P45845 (LYOX_PIG) 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

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
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.
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. Probably contains sulfotyrosine.
Sequence similarities	Belongs to the lysyl oxidase family.
Mass spectrometry	Molecular mass is 29377 Da from positions 1 - 249. Determined by MALDI. Ref.2

Ontologies

Keywords
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond LTQ Sulfation TPQ
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro protein-lysine 6-oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 249	249	Protein-lysine 6-oxidase		PRO_0000156409
Regions
	Region	45 – 249	205	Lysyl-oxidase like By similarity
Sites
	Metal binding	124	1	Copper Potential
	Metal binding	126	1	Copper Potential
	Metal binding	128	1	Copper Potential
Amino acid modifications
	Modified residue	187	1	2',4',5'-topaquinone By similarity
	Disulfide bond	70 ↔ 76		By similarity
	Disulfide bond	123 ↔ 172		By similarity
	Disulfide bond	156 ↔ 162		By similarity
	Disulfide bond	183 ↔ 193		By similarity
	Disulfide bond	230 ↔ 244		By similarity
	Cross-link	152 ↔ 187		Lysine tyrosylquinone (Lys-Tyr) By similarity
Experimental info
	Sequence conflict	121	1	H → S AA sequence Ref.2
	Sequence conflict	157	1	L → K AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P45845 [UniParc]. Last modified April 17, 2007. Version 2. Checksum: C2E71087CD799111	FASTA	249	29,073
	10 20 30 40 50 60 DDPYNPYKYS DDNPYYNYYX XXERPRPGSR YRPGYGTGYF QYGLPDLVPD PYYIQASTYV 70 80 90 100 110 120 QKMSMYNLRC AAEENCLAST AYRADVRDYD HRVLLRFPQR VKNQGTSDFL PSRPRYSWEW 130 140 150 160 170 180 HSCHQHYHSM DEFSHYDLLD ASTQRRVAEG HKASFCLEDT SCDYGYHRRF ACTAHTQGLS 190 200 210 220 230 240 PGCYDTYNAD IDCQWIDITD VKPGNYILKV SVNPSYLVPE SDYSNNVVRC EIRYTGHHAY ASGCTISPY

References

[1]	Cronshaw A.D., Hulmes D.J.S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE.
[2]	"The proteolytic processing site of the precursor of lysyl oxidase." Cronshaw A.D., Fothergill-Gilmore L.A., Hulmes D.J.S. Biochem. J. 306:279-284(1995) [PubMed: 7864821] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19; 23-44; 49-121 AND 131-184, MASS SPECTROMETRY. Tissue: Skin.
[3]	"TRAMP (tyrosine rich acidic matrix protein), a protein that co-purifies with lysyl oxidase from porcine skin. Identification of TRAMP as the dermatan sulphate proteoglycan-associated 22K extracellular matrix protein." Cronshaw A.D., Macbeath J.R.E., Shackleton D.R., Collins J.F., Fothergill-Gilmore L.A., Hulmes D.J.S. Matrix 13:255-266(1993) [PubMed: 8100985] [Abstract] Cited for: PROTEIN SEQUENCE OF 131-166, SULFATION. Tissue: Skin.

Cross-references

Sequence databases
PIR	S54337.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P45845.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
GeneTree	ENSGT00590000082729.
HOVERGEN	HBG000226.
OrthoDB	EOG402WSF.
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...

Entry information

Entry name

LYOX_PIG

Accession

Primary (citable) accession number: P45845
Secondary accession number(s): Q7M3F0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 17, 2007
Last modified:	October 19, 2011
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program