[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0888-7543(91)90057-L; PubMed=1685472 [NCBI, ExPASy, EBI, Israel, Japan] Haemaelaeinen E.-R., Jones T.A., Sheer D., Taskinen K., Pihlajaniemi T., Kivirikko K.I.; "Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2."; Genomics 11:508-516(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skin; PubMed=1357535 [NCBI, ExPASy, EBI, Israel, Japan] Mariani T.J., Trackman P.C., Kagan H.M., Eddy R.L., Shows T.B., Boyd C.D., Deak S.B.; "The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene)."; Matrix 12:242-248(1992).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. DOI=10.1074/jbc.270.13.7176; PubMed=7706256 [NCBI, ExPASy, EBI, Israel, Japan] Kim Y., Boyd C.D., Csiszar K.; "A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase."; J. Biol. Chem. 270:7176-7182(1995).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1023/A:1006913122261; PubMed=10391127 [NCBI, ExPASy, EBI, Israel, Japan] Contente S., Kenyon K., Sriraman P., Subramanyan S., Friedman R.M.; "Epigenetic inhibition of lysyl oxidase transcription after transformation by ras oncogene."; Mol. Cell. Biochem. 194:79-91(1999).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; 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).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213. DOI=10.1006/geno.1993.1369; PubMed=7902322 [NCBI, ExPASy, EBI, Israel, Japan] Haemaelaeinen E.-R., Kemppainen R., Pihlajaniemi T., Kivirikko K.I.; "Structure of the human lysyl oxidase gene."; Genomics 17:544-548(1993).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-216. TISSUE=Blood; PubMed=1352776 [NCBI, ExPASy, EBI, Israel, Japan] Svinarich D.M., Twomey T.A., Macauley S.P., Krebs C.J., Yang T.P., Krawetz S.A.; "Characterization of the human lysyl oxidase gene locus."; J. Biol. Chem. 267:14382-14387(1992).
[8]	DISEASE. PubMed=9111998 [NCBI, ExPASy, EBI, Israel, Japan] Khakoo A., Thomas R., Trompeter R., Duffy P., Price R., Pope F.M.; "Congenital cutis laxa and lysyl oxidase deficiency."; Clin. Genet. 51:109-114(1997).
[9]	VARIANT GLN-158. DOI=10.1006/geno.1993.1203; PubMed=8100215 [NCBI, ExPASy, EBI, Israel, Japan] Csiszar K., Mariani T.J., Gosin J.S., Deak S.B., Boyd C.D.; "A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene."; Genomics 16:401-406(1993).

Comments

FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression.
CATALYTIC ACTIVITY: Peptidyl-L-lysyl-peptide + O₂ + H₂O = peptidyl-allysyl-peptide + NH₃ + H₂O₂.
COFACTOR: Copper.
COFACTOR: Contains 1 lysine tyrosylquinone (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Heart, placenta, skeletal muscle, kidney, lung and pancreas.
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.
DISEASE: Defects in LOX may be a cause of autosomal recessive cutis laxa type I (CL type I) [MIM:219100].
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

S78694; AAB21243.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M94054; AAA59525.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S45875; AAB23549.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039291; AAD02130.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074820; AAH74820.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074872; AAH74872.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089436; AAH89436.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L16895; AAA16870.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M84150; AAA59541.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A47529; OXHUL.

NP_002308.2; -.

3D structure databases

ModBase

P28300.

Organism-specific databases

HIX0031956; -.

HGNC:6664; LOX.

LOX.

153455; gene. [NCBI / EBI]
219100; phenotype. [NCBI / EBI]

209; Cutis laxa.

PA30427; -.

Gene expression databases

ArrayExpress

P28300; -.

CleanEx

HS_LOX; -.

GermOnline

ENSG00000113083; Homo sapiens.

Ontologies

GO:0005507;	Molecular function: copper ion binding (traceable author statement from ProtInc).
GO:0004720;	Molecular function: protein-lysine 6-oxidase activity (traceable author statement from ProtInc).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006464;	Biological process: protein modification process (traceable author statement from ProtInc).
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.

Proteomic databases

P28300; -.

Genome annotation databases

Ensembl

ENSG00000113083; Homo sapiens. [Contig view]

GeneID

4015; -.

KEGG

hsa:4015; -.

Phylogenomic databases

HOGENOM

P28300; -.

HOVERGEN

P28300; -.

Other

NextBio

15752; -.

SOURCE

LOX; Homo sapiens.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 168`	`147`	`By similarity.`	`PRO_0000018520`
`CHAIN`	`169 417`	`249`	`Protein-lysine 6-oxidase.`	`PRO_0000018521`
`REGION`	`213 417`	`205`	`Lysyl-oxidase like.`
`METAL`	`292 292`		`Copper (Potential).`
`METAL`	`294 294`		`Copper (Potential).`
`METAL`	`296 296`		`Copper (Potential).`
`MOD_RES`	`355 355`		`2',4',5'-topaquinone (By similarity).`
`CARBOHYD`	`81 81`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`97 97`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`144 144`		`N-linked (GlcNAc...) (Potential).`
`CROSSLNK`	`320 355`		`Lysine tyrosylquinone (Lys-Tyr) (By similarity).`
`VARIANT`	`158 158`	`1`	`R -> Q (in dbSNP:rs1800449 [NCBI]).`	`VAR_004282`
`CONFLICT`	`30 30`		`Q -> H (in Ref. 3).`
`CONFLICT`	`31 31`		`P -> A (in Ref. 3).`
`CONFLICT`	`95 95`		`R -> A (in Ref. 3).`
`CONFLICT`	`102 102`		`A -> G (in Ref. 1; AAB21243).`
`CONFLICT`	`137 137`		`A -> R (in Ref. 2; AAA59525/AAB23549).`
`CONFLICT`	`139 139`		`A -> P (in Ref. 1; AAB21243).`
`CONFLICT`	`304 305`		`YD -> LY (in Ref. 1; AAB21243).`
`CONFLICT`	`315 315`		`V -> W (in Ref. 1; AAB21243).`

Sequence information

Length: 417 AA [This is the length of the unprocessed precursor]

Molecular weight: 46944 Da [This is the MW of the unprocessed precursor]

CRC64: 6412A78443E03F04 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRFAWTVLLL GPLQLCALVH CAPPAAGQQQ PPREPPAAPG AWRQQIQWEN NGQVFSLLSL 

        70         80         90        100        110        120 
GSQYQPQRRR DPGAAVPGAA NASAQQPRTP ILLIRDNRTA AARTRTAGSS GVTAGRPRPT 

       130        140        150        160        170        180 
ARHWFQAGYS TSRAREAGAS RAENQTAPGE VPALSNLRPP SRVDGMVGDD PYNPYKYSDD 

       190        200        210        220        230        240 
NPYYNYYDTY ERPRPGGRYR PGYGTGYFQY GLPDLVADPY YIQASTYVQK MSMYNLRCAA 

       250        260        270        280        290        300 
EENCLASTAY RADVRDYDHR VLLRFPQRVK NQGTSDFLPS RPRYSWEWHS CHQHYHSMDE 

       310        320        330        340        350        360 
FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC TAHTQGLSPG CYDTYGADID 

       370        380        390        400        410 
CQWIDITDVK PGNYILKVSV NPSYLVPESD YTNNVVRCDI RYTGHHAYAS GCTISPY

P28300 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