P16636 (LYOX_RAT) Reviewed, UniProtKB/Swiss-Prot

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
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.
Tissue specificity	Aorta and lung. Ref.1
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. The N-terminus is blocked.
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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein LTQ TPQ
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	collagen fibril organization Inferred from direct assay. Source: RGD elastic fiber assembly Inferred from mutant phenotype. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to steroid hormone stimulus Inferred from direct assay. Source: RGD wound healing Inferred from mutant phenotype. Source: RGD
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: RGD
Molecular function	copper ion binding Inferred from mutant phenotype. Source: RGD protein-lysine 6-oxidase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 162	141			PRO_0000018524
	Chain	163 – 411	249	Protein-lysine 6-oxidase		PRO_0000018525
Regions
	Region	207 – 411	205	Lysyl-oxidase like
Sites
	Metal binding	286	1	Copper Potential
	Metal binding	288	1	Copper Potential
	Metal binding	290	1	Copper Potential
Amino acid modifications
	Modified residue	349	1	2',4',5'-topaquinone By similarity
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	138	1	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

Sequences

	Sequence		Length	Mass (Da)
	P16636 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: EE68C9C5AACDFC1A	FASTA	411	46,559
	10 20 30 40 50 60 MRFAWTVLFL GQLQFCPLLR CAPQAPREPP AAPGAWRQTI QWENNGQVFS LLSLGAQYQP 70 80 90 100 110 120 QRRRDSSATA PRADGNAAAQ PRTPILLLRD NRTASARART PSPSGVAAGR PRPAARHWFQ 130 140 150 160 170 180 VGFSPSGAGD GASRRAANRT ASPQPPQLSN LRPPSHVDRM VGDDPYNPYK YSDDNPYYNY 190 200 210 220 230 240 YDTYERPRSG SRHRPGYGTG YFQYGLPDLV PDPYYIQAST YVQKMSMYNL RCAAEENCLA 250 260 270 280 290 300 SSAYRADVRD YDHRVLLRFP QRVKNQGTSD FLPSRPRYSW EWHSCHQHYH SMDEFSHYDL 310 320 330 340 350 360 LDASTQRRVA EGHKASFCLE DTSCDYGYHR RFACTAHTQG LSPGCYDTYA ADIDCQWIDI 370 380 390 400 410 TDVQPGNYIL KVSVNPSYLV PESDYSNNVV RCEIRYTGHH AYASGCTISP Y

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence." Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D., Troxler R.F., Kagan H.M. Biochemistry 29:4863-4870(1990) [PubMed: 1973052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Aorta.
[2]	"Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence." Trackman P.C., Pratt A.M., Wolanski A., Tang S.-S., Offner G.D., Troxler R.F., Kagan H.M. Biochemistry 30:8282-8282(1991) [PubMed: 1678281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
[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]. Tissue: Testis.
[4]	"Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase." Panchenko M.V., Stetler-Stevenson W.G., Trubetskoy O.V., Gacheru S.N., Kagan H.M. J. Biol. Chem. 271:7113-7119(1996) [PubMed: 8636146] [Abstract] Cited for: PROTEIN SEQUENCE OF 163-167, PROTEOLYTIC PROCESSING OF N-TERMINAL.
[5]	"Post-translational glycosylation and proteolytic processing of a lysyl oxidase precursor." Trackman P.C., Bedell-Hogan D., Tang J., Kagan H.M. J. Biol. Chem. 267:8666-8671(1992) [PubMed: 1349020] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF N-TERMINAL.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U11038 mRNA. Translation: AAC52176.1. J02903 mRNA. Translation: AAA41537.1. BC078861 mRNA. Translation: AAH78861.1.
IPI	IPI00214661.
PIR	OXRTL. B40557.
RefSeq	NP_058757.1. NM_017061.2.
UniGene	Rn.11372.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P16636.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000019844; ENSRNOP00000019844; ENSRNOG00000014426.
GeneID	24914.
KEGG	rno:24914.
UCSC	NM_017061. rat.
Organism-specific databases
CTD	4015.
RGD	3015. Lox.
Phylogenomic databases
eggNOG	roNOG08345.
GeneTree	ENSGT00590000082729.
HOVERGEN	HBG000226.
InParanoid	P16636.
OrthoDB	EOG402WSF.
PhylomeDB	P16636.
Gene expression databases
ArrayExpress	P16636.
Genevestigator	P16636.
GermOnline	ENSRNOG00000014426. Rattus norvegicus.
Family and domain databases
InterPro	IPR001695. Lysyl_oxidase. IPR019828. Lysyl_oxidase_CS. [Graphical view]
KO	K00277.
Pfam	PF01186. Lysyl_oxidase. 1 hit. [Graphical view]
PRINTS	PR00074. LYSYLOXIDASE.
PROSITE	PS00926. LYSYL_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604837.
PMAP-CutDB	P16636.

Entry information

Entry name

LYOX_RAT

Accession

Primary (citable) accession number: P16636

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	November 1, 1995
Last modified:	November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program