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Prolyl endopeptidase FAP (EC 3.4.21.26) (170 kDa melanoma membrane-bound gelatinase) (Dipeptidyl peptidase FAP) (EC 3.4.14.5) (Fibroblast activation protein alpha) (FAPalpha) (Gelatine degradation protease FAP) (EC 3.4.21.-) (Integral membrane serine protease) (Post-proline cleaving enzyme) (Serine integral membrane protease) (SIMP) (Surface-expressed protease) (Seprase) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]

 SEPR_HUMAN              Reviewed;         760 AA.
Q12884; O00199; Q53TP5; Q86Z29; Q99998; Q9UID4;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 5.
25-OCT-2017, entry version 173.
RecName: Full=Prolyl endopeptidase FAP {ECO:0000305};
EC=3.4.21.26 {ECO:0000269|PubMed:16223769};
AltName: Full=170 kDa melanoma membrane-bound gelatinase {ECO:0000303|PubMed:2172980, ECO:0000303|PubMed:9065413};
AltName: Full=Dipeptidyl peptidase FAP {ECO:0000305};
EC=3.4.14.5 {ECO:0000269|PubMed:10347120};
AltName: Full=Fibroblast activation protein alpha {ECO:0000303|PubMed:7911242};
Short=FAPalpha {ECO:0000250|UniProtKB:P97321};
AltName: Full=Gelatine degradation protease FAP {ECO:0000305};
EC=3.4.21.- {ECO:0000269|PubMed:9065413};
AltName: Full=Integral membrane serine protease {ECO:0000303|PubMed:9247085};
AltName: Full=Post-proline cleaving enzyme {ECO:0000305};
AltName: Full=Serine integral membrane protease {ECO:0000303|PubMed:9247085};
Short=SIMP {ECO:0000303|PubMed:9247085};
AltName: Full=Surface-expressed protease {ECO:0000303|PubMed:2172980};
Short=Seprase {ECO:0000303|PubMed:7923219};
Contains:
RecName: Full=Antiplasmin-cleaving enzyme FAP, soluble form {ECO:0000303|PubMed:14751930};
Short=APCE {ECO:0000303|PubMed:14751930};
EC=3.4.14.5 {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769};
EC=3.4.21.- {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769};
EC=3.4.21.26 {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769};
Name=FAP {ECO:0000312|HGNC:HGNC:3590};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Fibroblast;
PubMed=7911242; DOI=10.1073/pnas.91.12.5657;
Scanlan M.J., Raj B.K.M., Calvo B., Garin-Chesa P., Sanz-Moncasi M.P.,
Healey J.H., Old L.J., Rettig W.J.;
"Molecular cloning of fibroblast activation protein alpha, a member of
the serine protease family selectively expressed in stromal
fibroblasts of epithelial cancers.";
Proc. Natl. Acad. Sci. U.S.A. 91:5657-5661(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Melanoma;
PubMed=9247085; DOI=10.1016/S0925-4439(97)00032-X;
Goldstein L.A., Ghersi G., Pineiro-Sanchez M.L., Salamone M., Yeh Y.,
Flessate D., Chen W.-T.;
"Molecular cloning of seprase: a serine integral membrane protease
from human melanoma.";
Biochim. Biophys. Acta 1361:11-19(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 220-229;
461-472 AND 511-518, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR
LOCATION.
TISSUE=Melanoma;
PubMed=9065413; DOI=10.1074/jbc.272.12.7595;
Pineiro-Sanchez M.L., Goldstein L.A., Dodt J., Howard L., Yeh Y.,
Chen W.-T.;
"Identification of the 170-kDa melanoma membrane-bound gelatinase
(seprase) as a serine integral membrane protease.";
J. Biol. Chem. 272:7595-7601(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Melanoma;
PubMed=10644713; DOI=10.1074/jbc.275.4.2554;
Goldstein L.A., Chen W.-T.;
"Identification of an alternatively spliced seprase mRNA that encodes
a novel intracellular isoform.";
J. Biol. Chem. 275:2554-2559(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 24-38; 210-219; 247-254; 487-499; 500-509 AND
522-530, FUNCTION (SOLUBLE FORM), CATALYTIC ACTIVITY, AND SUBCELLULAR
LOCATION.
