQR; Eukaryota.
DR InParanoid; Q05063; -.
DR OrthoDB; 815466at2759; -.
DR PhylomeDB; Q05063; -.
DR PRO; PR:Q05063; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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:0030199; P:collagen fibril organization; IBA:GO_Central.
DR GO; GO:0018057; P:peptidyl-lysine oxidation; ISS:UniProtKB.
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; Disulfide bond; Glycoprotein; LTQ; Metal-binding; Oxidoreductase;
KW Reference proteome; Secreted; Signal; Sulfation; TPQ.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..171
FT /note="Removed by BMP1"
FT /evidence="ECO:0000250|UniProtKB:P16636"
FT /id="PRO_0000018526"
FT CHAIN 172..420
FT /note="Protein-lysine 6-oxidase, long form"
FT /evidence="ECO:0000250|UniProtKB:P16636"
FT /id="PRO_0000018527"
FT CHAIN 222..420
FT /note="Protein-lysine 6-oxidase, short form"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT /id="PRO_0000447889"
FT REGION 54..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..420
FT /note="Lysyl-oxidase like"
FT COMPBIAS 135..150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 297
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT BINDING 299
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255"
FT SITE 221..222
FT /note="Cleavage; by ADAMTS2 and ADAMTS14"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT MOD_RES 190
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28300"
FT MOD_RES 358
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 241..247
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 294..343
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 327..333
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 354..364
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT DISULFID 401..415
FT /evidence="ECO:0000250|UniProtKB:P33072"
FT CROSSLNK 323..358
FT /note="Lysine tyrosylquinone (Lys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P33072"
SQ SEQUENCE 420 AA; 48153 MW; E0CBE81DD625F5C2 CRC64;
MRCAPPGLLL AQLHACIFWS GLWPAGCQSP PAAWRQRIQW ENNGQVYSLL SQGAQYQPPR
RRQGAEPASS PVLLLRGNGS VPRAAAAAAA RPQPEPQPQA QPQPRPRSSR RQPLGRRHWF
QAGYRAPSGS ARPAPRRRPR GRRSRRRERA ERRRAAAPSG LRPGREDVMV GDDPYSPYKY
TDDNPYYNYY DTYERPRQGS RYRPGYGTGY FQYGLPDLVP DPYYIQASTY VQRMSMYNLR
CAAEENCLAS SAYRADVRDY DNRVLLRFPQ RVKNQGTSDF LPSRPRYSWE WHSCHQHYHS
MDEFSHYDLL DASSHRKVAE GHKASFCLED TSCDYGYYRR YACTAHTQGL SPGCYDTYNA
DIDCQWIDIT DVKPGNYILK VSVNPSYLVP ESDYSNNIVR CDIRYTGHHA YASGCTISPY
