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   16-JUN-2009, entry version 59.
DE   RecName: Full=Protein-lysine 6-oxidase;
DE            EC=1.4.3.13;
DE   AltName: Full=Lysyl oxidase;
DE   Flags: Precursor;
GN   Name=LOX;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=93077497; PubMed=1360009;
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
CC       deamination of peptidyl lysine residues in precursors to fibrous
CC       collagen and 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: Peptidyl-L-lysyl-peptide + O(2) + H(2)O =
CC       peptidyl-allysyl-peptide + NH(3) + H(2)O(2).
CC   -!- COFACTOR: Copper (By similarity).
CC   -!- COFACTOR: Contains 1 lysine tyrosylquinone (By similarity).
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
CC       total 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
CC       topaquinone produced by oxidation of tyrosine.
CC   -!- MISCELLANEOUS: The propeptide plays a role in directing the
CC       deposition of this enzyme to elastic fibers, via interaction with
CC       tropoelastin (By similarity).
CC   -!- SIMILARITY: Belongs to the lysyl oxidase family.
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DR   EMBL; M97881; AAA48942.1; -; mRNA.
DR   IPI; IPI00579818; -.
DR   PIR; A45166; A45166.
DR   RefSeq; NP_990812.1; -.
DR   UniGene; Gga.4303; -.
DR   GeneID; 396474; -.
DR   KEGG; gga:396474; -.
DR   HOGENOM; Q05063; -.
DR   HOVERGEN; Q05063; -.
DR   BRENDA; 1.4.3.13; 4.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Copper; Glycoprotein; LTQ; Metal-binding; Oxidoreductase; Secreted;
KW   Signal; TPQ.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22    171       By similarity.
FT                                /FTId=PRO_0000018526.
FT   CHAIN       172    420       Protein-lysine 6-oxidase.
FT                                /FTId=PRO_0000018527.
FT   REGION      216    420       Lysyl-oxidase like.
FT   COMPBIAS     58    286       Arg/Pro-rich.
FT   METAL       295    295       Copper (Potential).
FT   METAL       297    297       Copper (Potential).
FT   METAL       299    299       Copper (Potential).
FT   MOD_RES     358    358       2',4',5'-topaquinone (By similarity).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    323    358       Lysine tyrosylquinone (Lys-Tyr) (By
FT                                similarity).
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
//