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Reviewed, UniProtKB/Swiss-Prot P45845 (LYOX_PIG)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-lysine 6-oxidase
    EC=1.4.3.13
Alternative name(s):
    Lysyl oxidase
Gene names
Name: LOX
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Secretedextracellular 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 componentSecreted
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMLTQ
Sulfation
TPQ
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein-lysine 6-oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Protein-lysine 6-oxidase
PRO_0000156409

Regions

Region45 – 249205Lysyl-oxidase like By similarity

Sites

Metal binding1241Copper Potential
Metal binding1261Copper Potential
Metal binding1281Copper Potential

Amino acid modifications

Modified residue18712',4',5'-topaquinone By similarity
Cross-link152 ↔ 187Lysine tyrosylquinone (Lys-Tyr) By similarity

Experimental info

Sequence conflict1211H → S AA sequence Ref.2
Sequence conflict1571L → K AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P45845-1 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: C2E71087CD799111

FASTA24929,073
        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 

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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

PIRS54337.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP45845.

Enzyme and pathway databases

BRENDA1.4.3.13. 249.

Family and domain databases

InterProIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSPR00074. LYSYLOXIDASE.
PROSITEPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYOX_PIG
AccessionPrimary (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: June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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