[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1678898 [NCBI, ExPASy, EBI, Israel, Japan] Kenyon K., Contente S., Trackman P.C., Tang J., Kagan H.M., Friedman R.M.; "Lysyl oxidase and rrg messenger RNA."; Science 253:802-802(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=NIH Swiss; DOI=10.1006/geno.1993.1202; PubMed=8100214 [NCBI, ExPASy, EBI, Israel, Japan] Contente S., Csiszar K., Kenyon K., Friedman R.M.; "Structure of the mouse lysyl oxidase gene."; Genomics 16:395-400(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N-3; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	ROLE OF PROPEPTIDE. DOI=10.1074/jbc.M506832200; PubMed=16251195 [NCBI, ExPASy, EBI, Israel, Japan] Thomassin L., Werneck C.C., Broekelmann T.J., Gleyzal C., Hornstra I.K., Mecham R.P., Sommer P.; "The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers."; J. Biol. Chem. 280:42848-42855(2005).

Comments

FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin.
FUNCTION: Regulator of Ras expression. May play a role in tumor suppression.
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.
MISCELLANEOUS: The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin.
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

M65142; AAA19032.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M65143; AAA20185.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L04262; AAA99899.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L04263; AAA99899.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L04264; AAA99899.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018439; AAH18439.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A47005; OXMSL.

NP_034858.2; -.

3D structure databases

ModBase

P28301.

Protein-protein interaction databases

IntAct

P28301; -.

Organism-specific databases

MGI

MGI:96817; Lox.

Gene expression databases

ArrayExpress

P28301; -.

CleanEx

MM_LOX; -.

Ontologies

GO:0005581;	Cellular component: collagen (inferred from direct assay from MGI).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0004720;	Molecular function: protein-lysine 6-oxidase activity (inferred from direct assay from MGI).
GO:0001568;	Biological process: blood vessel development (inferred from mutant phenotype from MGI).
GO:0030199;	Biological process: collagen fibril organization (inferred from mutant phenotype from MGI).
GO:0048251;	Biological process: elastic fiber assembly (inferred from mutant phenotype from MGI).
GO:0030324;	Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0007169;	Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (non-traceable author statement from UniProtKB).
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

P28301.

Genome annotation databases

Ensembl

ENSMUSG00000024529; Mus musculus. [Contig view]

GeneID

16948; -.

KEGG

mmu:16948; -.

Phylogenomic databases

HOGENOM

P28301; -.

HOVERGEN

P28301; -.

Other

NextBio

290992; -.

SOURCE

Lox; Mus musculus.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 162`	`141`	`By similarity.`	`PRO_0000018522`
`CHAIN`	`163 411`	`249`	`Protein-lysine 6-oxidase.`	`PRO_0000018523`
`REGION`	`207 411`	`205`	`Lysyl-oxidase like.`
`METAL`	`286 286`		`Copper (Potential).`
`METAL`	`288 288`		`Copper (Potential).`
`METAL`	`290 290`		`Copper (Potential).`
`MOD_RES`	`349 349`		`2',4',5'-topaquinone (By similarity).`
`CARBOHYD`	`91 91`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`138 138`		`N-linked (GlcNAc...) (Potential).`
`CROSSLNK`	`314 349`		`Lysine tyrosylquinone (Lys-Tyr) (By similarity).`
`CONFLICT`	`333 333`		`A -> G (in Ref. 2; AAA99899).`

Sequence information

Length: 411 AA [This is the length of the unprocessed precursor]

Molecular weight: 46701 Da [This is the MW of the unprocessed precursor]

CRC64: DBC0563A9C0AEB52 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRFAWAVLLL GPLQLCPLLR CAPQTPREPP AAPGAWRQTI QWENNGQVFS LLSLGAQYQP 

        70         80         90        100        110        120 
QRRRDPSATA RRPDGDAASQ PRTPILLLRD NRTASTRART PSPSGVAAGR PRPAARHWFQ 

       130        140        150        160        170        180 
AGFSPSGARD GASRRAANRT ASPQPPQLSN LRPPSHIDRM VGDDPYNPYK YSDDNPYYNY 

       190        200        210        220        230        240 
YDTYERPRPG SRNRPGYGTG YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA 

       250        260        270        280        290        300 
SSAYRADVRD YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL 

       310        320        330        340        350        360 
LDANTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA ADIDCQWIDI 

       370        380        390        400        410 
TDVQPGNYIL KVSVNPSYLV PESDYTNNVV RCDIRYTGHH AYASGCTISP Y

P28301 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