Lox
entrez
24914
canonical
uniprot
P16636
canonical
ensembl
ENSRNOG00000014426
resolver
ensembl
ENSRNOG00055018147
resolver
ensembl
ENSRNOG00060012348
resolver
ensembl
ENSRNOG00065004171
resolver
ensp
ENSRNOP00000019844
resolver
ensp
ENSRNOP00055024718
resolver
ensp
ENSRNOP00060016498
resolver
ensp
ENSRNOP00065004350
resolver
enst
ENSRNOT00000019844
resolver
enst
ENSRNOT00055030727
resolver
enst
ENSRNOT00060020923
resolver
enst
ENSRNOT00065006090
resolver
genesymbol
Lox
resolver
uniprot_entry
LYOX_RAT
resolver
amino_acid_sequence
MRFAWTVLFLGQLQFCPLLRCAPQAPREPPAAPGAWRQTIQWENNGQVFSLLSLGAQYQPQRRRDSSATAPRADGNAAAQPRTPILLLRDNRTASARARTPSPSGVAAGRPRPAARHWFQVGFSPSGAGDGASRRAANRTASPQPPQLSNLRPPSHVDRMVGDDPYNPYKYSDDNPYYNYYDTYERPRSGSRHRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYSNNVVRCEIRYTGHHAYASGCTISPY
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 (PubMed:16432278). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity). {ECO:0000250|UniProtKB:P28301, ECO:0000269|PubMed:16432278}.
uniprot
proteins
mass_dalton
46559
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 (By similarity). 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 (By similarity). 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:0000250|UniProtKB:P28301}.; 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
1349020
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16432278
uniprot
proteins
pubmed
1678281
uniprot
proteins
pubmed
1973052
uniprot
proteins
pubmed
26479776
uniprot
proteins
pubmed
8636146
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28301}. Secreted, extracellular space.
uniprot
proteins