Summary for peptidase S01.214: coagulation factor IXa

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors Pharma

 

Names
MEROPS Namecoagulation factor IXa
Other namesChristmas factor (activated), F9 g.p. (Homo sapiens) (activated)
Domain architecture
MEROPS Classification
Classification Clan PA >> Subclan PA(S) >> Family S1 >> Subfamily A >> S01.214
Holotypecoagulation factor IXa (Homo sapiens), Uniprot accession P00740 (peptidase unit: 227-461), MERNUM MER0000216
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeSerine
PeplistIncluded in the Peplist with identifier PL00308
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.22
EnzymologyBRENDA database
Proteolytic eventsCutDB database (3 cleavages)
Activity statushuman: active (Schmidt & Bajaj, 2004)
mouse: active (Kundu et al., 1998)
PhysiologyFormed from coagulation factor IX by the action of factor XIa or factor VIIa. Factor IXa then proteolytically activates coagulation factor X, and may act on factor VII also (Bajaj et al., 2004).
KnockoutHereditary deficiency is the cause of hemophila B, which is X-linked. A variety of different mutations are known (Giannelli et al., 1996). Knockout mice also have a severe bleeding disorder (Kundu et al., 1998).
Pharmaceutical relevanceA possible target for gene therapy of hemophilia B (Kundu et al., 1998). In a rat model of thromboembolic stroke, an inhibitory monoclonal antibody gave promising results, and within four hours of stroke produced a more favorable outcome than tissue-type plasminogen activator (Toomey et al., 2002). Administration of recombinant factor IX is reportedly a safe and effective treatment for hemophilia B (Shapiro et al., 2004).
Pathways KEGGComplement and coagulation cascades
Other databases WIKIPEDIAhttp://en.wikipedia.org/wiki/Coagulation_factor_Ixa
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/g/RScissile bond-/-/-/- (based on 12 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 0 6 0 0 0 3 3
Pro 2 0 1 0 0 0 0 0
Ala 0 0 0 0 0 0 0 0
Val 0 1 1 0 0 3 0 0
Leu 0 2 1 0 0 0 0 0
Ile 0 0 0 0 3 0 0 0
Met 0 0 0 0 1 0 0 0
Phe 0 0 0 0 0 0 0 0
Tyr 0 0 0 0 0 0 0 0
Trp 0 0 1 0 0 0 0 0
Ser 0 0 0 0 0 0 0 0
Thr 0 0 1 0 0 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 1 0 0 0 0 0 1 1
Gln 1 2 0 0 0 0 0 0
Asp 0 0 0 0 0 0 0 0
Glu 0 1 0 0 0 0 0 0
Lys 0 0 0 0 0 1 0 0
Arg 0 0 0 12 0 0 0 0
His 0 0 0 0 0 0 0 0
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
F9 Xq27.1-q27.2 ENSG00000101981 2158 F9 306900
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
F9 X:22.0 ENSMUSG00000031138 14071 MGI:88384