Reviewed,
UniProtKB/Swiss-Prot P45845 (LYOX_PIG)
Last modified
November 25, 2008.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein-lysine 6-oxidase EC=1.4.3.13 Alternative name(s): Lysyl oxidase | ||
| Gene names |
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| Organism | Sus scrofa (Pig) | ||
| 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. |
| Sequence processing | The displayed sequence is not processed. |
| 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 + O(2) + H(2)O = peptidyl-allysyl-peptide + NH(3) + H(2)O(2). |
| Cofactor | Copper By similarity. Contains 1 lysine tyrosylquinone By similarity. |
| Subcellular location | |
| 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 weight 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 | LTQ Sulfation TPQ |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: InterPro protein-lysine 6-oxidase activityInferred from electronic annotation. Source: InterPro |
| 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 | ||||||||
| 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
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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 | |
|---|---|
| PIR | S54337. |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P45845. |
Family and domain databases | |
| InterPro | IPR001695. Lysyl_oxidase. [Graphical view] |
| Pfam | PF01186. Lysyl_oxidase. 1 hit. [Graphical view] |
| 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 |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