PubMed=14751930; DOI=10.1182/blood-2003-12-4240;
Lee K.N., Jackson K.W., Christiansen V.J., Chung K.H., McKee P.A.;
"A novel plasma proteinase potentiates alpha2-antiplasmin inhibition
of fibrin digestion.";
Blood 103:3783-3788(2004).
[9]
PROTEIN SEQUENCE OF 192-208; 220-240 AND 510-521, AND INDUCTION.
PubMed=7519584; DOI=10.1002/ijc.2910580314;
Rettig W.J., Su S.L., Fortunato S.R., Scanlan M.J., Raj B.K.M.,
Garin-Chesa P., Healey J.H., Old L.J.;
"Fibroblast activation protein: purification, epitope mapping and
induction by growth factors.";
Int. J. Cancer 58:385-392(1994).
[10]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2172980; DOI=10.1073/pnas.87.21.8296;
Aoyama A., Chen W.T.;
"A 170-kDa membrane-bound protease is associated with the expression
of invasiveness by human malignant melanoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:8296-8300(1990).
[11]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=7923219;
Monsky W.L., Lin C.Y., Aoyama A., Kelly T., Akiyama S.K.,
Mueller S.C., Chen W.T.;
"A potential marker protease of invasiveness, seprase, is localized on
invadopodia of human malignant melanoma cells.";
Cancer Res. 54:5702-5710(1994).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=10347120; DOI=10.1002/hep.510290631;
Levy M.T., McCaughan G.W., Abbott C.A., Park J.E., Cunningham A.M.,
Mueller E., Rettig W.J., Gorrell M.D.;
"Fibroblast activation protein: a cell surface dipeptidyl peptidase
and gelatinase expressed by stellate cells at the tissue remodelling
interface in human cirrhosis.";
Hepatology 29:1768-1778(1999).
[13]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS
OF SER-624.
PubMed=10593948; DOI=10.1074/jbc.274.51.36505;
Park J.E., Lenter M.C., Zimmermann R.N., Garin-Chesa P., Old L.J.,
Rettig W.J.;
"Fibroblast activation protein, a dual specificity serine protease
expressed in reactive human tumor stromal fibroblasts.";
J. Biol. Chem. 274:36505-36512(1999).
[14]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH ITGA3 AND
ITGB1, ASSOCIATION WITH INTEGRIN ALPHA-3/BETA-1, AND SUBCELLULAR
LOCATION.
PubMed=10455171; DOI=10.1074/jbc.274.35.24947;
Mueller S.C., Ghersi G., Akiyama S.K., Sang Q.X., Howard L.,
Pineiro-Sanchez M., Nakahara H., Yeh Y., Chen W.T.;
"A novel protease-docking function of integrin at invadopodia.";
J. Biol. Chem. 274:24947-24952(1999).
[15]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PLAUR, AND SUBCELLULAR
LOCATION.
PubMed=12376466; DOI=10.1093/carcin/23.10.1593;
Artym V.V., Kindzelskii A.L., Chen W.T., Petty H.R.;
"Molecular proximity of seprase and the urokinase-type plasminogen
activator receptor on malignant melanoma cell membranes: dependence on
beta1 integrins and the cytoskeleton.";
Carcinogenesis 23:1593-1601(2002).
[16]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF GLU-203; GLU-204 AND SER-624.
PubMed=16175601; DOI=10.1002/hep.20853;
Wang X.M., Yu D.M., McCaughan G.W., Gorrell M.D.;
"Fibroblast activation protein increases apoptosis, cell adhesion, and
migration by the LX-2 human stellate cell line.";
Hepatology 42:935-945(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99 AND ASN-227.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17105646; DOI=10.1186/ar2080;
Bauer S., Jendro M.C., Wadle A., Kleber S., Stenner F., Dinser R.,
Reich A., Faccin E., Goedde S., Dinges H., Mueller-Ladner U.,
Renner C.;
"Fibroblast activation protein is expressed by rheumatoid
myofibroblast-like synoviocytes.";
Arthritis Res. Ther. 8:R171-R171(2006).
