Protein-lysine 6-oxidase precursor - Homo sapiens (Human)

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Names and origin

Protein names

Recommended name:
    Protein-lysine 6-oxidase
    EC=1.4.3.13
Alternative name(s):
    Lysyl oxidase

Gene names

Name:

LOX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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. Contains 1 lysine tyrosylquinone By similarity.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Heart, placenta, skeletal muscle, kidney, lung and pancreas. Ref.3
Post-translational modification	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.
Involvement in disease	Defects in LOX may be a cause of autosomal recessive cutis laxa type I (CL type I) [MIM:219100]. Ref.9
Miscellaneous	The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin By similarity.
Sequence similarities	Belongs to the lysyl oxidase family.

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Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein LTQ TPQ
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein modification process Ref.1 Traceable author statement. Source: ProtInc transmembrane receptor protein tyrosine kinase signaling pathway Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Ref.2 Traceable author statement. Source: ProtInc protein-lysine 6-oxidase activity Ref.8 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 168

147

By similarity

PRO_0000018520

Chain

169 – 417

249

Protein-lysine 6-oxidase

PRO_0000018521

Regions

Region

213 – 417

205

Lysyl-oxidase like

Sites

Metal binding

292

1

Copper Potential

Metal binding

294

1

Copper Potential

Metal binding

296

1

Copper Potential

Amino acid modifications

Modified residue

355

1

2',4',5'-topaquinone By similarity

Glycosylation

81

1

N-linked (GlcNAc...) Potential

Glycosylation

97

1

N-linked (GlcNAc...) Potential

Glycosylation

144

1

N-linked (GlcNAc...) Potential

Cross-link

320 ↔ 355

Lysine tyrosylquinone (Lys-Tyr) By similarity

Natural variations

Natural variant

158

1

R → Q: dbSNP rs1800449. Ref.5 Ref.10

VAR_004282

Experimental info

Sequence conflict

30

1

Q → H Ref.3

Sequence conflict

31

1

P → A Ref.3

Sequence conflict

95

1

R → A Ref.3

Sequence conflict

102

1

A → G in AAB21243. Ref.1

Sequence conflict

137

1

A → R in AAA59525. Ref.2

Sequence conflict

137

1

A → R in AAB23549. Ref.2

Sequence conflict

139

1

A → P in AAB21243. Ref.1

Sequence conflict

304 – 305

2

YD → LY in AAB21243. Ref.1

Sequence conflict

315

1

V → W in AAB21243. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P28300-1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 6412A78443E03F04
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FASTA

417

46,944

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2." Haemaelaeinen E.-R., Jones T.A., Sheer D., Taskinen K., Pihlajaniemi T., Kivirikko K.I. Genomics 11:508-516(1991) [PubMed: 1685472] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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)." Mariani T.J., Trackman P.C., Kagan H.M., Eddy R.L., Shows T.B., Boyd C.D., Deak S.B. Matrix 12:242-248(1992) [PubMed: 1357535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skin.
[3]	"A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase." Kim Y., Boyd C.D., Csiszar K. J. Biol. Chem. 270:7176-7182(1995) [PubMed: 7706256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]	"Epigenetic inhibition of lysyl oxidase transcription after transformation by ras oncogene." Contente S., Kenyon K., Sriraman P., Subramanyan S., Friedman R.M. Mol. Cell. Biochem. 194:79-91(1999) [PubMed: 10391127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-158.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"Structure of the human lysyl oxidase gene." Haemaelaeinen E.-R., Kemppainen R., Pihlajaniemi T., Kivirikko K.I. Genomics 17:544-548(1993) [PubMed: 7902322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213.
[8]	"Characterization of the human lysyl oxidase gene locus." Svinarich D.M., Twomey T.A., Macauley S.P., Krebs C.J., Yang T.P., Krawetz S.A. J. Biol. Chem. 267:14382-14387(1992) [PubMed: 1352776] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-216. Tissue: Blood.
[9]	"Congenital cutis laxa and lysyl oxidase deficiency." Khakoo A., Thomas R., Trompeter R., Duffy P., Price R., Pope F.M. Clin. Genet. 51:109-114(1997) [PubMed: 9111998] [Abstract] Cited for: DISEASE.
[10]	"A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene." Csiszar K., Mariani T.J., Gosin J.S., Deak S.B., Boyd C.D. Genomics 16:401-406(1993) [PubMed: 8100215] [Abstract] Cited for: VARIANT GLN-158.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases
	S78694 mRNA. Translation: AAB21243.1. M94054 mRNA. Translation: AAA59525.1. S45875 mRNA. Translation: AAB23549.1. AF039291 mRNA. Translation: AAD02130.1. AK312269 mRNA. Translation: BAG35200.1. BC074820 mRNA. Translation: AAH74820.1. BC074872 mRNA. Translation: AAH74872.1. BC089436 mRNA. Translation: AAH89436.1. L16895 Unassigned DNA. Translation: AAA16870.1. M84150 Genomic DNA. Translation: AAA59541.1.
IPI	IPI00002802.
PIR	OXHUL. A47529.
RefSeq	NP_002308.2.
UniGene	Hs.102267
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	P28300.
PRIDE	P28300.
Genome annotation databases
Ensembl	ENSG00000113083. Homo sapiens. [Contig view]
GeneID	4015.
KEGG	hsa:4015.
UCSC	uc003ksu.1. human.
Organism-specific databases
GeneCards	GC05M121429.
H-InvDB	HIX0031956.
HGNC	HGNC:6664. LOX.
MIM	153455. gene. 219100. phenotype.
Orphanet	209. Cutis laxa.
PharmGKB	PA30427.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P28300.
HOVERGEN	P28300.
OMA	P28300. ENNGQVF.
Enzyme and pathway databases
BRENDA	1.4.3.13. 247.
Gene expression databases
ArrayExpress	P28300.
Bgee	P28300.
CleanEx	HS_LOX.
GermOnline	ENSG00000113083. Homo sapiens.
Family and domain databases
InterPro	IPR001695. Lysyl_oxidase. IPR019828. Lysyl_oxidase_CS. [Graphical view]
Pfam	PF01186. Lysyl_oxidase. 1 hit. [Graphical view]
PRINTS	PR00074. LYSYLOXIDASE.
PROSITE	PS00926. LYSYL_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15752.
PMAP-CutDB	P28300.
SOURCE	Search...

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Entry information

Entry name

LYOX_HUMAN

Accession

Primary (citable) accession number: P28300
Secondary accession number(s): B2R5Q3, Q5FWF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 1, 1993
Last modified:	July 7, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents