F1RD85 · LOX3A_DANRE
- ProteinLysyl oxidase homolog 3A
- Geneloxl3a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids739 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins. Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin. Can mediate oxidation of lysine residues that are acetylated. Also able to catalyze deacetylation of lysine residues (By similarity).
Catalytic activity
- H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4+
- H2O + N6-acetyl-L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + acetamide + H2O2
Cofactor
Protein has several cofactor binding sites:
Note: Contains 1 lysine tyrosylquinone.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular space | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | copper ion binding | |
Molecular Function | fibronectin binding | |
Molecular Function | protein-lysine 6-oxidase activity | |
Biological Process | collagen fibril organization | |
Biological Process | fibronectin fibril organization | |
Biological Process | inflammatory response | |
Biological Process | lung development | |
Biological Process | negative regulation of T-helper 17 cell lineage commitment | |
Biological Process | peptidyl-lysine oxidation | |
Biological Process | positive regulation of integrin-mediated signaling pathway | |
Biological Process | roof of mouth development | |
Biological Process | somite development | |
Biological Process | spinal cord development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysyl oxidase homolog 3A
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionF1RD85
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: It is unclear how loxl3a is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (loxl2) also has intracellular and extracellular localization despite the presence of a signal sequence.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MLRSELRDMVVAMVLWGILLPFCLS | ||||||
Chain | PRO_5003269238 | 26-739 | Lysyl oxidase homolog 3A | |||
Sequence: QTTSPSQDGKIKFRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICKDERLPGFAESNIIEMQVDEKRMEKIRLRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCVPGLQFTQGRVRKAKLNPVPQMRLKGGARAGEGRVEVLKGSEWGTVCDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVICNIPYMGFEKLMRLTGGRTRLEGRVELLLPAGGGVRDWGLICGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVICSDMASDLVLNAPLVEQTVYIEDRPLHLLYCAAEENCLAKSAAQASWPYGHRRLLRFSSEIHNIGKADFRPRLGRHSWVWHECHRHYHSMDIFTYYDLLSLNGTKVADGHKASFCLEDTECHEGVSKRYECANFGEQGITVGCWDLYRHDIDCQWIDITDVSPGNYILQVIINPNFEVAESDFTNNAMRCNCKYDGHRVWLHKCHLGDSFSEEAEKEFEHYPGQLNNKIS | ||||||
Disulfide bond | 64↔128 | |||||
Sequence: CDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDC | ||||||
Disulfide bond | 77↔138 | |||||
Sequence: CRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVIC | ||||||
Disulfide bond | 108↔118 | |||||
Sequence: CGGSENSIEKC | ||||||
Disulfide bond | 196↔261 | |||||
Sequence: CNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPC | ||||||
Disulfide bond | 209↔271 | |||||
Sequence: CGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSC | ||||||
Disulfide bond | 238↔248 | |||||
Sequence: CSGNEAHLSAC | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 318↔382 | |||||
Sequence: CDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDC | ||||||
Disulfide bond | 331↔392 | |||||
Sequence: CRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVIC | ||||||
Disulfide bond | 362↔372 | |||||
Sequence: CGGDEKSLWDC | ||||||
Disulfide bond | 433↔497 | |||||
Sequence: CGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSC | ||||||
Disulfide bond | 446↔510 | |||||
Sequence: CRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVIC | ||||||
Glycosylation | 468 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 479↔489 | |||||
Sequence: CKGDEMTLTDC | ||||||
Glycosylation | 611 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Cross-link | 620↔656 | Lysine tyrosylquinone (Lys-Tyr) | ||||
Sequence: KASFCLEDTECHEGVSKRYECANFGEQGITVGCWDLY | ||||||
Modified residue | 656 | 2',4',5'-topaquinone | ||||
Sequence: Y |
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Weakly expressed at 30 hours post fertilization (hpf) in the ventral head mesenchyme, but not spatially restricted after this time-point.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-139 | SRCR 1 | ||||
Sequence: FRLAGYPRKHNEGRIEVFYNREWGTICDDDFTLANAHVLCRQLGFVEALSWSHSAKYGPGSGKIWLDNVICGGSENSIEKCVSRGWGNSDCTHQEDAGVICK | ||||||
Domain | 166-272 | SRCR 2 | ||||
Sequence: LRPLKGAHAGRLPVTEGVVEVKFKEGWGHICNTGWTIKNSRVVCGMMGFPSQRSVGKKPNSLKSAYRIHSVTCSGNEAHLSACTMEFSRANSSAPCPGGGAAVVSCV | ||||||
Domain | 293-393 | SRCR 3 | ||||
Sequence: MRLKGGARAGEGRVEVLKGSEWGTVCDDHWNLQSASVVCRELGFGTAKEALTGARMGQGMGPIYMNEVQCGGDEKSLWDCPHQSITAEDCKHTEDASVICN | ||||||
Domain | 403-511 | SRCR 4 | ||||
Sequence: MRLTGGRTRLEGRVELLLPAGGGVRDWGLICGDGWTSREAMVVCRQLGLGHASSGLRETWYWDSSNVTEMVMSGVKCKGDEMTLTDCQHHSVVSCKRAGAQFSAGVICS |
Sequence similarities
Belongs to the lysyl oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length739
- Mass (Da)82,133
- Last updated2011-05-03 v1
- Checksum4EC48A1F52FF06D7
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5H1ZRI5 | A0A5H1ZRI5_DANRE | loxl3a | 791 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FP085411 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
FP085432 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
EF030483 EMBL· GenBank· DDBJ | ABM86969.1 EMBL· GenBank· DDBJ | mRNA |