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hyaluronan-binding protein 2; plasma hyaluronan-binding protein; hepatocyte growth factor activator-like protein; factor VII-activating protease; factor seven-activating protease; FSAP [Contains: hyaluronan-binding protein 2 50 kD heavy chain; hyaluronan-binding protein 2 50 kD heavy chain alternate form; hyaluronan-binding protein 2 27 kD light chain; hyaluronan-binding protein 2 27 kDa light chain alternate form] (HABP2, HGFAL, PHBP)
Function:
1) cleaves fibrinogen alpha-chain at multiple sites & fibrinogen beta-chain between Lys-53 & Lys-54
2) does NOT cleave fibrinogen gamma-chain, thus does NOT initiate formation of fibrin clot & does NOT cause fibrinolysis directly
3) does NOT cleave prothrombin & plasminogen but converts pro-urokinase) to active urokinase
4) activates coagulation factor VII
5) proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kD heavy chain & cleavage at Arg-313 or Lys-319 can give rise to the 27 kD light chain
6) heavy chain can undergo further proteolytic cleavage at Lys-169 or Arg-170 to give rise to 2 inactive 26 kD fragments
7) light chain can undergo further proteolytic cleavage at Arg-480 to give rise to inactive 17 kD & 8 kD fragments
Structure:
1) heterodimer; disulfide-linked
- heterodimer of a 50 kD heavy chain & a 27 kD light chain linked by a disulfide bond
2) belongs to the peptidase S1 family
3) contains 3 EGF-like domains
- contains 1 kringle domain
- contains 1 peptidase S1 domain
Compartment:
- secreted as an inactive single-chain precursor, activated to a heterodimeric form
General
glycoprotein
hyaluronan-binding protein
protease; proteinase; endopeptidase
secreted protein
Properties
SIZE: MW = 63 kD
entity length = 560 aa
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-23}
N-glycosylation site {N54}
EGF domain {73-109}
MOTIF: cysteine residue {C77}
MODIFICATION: cysteine residue {C88}
cysteine residue {C82}
MODIFICATION: cysteine residue {C97}
cysteine residue {C88}
MODIFICATION: cysteine residue {C77}
cysteine residue {C97}
MODIFICATION: cysteine residue {C82}
cysteine residue {C99}
MODIFICATION: cysteine residue {C108}
cysteine residue {C108}
MODIFICATION: cysteine residue {C99}
EGF domain {111-148}
MOTIF: cysteine residue {C115}
MODIFICATION: cysteine residue {C125}
cysteine residue {C120}
MODIFICATION: cysteine residue {C136}
cysteine residue {C125}
MODIFICATION: cysteine residue {C115}
cysteine residue {C136}
MODIFICATION: cysteine residue {C120}
cysteine residue {C138}
MODIFICATION: cysteine residue {C147}
cysteine residue {C147}
MODIFICATION: cysteine residue {C138}
EGF domain {150-188}
MOTIF: cysteine residue {C154}
MODIFICATION: cysteine residue {C165}
cysteine residue {C159}
MODIFICATION: cysteine residue {C176}
cysteine residue {C165}
MODIFICATION: cysteine residue {C154}
proteolytic site {169-170}
proteolytic site {170-171}
cysteine residue {C176}
MODIFICATION: cysteine residue {C159}
cysteine residue {C178}
MODIFICATION: cysteine residue {C187}
cysteine residue {C187}
MODIFICATION: cysteine residue {C178}
Kringle {193-276}
MOTIF: cysteine residue {C194}
MODIFICATION: cysteine residue {C276}
N-glycosylation site {N207}
cysteine residue {C215}
MODIFICATION: cysteine residue {C257}
cysteine residue {C246}
MODIFICATION: cysteine residue {C271}
cysteine residue {C257}
MODIFICATION: cysteine residue {C215}
cysteine residue {C271}
MODIFICATION: cysteine residue {C246}
cysteine residue {C276}
MODIFICATION: cysteine residue {C194}
cysteine residue {C301}
MODIFICATION: cysteine residue {C-INTERCHAIN}
S1 domain {314-555}
MOTIF: cysteine residue {C347}
MODIFICATION: cysteine residue {C363}
histidine residue {H362}
cysteine residue {C363}
MODIFICATION: cysteine residue {C347}
aspartate residue {D411}
cysteine residue {C447}
MODIFICATION: cysteine residue {C515}
cysteine residue {C477}
MODIFICATION: cysteine residue {C493}
proteolytic site {480-481}
cysteine residue {C493}
MODIFICATION: cysteine residue {C477}
cysteine residue {C505}
MODIFICATION: cysteine residue {C533}
serine residue {S509}
cysteine residue {C515}
MODIFICATION: cysteine residue {C447}
cysteine residue {C533}
MODIFICATION: cysteine residue {C505}
Database Correlations
OMIM 603924
UniProt Q14520
PFAM correlations
References
UniProt :accession Q14520