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

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P28301 (LYOX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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 protein level

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. Proteolytically activated by BMP1.
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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein LTQ TPQ
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood vessel development Inferred from mutant phenotype PubMed 12417550. Source: MGI collagen fibril organization Inferred from mutant phenotype PubMed 16126250. Source: MGI elastic fiber assembly Inferred from mutant phenotype PubMed 12417550 PubMed 16192629. Source: MGI lung development Inferred from mutant phenotype PubMed 16192629. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara wound healing Inferred from electronic annotation. Source: Compara
Cellular_component	collagen Inferred from direct assay PubMed 7901452. Source: MGI extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	copper ion binding Inferred from electronic annotation. Source: Compara protein-lysine 6-oxidase activity Inferred from direct assay PubMed 14140 PubMed 14741400 PubMed 16192629 PubMed 20889. Source: MGI
Complete GO annotation...

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

Disulfide bond

232 ↔ 238

By similarity

Disulfide bond

285 ↔ 334

By similarity

Disulfide bond

318 ↔ 324

By similarity

Disulfide bond

345 ↔ 355

By similarity

Disulfide bond

392 ↔ 406

By similarity

Cross-link

314 ↔ 349

Lysine tyrosylquinone (Lys-Tyr) By similarity

Experimental info

Sequence conflict

333

A → G in AAA99899. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P28301 [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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: ROLE OF PROPEPTIDE.
[5]	"Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase." Maruhashi T., Kii I., Saito M., Kudo A. J. Biol. Chem. 285:13294-13303(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC CLEAVAGE BY BMP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_010728.2.
UniGene	Mm.172.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P28301. 3 interactions.
MINT	MINT-1549500.
PTM databases
PhosphoSite	P28301.
Proteomic databases
PaxDb	P28301.
PRIDE	P28301.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025409; ENSMUSP00000025409; ENSMUSG00000024529. ENSMUST00000171470; ENSMUSP00000129247; ENSMUSG00000024529.
GeneID	16948.
KEGG	mmu:16948.
Organism-specific databases
CTD	4015.
MGI	MGI:96817. Lox.
Phylogenomic databases
eggNOG	NOG69196.
HOGENOM	HOG000234262.
HOVERGEN	HBG000226.
InParanoid	P28301.
KO	K00277.
OMA	YSDDNPY.
OrthoDB	EOG402WSF.
Gene expression databases
ArrayExpress	P28301.
Bgee	P28301.
CleanEx	MM_LOX.
Genevestigator	P28301.
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
NextBio	290992.
SOURCE	Search...

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:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents