P33072 (LYOX_BOVIN) 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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	418 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. Ref.3 Contains 1 lysine tyrosylquinone. Ref.3
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 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)
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
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 169	149	By similarity		PRO_0000045436
	Chain	170 – 418	249	Protein-lysine 6-oxidase		PRO_0000045437
Regions
	Region	214 – 418	205	Lysyl-oxidase like
Sites
	Metal binding	293	1	Copper Potential
	Metal binding	295	1	Copper Potential
	Metal binding	297	1	Copper Potential
Amino acid modifications
	Modified residue	356	1	2',4',5'-topaquinone
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Disulfide bond	239 ↔ 245		Ref.4
	Disulfide bond	292 ↔ 341		Ref.4
	Disulfide bond	325 ↔ 331		Ref.4
	Disulfide bond	352 ↔ 362		Ref.4
	Disulfide bond	399 ↔ 413		Ref.4
	Cross-link	321 ↔ 356		Lysine tyrosylquinone (Lys-Tyr)
Experimental info
	Sequence conflict	413 – 414	2	CT → QS AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P33072 [UniParc]. Last modified January 10, 2006. Version 3. Checksum: EC4C0F36A29FD860	FASTA	418	47,115
	10 20 30 40 50 60 MRFAWTALLG SLQLCALVRC APPAASHRQP PREQAAAPGA WRQKIQWENN GQVFSLLSLG 70 80 90 100 110 120 SQYQPQRRRD PGATAPGAAN ATAPQMRTPI LLLRNNRTAA ARVRTAGPSA AAAGRPRPAA 130 140 150 160 170 180 RHWFQAGYST SGAHDAGTSR ADNQTAPGEV PTLSNLRPPN RVEVDGMVGD DPYNPYKYTD 190 200 210 220 230 240 DNPYYNYYDT YERPRPGSRY RPGYGTGYFQ YGLPDLVPDP YYIQASTYVQ KMAMYNLRCA 250 260 270 280 290 300 AEENCLASSA YRXDVRDYDH RVLLRFPQRV KNQGTSDFLP SRPRYSWEWH SCHQHYHSMD 310 320 330 340 350 360 EFSHYDLLDA STQRRVAEGH KASFCLEDTS CDYGYHRRFA CTAHTQGLSP GCYDTYNADI 370 380 390 400 410 DCQWIDITDV KPGNYILKVS VNPSYLVPES DYSNNVVRCE IRYTGHHAYA SGCTISPY

References

[1]	"Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1." Borel A., Eichenberger D., Farjanel J., Kessler E., Gleyzal C., Hulmes D.J.S., Sommer P., Font B. J. Biol. Chem. 276:48944-48949(2001) [PubMed: 11684696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skin.
[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 29:4863-4870(1990) [PubMed: 1973052] [Abstract] Cited for: PROTEIN SEQUENCE OF 200-231; 266-284; 297-305; 316-323; 354-359; 379-398 AND 403-418. Tissue: Aorta.
[3]	"A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains." Wang S.X., Mure M., Medzihradszky K.F., Burlingame A.L., Brown D.E., Dooley D.M., Smith A.J., Kagan H.M., Klinman J.P. Science 273:1078-1084(1996) [PubMed: 8688089] [Abstract] Cited for: COFACTOR.
[4]	"Identification of the disulfide bonds of lysyl oxidase." Chen X., Greenaway F.T. J. Neural Transm. 118:1111-1114(2011) [PubMed: 21188434] [Abstract] Cited for: DISULFIDE BONDS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF421186 mRNA. Translation: AAL13313.1.
IPI	IPI00706501.
PIR	B30352.
UniGene	Bt.98817.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P33072.
Proteomic databases
PRIDE	P33072.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG09341.
GeneTree	ENSGT00590000082729.
HOVERGEN	HBG000226.
InParanoid	P33072.
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_BOVIN

Accession

Primary (citable) accession number: P33072
Secondary accession number(s): Q95L38

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	January 10, 2006
Last modified:	October 19, 2011
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program