B4F6N6 · LOXL2_XENTR
- ProteinLysyl oxidase homolog 2
- Geneloxl2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids767 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency. Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3. When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
Catalytic activity
- H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4+
Cofactor
Protein has several cofactor binding sites:
Note: Contains 1 lysine tyrosylquinone.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 542 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 543 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 619 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 621 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 623 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 715 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 717 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 720 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 721 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysyl oxidase homolog 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Silurana
Accessions
- Primary accessionB4F6N6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MLVTHIFLLTLSLSVPTLG | ||||||
Chain | PRO_0000418007 | 20-767 | Lysyl oxidase homolog 2 | |||
Sequence: QYEHWLYYPEYQASQAPEPLPTPARNVPQIHVRLAGEKRKHNEGRVEVYYEGEWGTVCDDDFSMYAAHIVCRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDCKHSEDVGVQCSDRRIPGFKVSNELPGQLEGLNIQVEEVRIRAILSAYRKRVPVTEGFVEVKVQGSWRQVCNAEWSSKNSRVVCGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTCSDGSPAVVSCTPGRAFAPSPGTGFGKAFRQEQPLVRLRGGANTGEGRVEVLKNGEWGTICDDKWNLVTASVVCRELGFGSAKEALAGAQMGQGMGHIHMSEIQCNGFEKSLIDCKFNVHSQGCNHEEDAAVRCNVPAMGFENQVRLSGGRHPTEGRVEVLMERNGTLRWGTVCSDTWGTMEAMIVCRQLGLGFASHAFQETWYWQGDINADDVVMSGVKCSGTEMSLAHCRHDGANINCPRGGGRFAAGVSCVETAPDLVLNAALVEQTTYLEDRPMFMLQCAHEEQCLSSSADRTSPTTGYRRLLRFSSQIHNNGQADFRPKTGRHSWIWHDCHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDSECETDVQKQYACANFGEQGITVGCWDVYRHDIDCQWVDITDVAPGDYFFQVIINPNQEVAESDYTNNIMKCRCRYDGHRIWMYNCHIGGSYSTETEEKFEHFSGLMNNQLSTR | ||||||
Disulfide bond | 77↔141 | |||||
Sequence: CDDDFSMYAAHIVCRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDC | ||||||
Disulfide bond | 90↔151 | |||||
Sequence: CRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDCKHSEDVGVQC | ||||||
Disulfide bond | 121↔131 | |||||
Sequence: CNGREKSIASC | ||||||
Disulfide bond | 211↔284 | |||||
Sequence: CNAEWSSKNSRVVCGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTC | ||||||
Disulfide bond | 224↔294 | |||||
Sequence: CGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTCSDGSPAVVSC | ||||||
Disulfide bond | 258↔268 | |||||
Sequence: CTGNEAHLSSC | ||||||
Glycosylation | 281 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 344↔407 | |||||
Sequence: CDDKWNLVTASVVCRELGFGSAKEALAGAQMGQGMGHIHMSEIQCNGFEKSLIDCKFNVHSQGC | ||||||
Disulfide bond | 357↔417 | |||||
Sequence: CRELGFGSAKEALAGAQMGQGMGHIHMSEIQCNGFEKSLIDCKFNVHSQGCNHEEDAAVRC | ||||||
Disulfide bond | 388↔398 | |||||
Sequence: CNGFEKSLIDC | ||||||
Glycosylation | 448 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 457↔523 | |||||
Sequence: CSDTWGTMEAMIVCRQLGLGFASHAFQETWYWQGDINADDVVMSGVKCSGTEMSLAHCRHDGANINC | ||||||
Disulfide bond | 470↔536 | |||||
Sequence: CRQLGLGFASHAFQETWYWQGDINADDVVMSGVKCSGTEMSLAHCRHDGANINCPRGGGRFAAGVSC | ||||||
Disulfide bond | 504↔514 | |||||
Sequence: CSGTEMSLAHC | ||||||
Disulfide bond | 566↔618 | |||||
Sequence: CAHEEQCLSSSADRTSPTTGYRRLLRFSSQIHNNGQADFRPKTGRHSWIWHDC | ||||||
Disulfide bond | 572↔688 | |||||
Sequence: CLSSSADRTSPTTGYRRLLRFSSQIHNNGQADFRPKTGRHSWIWHDCHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDSECETDVQKQYACANFGEQGITVGCWDVYRHDIDC | ||||||
Glycosylation | 637 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Cross-link | 646↔682 | Lysine tyrosylquinone (Lys-Tyr) | ||||
Sequence: KASFCLEDSECETDVQKQYACANFGEQGITVGCWDVY | ||||||
Disulfide bond | 650↔666 | |||||
Sequence: CLEDSECETDVQKQYAC | ||||||
Disulfide bond | 656↔678 | |||||
Sequence: CETDVQKQYACANFGEQGITVGC | ||||||
Modified residue | 682 | 2',4',5'-topaquinone | ||||
Sequence: Y | ||||||
Disulfide bond | 725↔739 | |||||
Sequence: CRCRYDGHRIWMYNC |
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
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-152 | SRCR 1 | ||||
Sequence: VRLAGEKRKHNEGRVEVYYEGEWGTVCDDDFSMYAAHIVCRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDCKHSEDVGVQCS | ||||||
Domain | 181-295 | SRCR 2 | ||||
Sequence: IRAILSAYRKRVPVTEGFVEVKVQGSWRQVCNAEWSSKNSRVVCGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTCSDGSPAVVSCT | ||||||
Domain | 319-418 | SRCR 3 | ||||
Sequence: VRLRGGANTGEGRVEVLKNGEWGTICDDKWNLVTASVVCRELGFGSAKEALAGAQMGQGMGHIHMSEIQCNGFEKSLIDCKFNVHSQGCNHEEDAAVRCN | ||||||
Domain | 428-537 | SRCR 4 | ||||
Sequence: VRLSGGRHPTEGRVEVLMERNGTLRWGTVCSDTWGTMEAMIVCRQLGLGFASHAFQETWYWQGDINADDVVMSGVKCSGTEMSLAHCRHDGANINCPRGGGRFAAGVSCV | ||||||
Region | 541-744 | Lysyl-oxidase like | ||||
Sequence: PDLVLNAALVEQTTYLEDRPMFMLQCAHEEQCLSSSADRTSPTTGYRRLLRFSSQIHNNGQADFRPKTGRHSWIWHDCHRHYHSMEVFTHYDLLSLNGTKVAEGHKASFCLEDSECETDVQKQYACANFGEQGITVGCWDVYRHDIDCQWVDITDVAPGDYFFQVIINPNQEVAESDYTNNIMKCRCRYDGHRIWMYNCHIGGS |
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.
- Length767
- Mass (Da)85,683
- Last updated2012-06-13 v2
- ChecksumBB7B467174A98552
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 309 | in Ref. 2; AAI67947 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAMC01014210 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014211 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014212 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014213 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014214 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014215 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014216 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014217 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014218 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014219 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014220 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014221 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014222 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014223 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014224 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014225 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AAMC01014226 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC167947 EMBL· GenBank· DDBJ | AAI67947.1 EMBL· GenBank· DDBJ | mRNA |