Search
lysyl oxidase homolog 3 (lysyl oxidase-like protein 3, LOXL3, LOXL)
Function:
Cofactor: Cu+2
Structure:
- contains 1 lysine tyrosylquinone
- contains 4 SRCR domains
- 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
Compartment: secreted
Expression:
- widely expressed
- highest levels in placenta, heart, ovary, testis, small intestine, spleen
General
glycoprotein
metalloprotein
oxidoreductase
secreted protein
Properties
SIZE: MW = 83 kD
entity length = 753 aa
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-25}
SRCR 1 {44-145}
MOTIF: cysteine residue {C70}
MODIFICATION: cysteine residue {C134}
cysteine residue {C83}
MODIFICATION: cysteine residue {C144}
N-glycosylation site {N111}
cysteine residue {C114}
MODIFICATION: cysteine residue {C124}
cysteine residue {C124}
MODIFICATION: cysteine residue {C114}
cysteine residue {C134}
MODIFICATION: cysteine residue {C70}
cysteine residue {C144}
MODIFICATION: cysteine residue {C83}
SRCR 2 {169-282}
MOTIF: cysteine residue {C201}
MODIFICATION: cysteine residue {C271}
cysteine residue {C214}
MODIFICATION: cysteine residue {C281}
cysteine residue {C248}
MODIFICATION: cysteine residue {C258}
cysteine residue {C258}
MODIFICATION: cysteine residue {C248}
N-glycosylation site {N266}
cysteine residue {C271}
MODIFICATION: cysteine residue {C201}
cysteine residue {C281}
MODIFICATION: cysteine residue {C214}
SRCR 3 {307-407}
MOTIF: cysteine residue {C332}
MODIFICATION: cysteine residue {C396}
cysteine residue {C345}
MODIFICATION: cysteine residue {C406}
cysteine residue {C376}
MODIFICATION: cysteine residue {C386}
cysteine residue {C386}
MODIFICATION: cysteine residue {C376}
N-glycosylation site {N390}
cysteine residue {C396}
MODIFICATION: cysteine residue {C332}
cysteine residue {C406}
MODIFICATION: cysteine residue {C345}
SRCR 4 {417-525}
MOTIF: cysteine residue {C446}
MODIFICATION: cysteine residue {C511}
cysteine residue {C459}
MODIFICATION: cysteine residue {C524}
N-glycosylation site {N481}
cysteine residue {C492}
MODIFICATION: cysteine residue {C502}
cysteine residue {C502}
MODIFICATION: cysteine residue {C492}
cysteine residue {C511}
MODIFICATION: cysteine residue {C446}
cysteine residue {C524}
MODIFICATION: cysteine residue {C459}
Lysyl-oxidase like {529-732}
MOTIF: copper [Cu]-binding site
SITE: 607-607
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 609-609
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 611-611
MOTIF: histidine residue (3)
N-glycosylation site {N625}
Database Correlations
OMIM 607163
UniProt P58215
PFAM correlations
References
UniProt :accession P58215