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hepatocyte growth factor activator (HGFAC)
Function:
- activates hepatocyte growth factor by converting it from a single chain to a heterodimeric form
Structure:
- heterodimer of a short chain & a long chain linked by a disulfide bond
- belongs to the peptidase S1 family
- contains 2 EGF-like domains
- contains 1 fibronectin type-I domain
- contains 1 fibronectin type-II domain
- contains 1 kringle domain
- contains 1 peptidase S1 domain
Compartment:
- secreted
- secreted as an inactive single-chain precursor & is then activated to a heterodimeric form
Expression: liver
Note: uncertain whether Met-1 is the initiator
General
glycoprotein
serine protease
Properties
SIZE: entity length = 655 aa
MW = 71 kD
MOTIF: signal sequence {1-35}
N-glycosylation site {N48}
fibronectin type II domain or F2 module
SITE: 103-150
FOR-BINDING-OF: collagen
MOTIF: cysteine residue {*1}
MODIFICATION: cysteine residue {*3}
cysteine residue {*2}
MODIFICATION: cysteine residue {*4}
cysteine residue {*3}
MODIFICATION: cysteine residue {*1}
cysteine residue {*4}
MODIFICATION: cysteine residue {*2}
cysteine residue {C108}
MODIFICATION: cysteine residue {C133}
cysteine residue {C122}
MODIFICATION: cysteine residue {C148}
cysteine residue {C133}
MODIFICATION: cysteine residue {C108}
cysteine residue {C148}
MODIFICATION: cysteine residue {C122}
EGF domain {160-198}
MOTIF: cysteine residue {C164}
MODIFICATION: cysteine residue {C175}
cysteine residue {C169}
MODIFICATION: cysteine residue {C186}
cysteine residue {C175}
MODIFICATION: cysteine residue {C164}
cysteine residue {C186}
MODIFICATION: cysteine residue {C169}
cysteine residue {C188}
MODIFICATION: cysteine residue {C197}
cysteine residue {C197}
MODIFICATION: cysteine residue {C188}
fibronectin type I domain or F1 module {200-240}
MOTIF: cysteine residue {C202}
MODIFICATION: cysteine residue {C230}
cysteine residue {C228}
MODIFICATION: cysteine residue {C237}
cysteine residue {C230}
MODIFICATION: cysteine residue {C202}
cysteine residue {C237}
MODIFICATION: cysteine residue {C228}
EGF domain {241-279}
MOTIF: cysteine residue {C245}
MODIFICATION: cysteine residue {C256}
cysteine residue {C250}
MODIFICATION: cysteine residue {C267}
cysteine residue {C256}
MODIFICATION: cysteine residue {C245}
cysteine residue {C267}
MODIFICATION: cysteine residue {C250}
cysteine residue {C269}
MODIFICATION: cysteine residue {C278}
cysteine residue {C278}
MODIFICATION: cysteine residue {C269}
Kringle {286-367}
MOTIF: cysteine residue {C286}
MODIFICATION: cysteine residue {C367}
N-glycosylation site {N290}
cysteine residue {C307}
MODIFICATION: cysteine residue {C349}
cysteine residue {C338}
MODIFICATION: cysteine residue {C362}
cysteine residue {C349}
MODIFICATION: cysteine residue {C307}
cysteine residue {C362}
MODIFICATION: cysteine residue {C338}
cysteine residue {C367}
MODIFICATION: cysteine residue {C286}
cysteine residue {C394}
MODIFICATION: cysteine residue {C-INTERCHAIN}
S1 domain {408-646}
MOTIF: cysteine residue {C432}
MODIFICATION: cysteine residue {C448}
cysteine residue {C440}
MODIFICATION: cysteine residue {C510}
histidine residue {H447}
cysteine residue {C448}
MODIFICATION: cysteine residue {C432}
N-glycosylation site {N468}
N-glycosylation site {N492}
aspartate residue {D497}
cysteine residue {C510}
MODIFICATION: cysteine residue {C440}
cysteine residue {C535}
MODIFICATION: cysteine residue {C604}
N-glycosylation site {N546}
cysteine residue {C567}
MODIFICATION: cysteine residue {C583}
cysteine residue {C583}
MODIFICATION: cysteine residue {C567}
cysteine residue {C594}
MODIFICATION: cysteine residue {C622}
serine residue {S598}
cysteine residue {C604}
MODIFICATION: cysteine residue {C535}
cysteine residue {C622}
MODIFICATION: cysteine residue {C594}
Database Correlations
OMIM 604552
UniProt Q04756
PFAM correlations
Entrez Gene 3083
Kegg hsa:3083
References
UniProt :accession Q04756