Lox
entrez
16948
canonical
uniprot
P28301
canonical
ensembl
ENSMUSG00000024529
resolver
ensp
ENSMUSP00000025409
resolver
ensp
ENSMUSP00000129247
resolver
enst
ENSMUST00000025409
resolver
enst
ENSMUST00000171470
resolver
genesymbol
Lox
resolver
genesymbol_syn
Rrg
resolver
uniprot
Q3TP83
resolver
uniprot
Q3TXH3
resolver
uniprot_entry
LYOX_MOUSE
resolver
uniprot_entry
Q3TP83_MOUSE
resolver
uniprot_entry
Q3TXH3_MOUSE
resolver
amino_acid_sequence
MRFAWAVLLLGPLQLCPLLRCAPQTPREPPAAPGAWRQTIQWENNGQVFSLLSLGAQYQPQRRRDPSATARRPDGDAASQPRTPILLLRDNRTASTRARTPSPSGVAAGRPRPAARHWFQAGFSPSGARDGASRRAANRTASPQPPQLSNLRPPSHIDRMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGSRNRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY
uniprot
proteins
ec_number
1.4.3.13
uniprot
proteins
function
FUNCTION: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (PubMed:27432961). {ECO:0000269|PubMed:27432961}.
uniprot
proteins
mass_dalton
46701
uniprot
proteins
mutagenesis
MUTAGEN 292; /note="M->R: Homozygous mice display tortuous vessels aneurysm, loss of oxidase activity and die perinatally of aortic aneurysm and dissection. Heterozygous mice display thicker arterial wall with discontinuous elastic lamellae."; /evidence="ECO:0000269|PubMed:27432961
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:P33072}.; PTM: Proteolytically cleaved by BMP1 which removes the propeptide (PubMed:20181949). Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (By similarity). The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (PubMed:16251195). Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (By similarity). Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (By similarity). {ECO:0000250|UniProtKB:P28300, ECO:0000269|PubMed:16251195, ECO:0000269|PubMed:20181949}.; PTM: Sulfated at Tyr-181 and also at either Tyr-177 or Tyr-178 which enhances binding to collagen. {ECO:0000250|UniProtKB:P28300}.
uniprot
proteins
protein_family
Lysyl oxidase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16251195
uniprot
proteins
pubmed
1678898
uniprot
proteins
pubmed
20181949
uniprot
proteins
pubmed
27432961
uniprot
proteins
pubmed
8100214
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27432961}. Secreted, extracellular space.
uniprot
proteins