[1]	PROTEIN SEQUENCE. Cronshaw A.D., Hulmes D.J.S.; Submitted (MAR-2007) to UniProtKB.
[2]	PROTEIN SEQUENCE OF 1-19; 23-44; 49-121 AND 131-184, AND MASS SPECTROMETRY. TISSUE=Skin; PubMed=7864821 [NCBI, ExPASy, EBI, Israel, Japan] Cronshaw A.D., Fothergill-Gilmore L.A., Hulmes D.J.S.; "The proteolytic processing site of the precursor of lysyl oxidase."; Biochem. J. 306:279-284(1995).
[3]	PROTEIN SEQUENCE OF 131-166, AND SULFATION. TISSUE=Skin; PubMed=8100985 [NCBI, ExPASy, EBI, Israel, Japan] Cronshaw A.D., Macbeath J.R.E., Shackleton D.R., Collins J.F., Fothergill-Gilmore L.A., Hulmes D.J.S.; "TRAMP (tyrosine rich acidic matrix protein), a protein that co-purifies with lysyl oxidase from porcine skin. Identification of TRAMP as the dermatan sulphate proteoglycan-associated 22K extracellular matrix protein."; Matrix 13:255-266(1993).

Comments

FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin.
CATALYTIC ACTIVITY: Peptidyl-L-lysyl-peptide + O₂ + H₂O = peptidyl-allysyl-peptide + NH₃ + H₂O₂.
COFACTOR: Copper (By similarity).
COFACTOR: Contains 1 lysine tyrosylquinone (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space.
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
PTM: Probably contains sulfotyrosine.
MASS SPECTROMETRY: Mass=29377; Method=MALDI; Range=1-249; Source=PubMed:7864821;.
SIMILARITY: Belongs to the lysyl oxidase family.

Copyright

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Cross-references

Sequence databases
PIR	S54337; S54337.
3D structure databases
ModBase	P45845.
Family and domain databases
InterPro	IPR001695; Lysyl_oxidase. Graphical view of domain structure.
Pfam	PF01186; Lysyl_oxidase; 1. Pfam graphical view of domain structure.
PROSITE	PS00926; LYSYL_OXIDASE; 1.
BLOCKS	P45845.
Phylogenomic databases
HOVERGEN	P45845; -.
Other
ProtoNet	P45845.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Copper; Direct protein sequencing; LTQ; Metal-binding; Oxidoreductase; Secreted; Sulfation; TPQ.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 249`	`249`	`Protein-lysine 6-oxidase.`	`PRO_0000156409`
`REGION`	`45 249`	`205`	`Lysyl-oxidase like (By similarity).`
`METAL`	`124 124`		`Copper (Potential).`
`METAL`	`126 126`		`Copper (Potential).`
`METAL`	`128 128`		`Copper (Potential).`
`MOD_RES`	`187 187`		`2',4',5'-topaquinone (By similarity).`
`CROSSLNK`	`152 187`		`Lysine tyrosylquinone (Lys-Tyr) (By similarity).`
`CONFLICT`	`121 121`		`H -> S (in Ref. 2; AA sequence).`
`CONFLICT`	`157 157`		`L -> K (in Ref. 2; AA sequence).`

Sequence information

Length: 249 AA [This is the length of the unprocessed precursor]

Molecular weight: 29073 Da [This is the MW of the unprocessed precursor]

CRC64: C2E71087CD799111 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DDPYNPYKYS DDNPYYNYYX XXERPRPGSR YRPGYGTGYF QYGLPDLVPD PYYIQASTYV 

        70         80         90        100        110        120 
QKMSMYNLRC AAEENCLAST AYRADVRDYD HRVLLRFPQR VKNQGTSDFL PSRPRYSWEW 

       130        140        150        160        170        180 
HSCHQHYHSM DEFSHYDLLD ASTQRRVAEG HKASFCLEDT SCDYGYHRRF ACTAHTQGLS 

       190        200        210        220        230        240 
PGCYDTYNAD IDCQWIDITD VKPGNYILKV SVNPSYLVPE SDYSNNVVRC EIRYTGHHAY 


ASGCTISPY

P45845 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools