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Information on EC 3.4.21.B28 - fibroblast activation protein alpha subunit and Organism(s) Mus musculus and UniProt Accession P97321

for references in articles please use BRENDA:EC3.4.21.B28
preliminary BRENDA-supplied EC number
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This record set is specific for:
Mus musculus
UNIPROT: P97321
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Tetrapoda
Reaction Schemes
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fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Met-alpha2-antiplasmin is cleaved N-terminally at Pro3-Leu4 and Pro12-Asn13 into Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin
fibroblast activation protein requires substrates with Pro at P1 and Gly or D-amino acids at P2. Met-alpha2-antiplasmin is cleaved N-terminally at Pro3-Leu4 and Pro12-Asn13 into Asn-alpha2-antiplasmin that is rapidly cross-linked to fibrin and protects it from digestion by plasmin.
Synonyms
fap, fapalpha, fap-alpha, fibroblast activation protein-alpha, antiplasmin-cleaving enzyme, fibroblast activation factor, z-pro-prolinal-insensitive peptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FAP-specific protease
-
fibroblast activation protein alpha
member of the group type II integral serine proteases, subfamily S9b, with gelatinase and N-terminal post-prolyl amino peptidase activities
fibroblast activation protein-specific protease
-
surface expressed protease
-
FAPalpha
-
-
fibroblast activation protein
-
has also endopeptidase activity
fibroblast activation protein-alpha
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
352031-63-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Boc-Ala-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Boc-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
show the reaction diagram
-
-
-
-
?
acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
acetyl-Gly-Pro-Gly-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
show the reaction diagram
-
most efficient substrate, FAP shows a greater catalytic efficiency for acetyl-Gly-Pro-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate than for acetyl-Gly-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate and TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
-
-
?
Ala-Pro-Ala-Pro-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
Ala-Pro-Ala-Pro + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
complement C1q tumor necrosis factor-related protein 6 + H2O
?
show the reaction diagram
-
cleavage at position 26 after a Val-Pro sequence
-
-
?
CXCL-5 + H2O
?
show the reaction diagram
-
processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
-
-
?
extracellular matrix protein 1 + H2O
?
show the reaction diagram
-
cleavage occurrs at position 142 after a Lys-Pro sequence
-
-
?
extracellular matrix protein CN-I + H2O
?
show the reaction diagram
-
-
-
-
?
extracellular matrix protein CN-III + H2O
?
show the reaction diagram
-
-
-
-
?
extracellular matrix protein CN-V + H2O
?
show the reaction diagram
-
-
-
-
?
fibrillin-2 + H2O
?
show the reaction diagram
-
cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
-
-
?
lysyl oxidase homolog 2 + H2O
?
show the reaction diagram
-
cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
-
-
?
TSGP-9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate + H2O
TSGP + 9-di-3-sulfonylpropylaminobenzo[a]phenoxazonium perchlorate
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type V collagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
cleavage of type I collagen by fibroblast activation protein-? enhances class A scavenger receptor mediated macrophage adhesion
-
-
?
complement C1q tumor necrosis factor-related protein 6 + H2O
?
show the reaction diagram
-
cleavage at position 26 after a Val-Pro sequence
-
-
?
CXCL-5 + H2O
?
show the reaction diagram
-
processing of CXCL-5 at position 42, which is after an Ala-Pro sequence
-
-
?
extracellular matrix protein 1 + H2O
?
show the reaction diagram
-
cleavage occurrs at position 142 after a Lys-Pro sequence
-
-
?
extracellular matrix protein CN-I + H2O
?
show the reaction diagram
-
-
-
-
?
extracellular matrix protein CN-III + H2O
?
show the reaction diagram
-
-
-
-
?
extracellular matrix protein CN-V + H2O
?
show the reaction diagram
-
-
-
-
?
fibrillin-2 + H2O
?
show the reaction diagram
-
cleavage occurrs at position 60, in the propeptide domain, after a Gly-Pro sequence
-
-
?
lysyl oxidase homolog 2 + H2O
?
show the reaction diagram
-
cleavage at position 36 after a Tyr-Pro sequence that follows the signal peptide
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type V collagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyze the post-proline bond
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(2-aminoethyl)-benzenesulfonylfluoride
5 mM
4-amidino-phenylsulfonylfluoride
0.5 mM
diisopropylfluorophosphate
0.005 mM
N-ethylmaleimide
-
Phenylmethylsulfonylfluoride
1 mM
Talabostat
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
L-Ala-Pro-7-amido-4-trifluoromethylcoumarin
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lowenzyme activity
Manually annotated by BRENDA team
lowenzyme activity
Manually annotated by BRENDA team
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver
Manually annotated by BRENDA team
the protease fibroblast activation protein is a specific marker of activated mesenchymal cells in tumor stroma and fibrotic liver
Manually annotated by BRENDA team
high enzyme activity
Manually annotated by BRENDA team
lowenzyme activity
Manually annotated by BRENDA team
high enzyme activity
Manually annotated by BRENDA team
high enzyme activity
Manually annotated by BRENDA team
lowenzyme activity
Manually annotated by BRENDA team
high enzyme activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
transmembrane-anchored
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
plasma from FAP-deficient mice exhibits slower than wild-type clotting times
physiological function
-
the enzyme plays a role in mediating communication between activated fibroblasts and macrophages
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SEPR_MOUSE
761
1
87945
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S624A
-
FAP serine mutant lacking enzymatic activity, as wild type does not rescue dipeptidyl peptidase IV cell surface expression but is a more potent tumor suppressor than the wild type
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
S-200 gel filtration, hydroxylapatite column chromatography, Cibacron blue chromatography, and WGA-agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
-
subcloned into tetracyline-inducible vectors
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
tumor suppressor that abrogates tumorigenicity through regulation of cell growth and survival, in vitro, FAP expression restores contact inhibition, leads to cell cylcle arrest at G0/G1 phase, increases susceptibility to stress-induced apoptosis, and leads to caspase activation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramirez-Montagut, T.; Blachere, N.E.; Sviderskaya, E.V.; Bennett, D.C.; Rettig, W.J.; Garin-Chesa, P.; Houghton, A.N.
FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor
Oncogene
23
5435-5446
2004
Mus musculus, Mus musculus C57BL/6
Manually annotated by BRENDA team
O'Brien, P.; O'Connor, B.F.
Seprase: An overview of an important matrix serine protease
Biochim. Biophys. Acta
1784
1130-1145
2008
Bos taurus, Gallus gallus, Mus musculus (P97321), Homo sapiens (Q12884), Xenopus laevis (Q91651)
Manually annotated by BRENDA team
Lai, K.S.; Ho, N.; Cheng, J.D.; Tung, C.
Selective fluorescence probes for dipeptidyl peptidase activity-fibroblast activation protein and dipeptidyl peptidase IV
Bioconjug. Chem.
18
1246-1250
2007
Mus musculus
Manually annotated by BRENDA team
Keane, F.M.; Yao, T.W.; Seelk, S.; Gall, M.G.; Chowdhury, S.; Poplawski, S.E.; Lai, J.H.; Li, Y.; Wu, W.; Farrell, P.; Vieira de Ribeiro, A.J.; Osborne, B.; Yu, D.M.; Seth, D.; Rahman, K.; Haber, P.; Topaloglu, A.K.; Wang, C.; Thomson, S.; Hennessy, A.; Prins, J.; Twigg, S.M.; McLennan, S.V.; McCaughan, G.W.; Ba, B.a.c.
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs
FEBS open bio
4
43-54
2013
Papio sp., Mus musculus (P97321), Mus musculus, Homo sapiens (Q12844), Homo sapiens
Manually annotated by BRENDA team
Zhang, H.E.; Hamson, E.J.; Koczorowska, M.M.; Tholen, S.; Chowdhury, S.; Bailey, C.G.; Lay, A.J.; Twigg, S.M.; Lee, Q.; Roediger, B.; Biniossek, M.L.; ORourke, M.B.; McCaughan, G.W.; Keane, F.M.; Schilling, O.; Gorrell, M.D.
Identification of novel natural substrates of fibroblast activation protein-alpha by differential degradomics and proteomics
Mol. Cell. Proteomics
18
65-85
2019
Mus musculus
Manually annotated by BRENDA team
Mazur, A.; Holthoff, E.; Vadali, S.; Kelly, T.; Post, S.R.
Cleavage of type I collagen by fibroblast activation protein-alpha enhances class A scavenger receptor mediated macrophage adhesion
PLoS ONE
11
e0150287
2016
Mus musculus
Manually annotated by BRENDA team