Protein-lysine 6-oxidase precursor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P28301 (LYOX_MOUSE)

Last modified June 16, 2009. Version 79. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Ras excision protein

Gene names

Name:	Lox
Synonyms:	Rrg

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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. 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. Contains 1 lysine tyrosylquinone By similarity.
Subcellular location	Secreted › extracellular space.
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.
Miscellaneous	The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin.
Sequence similarities	Belongs to the lysyl oxidase family.

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Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein LTQ TPQ
Gene Ontology (GO)
Biological process	blood vessel development Inferred from mutant phenotype. Source: MGI collagen fibril organization Inferred from mutant phenotype. Source: MGI elastic fiber assembly Inferred from mutant phenotype. Source: MGI lung development Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase signaling pathway Non-traceable author statement. Source: UniProtKB
Cellular component	collagen Inferred from direct assay. Source: MGI extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.4 Inferred from physical interaction. Source: MGI protein-lysine 6-oxidase activity Inferred from direct assay. Source: MGI
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

Potential

Propeptide

22 – 162

141

By similarity

PRO_0000018522

Chain

163 – 411

249

Protein-lysine 6-oxidase

PRO_0000018523

Regions

Region

207 – 411

205

Lysyl-oxidase like

Sites

Metal binding

286

Copper Potential

Metal binding

288

Copper Potential

Metal binding

290

Copper Potential

Amino acid modifications

Modified residue

349

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

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

138

N-linked (GlcNAc...) Potential

Cross-link

314 ↔ 349

Lysine tyrosylquinone (Lys-Tyr) By similarity

Experimental info

Sequence conflict

333

A → G in AAA99899. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P28301-1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: DBC0563A9C0AEB52
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FASTA

411

46,701

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lysyl oxidase and rrg messenger RNA." Kenyon K., Contente S., Trackman P.C., Tang J., Kagan H.M., Friedman R.M. Science 253:802-802(1991) [PubMed: 1678898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of the mouse lysyl oxidase gene." Contente S., Csiszar K., Kenyon K., Friedman R.M. Genomics 16:395-400(1993) [PubMed: 8100214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NIH Swiss.
[3]	"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]. Strain: FVB/N-3. Tissue: Mammary gland.
[4]	"The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers." Thomassin L., Werneck C.C., Broekelmann T.J., Gleyzal C., Hornstra I.K., Mecham R.P., Sommer P. J. Biol. Chem. 280:42848-42855(2005) [PubMed: 16251195] [Abstract] Cited for: ROLE OF PROPEPTIDE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M65142 mRNA. Translation: AAA19032.1. M65143 mRNA. Translation: AAA20185.1. L04262, L04263, L04264 Genomic DNA. Translation: AAA99899.1. BC018439 mRNA. Translation: AAH18439.1.
IPI	IPI00310056.
PIR	OXMSL. A47005.
RefSeq	NP_034858.2.
UniGene	Mm.172
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P28301. 1 interaction.
Genome annotation databases
Ensembl	ENSMUSG00000024529. Mus musculus. [Contig view]
GeneID	16948.
KEGG	mmu:16948.
Organism-specific databases
MGI	MGI:96817. Lox.
Phylogenomic databases
HOGENOM	P28301.
HOVERGEN	P28301.
OMA	P28301. ENNGQVF.
Enzyme and pathway databases
BRENDA	1.4.3.13. 244.
Gene expression databases
ArrayExpress	P28301.
Bgee	P28301.
CleanEx	MM_LOX.
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	290992.
SOURCE	Search...

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Entry information

Entry name

LYOX_MOUSE

Accession

Primary (citable) accession number: P28301

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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