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Leishmanolysin-like peptidase (invadolysin, LMLN)
Function:
- essential for the coordination of mitotic progression
- plays a role in cell migration (putative)
Cofactor: binds 1 Zn+ per subunit (putative)
Structure: belongs to the peptidase M8 family
Compartment:
- cytoplasm
- found in ring-likestructures resembling invadopodia
- in migrating cells it relocalizes from internal structures to the leading edge of cells
Alternative splicing: named isoforms=2
General
glycoprotein
peptidase; peptide hydrolase
Properties
SIZE: entity length = 655 aa
MW = 74 kD
MOTIF: cysteine residue {C172}
MODIFICATION: cysteine residue {C235}
cysteine residue {C235}
MODIFICATION: cysteine residue {C172}
Zn+2-binding site
SITE: 272-272
glutamate residue {E273}
Zn+2-binding site
SITE: 276-276
N-glycosylation site {N308}
active site
cysteine residue {C358}
MODIFICATION: cysteine residue {C419}
Zn+2-binding site
SITE: 378-378
cysteine residue {C419}
MODIFICATION: cysteine residue {C358}
cysteine residue {C431}
MODIFICATION: cysteine residue {C525}
cysteine residue {C525}
MODIFICATION: cysteine residue {C431}
cysteine residue {C555}
MODIFICATION: cysteine residue {C602}
cysteine residue {C602}
MODIFICATION: cysteine residue {C555}
N-glycosylation site {N615}
Database Correlations
UniProt Q96KR4
Pfam PF01457
References
UniProt :accession Q96KR4