[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skin; DOI=10.1074/jbc.M109499200; PubMed=11684696 [NCBI, ExPASy, EBI, Israel, Japan] Borel A., Eichenberger D., Farjanel J., Kessler E., Gleyzal C., Hulmes D.J.S., Sommer P., Font B.; "Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1."; J. Biol. Chem. 276:48944-48949(2001).
[2]	PROTEIN SEQUENCE OF 200-231; 266-284; 297-305; 316-323; 354-359; 379-398 AND 403-418. TISSUE=Aorta; DOI=10.1021/bi00472a016; PubMed=1973052 [NCBI, ExPASy, EBI, Israel, Japan] Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D., Troxler R.F., Kagan H.M.; "Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence."; Biochemistry 29:4863-4870(1990).
[3]	COFACTOR. PubMed=8688089 [NCBI, ExPASy, EBI, Israel, Japan] Wang S.X., Mure M., Medzihradszky K.F., Burlingame A.L., Brown D.E., Dooley D.M., Smith A.J., Kagan H.M., Klinman J.P.; "A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains."; Science 273:1078-1084(1996).

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.
COFACTOR: Contains 1 lysine tyrosylquinone.
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.
MISCELLANEOUS: The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (By similarity).
SIMILARITY: Belongs to the lysyl oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF421186; AAL13313.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B30352; B30352.

UniGene

Bt.98817

3D structure databases

ModBase

P33072.

Ontologies

GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0004720;	Molecular function: protein-lysine 6-oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001695; Lysyl_oxidase.
Graphical view of domain structure.

Pfam

PF01186; Lysyl_oxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00074; LYSYLOXIDASE.

PROSITE

PS00926; LYSYL_OXIDASE; 1.

ProtoNet

P33072.

Genome annotation databases

Ensembl

ENSBTAG00000012994; Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P33072; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 169`	`149`	`By similarity.`	`PRO_0000045436`
`CHAIN`	`170 418`	`249`	`Protein-lysine 6-oxidase.`	`PRO_0000045437`
`REGION`	`214 418`	`205`	`Lysyl-oxidase like.`
`METAL`	`293 293`		`Copper (Potential).`
`METAL`	`295 295`		`Copper (Potential).`
`METAL`	`297 297`		`Copper (Potential).`
`MOD_RES`	`356 356`		`2',4',5'-topaquinone.`
`CARBOHYD`	`80 80`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`96 96`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`143 143`		`N-linked (GlcNAc...) (Potential).`
`CROSSLNK`	`321 356`		`Lysine tyrosylquinone (Lys-Tyr).`
`CONFLICT`	`413 414`		`CT -> QS (in Ref. 2; AA sequence).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47115 Da [This is the MW of the unprocessed precursor]

CRC64: EC4C0F36A29FD860 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRFAWTALLG SLQLCALVRC APPAASHRQP PREQAAAPGA WRQKIQWENN GQVFSLLSLG 

        70         80         90        100        110        120 
SQYQPQRRRD PGATAPGAAN ATAPQMRTPI LLLRNNRTAA ARVRTAGPSA AAAGRPRPAA 

       130        140        150        160        170        180 
RHWFQAGYST SGAHDAGTSR ADNQTAPGEV PTLSNLRPPN RVEVDGMVGD DPYNPYKYTD 

       190        200        210        220        230        240 
DNPYYNYYDT YERPRPGSRY RPGYGTGYFQ YGLPDLVPDP YYIQASTYVQ KMAMYNLRCA 

       250        260        270        280        290        300 
AEENCLASSA YRXDVRDYDH RVLLRFPQRV KNQGTSDFLP SRPRYSWEWH SCHQHYHSMD 

       310        320        330        340        350        360 
EFSHYDLLDA STQRRVAEGH KASFCLEDTS CDYGYHRRFA CTAHTQGLSP GCYDTYNADI 

       370        380        390        400        410 
DCQWIDITDV KPGNYILKVS VNPSYLVPES DYSNNVVRCE IRYTGHHAYA SGCTISPY

P33072 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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