[19]
FUNCTION (PLASMA MEMBRANE AND SOLUBLE FORMS), CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16223769; DOI=10.1182/blood-2005-08-3452;
Lee K.N., Jackson K.W., Christiansen V.J., Lee C.S., Chun J.G.,
McKee P.A.;
"Antiplasmin-cleaving enzyme is a soluble form of fibroblast
activation protein.";
Blood 107:1397-1404(2006).
[20]
FUNCTION, CATALYTIC ACTIVITY, HETERODIMERIZATION WITH DPP4, AND
SUBCELLULAR LOCATION.
PubMed=16651416; DOI=10.1158/0008-5472.CAN-05-1245;
Ghersi G., Zhao Q., Salamone M., Yeh Y., Zucker S., Chen W.T.;
"The protease complex consisting of dipeptidyl peptidase IV and
seprase plays a role in the migration and invasion of human
endothelial cells in collagenous matrices.";
Cancer Res. 66:4652-4661(2006).
[21]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
ENZYME REGULATION.
PubMed=16480718; DOI=10.1016/j.febslet.2006.01.087;
Edosada C.Y., Quan C., Tran T., Pham V., Wiesmann C., Fairbrother W.,
Wolf B.B.;
"Peptide substrate profiling defines fibroblast activation protein as
an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity.";
FEBS Lett. 580:1581-1586(2006).
[22]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, AND SUBUNIT.
PubMed=16410248; DOI=10.1074/jbc.M511112200;
Edosada C.Y., Quan C., Wiesmann C., Tran T., Sutherlin D.,
Reynolds M., Elliott J.M., Raab H., Fairbrother W., Wolf B.B.;
"Selective inhibition of fibroblast activation protein protease based
on dipeptide substrate specificity.";
J. Biol. Chem. 281:7437-7444(2006).
[23]
FUNCTION, MUTAGENESIS OF ARG-123; GLU-203; TYR-656; ALA-657 AND
ASN-704, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME
REGULATION.
PubMed=17381073; DOI=10.1021/bi062227y;
Meadows S.A., Edosada C.Y., Mayeda M., Tran T., Quan C., Raab H.,
Wiesmann C., Wolf B.B.;
"Ala657 and conserved active site residues promote fibroblast
activation protein endopeptidase activity via distinct mechanisms of
transition state stabilization.";
Biochemistry 46:4598-4605(2007).
[24]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18095711; DOI=10.1021/bi701921b;
Aggarwal S., Brennen W.N., Kole T.P., Schneider E., Topaloglu O.,
Yates M., Cotter R.J., Denmeade S.R.;
"Fibroblast activation protein peptide substrates identified from
human collagen I derived gelatin cleavage sites.";
Biochemistry 47:1076-1086(2008).
[25]
REVIEW, AND FUNCTION.
PubMed=18262497; DOI=10.1016/j.bbapap.2008.01.006;
O'Brien P., O'Connor B.F.;
"Seprase: an overview of an important matrix serine protease.";
Biochim. Biophys. Acta 1784:1130-1145(2008).
[26]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=20707604; DOI=10.1515/BC.2010.119;
Mentlein R., Hattermann K., Hemion C., Jungbluth A.A., Held-Feindt J.;
"Expression and role of the cell surface protease seprase/fibroblast
activation protein-alpha (FAP-alpha) in astroglial tumors.";
Biol. Chem. 392:199-207(2011).
[27]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21314817; DOI=10.1111/j.1742-4658.2011.08051.x;
Keane F.M., Nadvi N.A., Yao T.W., Gorrell M.D.;
"Neuropeptide Y, B-type natriuretic peptide, substance P and peptide
YY are novel substrates of fibroblast activation protein-alpha.";
FEBS J. 278:1316-1332(2011).
[28]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21288888; DOI=10.1093/jb/mvr017;
Huang C.H., Suen C.S., Lin C.T., Chien C.H., Lee H.Y., Chung K.M.,
Tsai T.Y., Jiaang W.T., Hwang M.J., Chen X.;
"Cleavage-site specificity of prolyl endopeptidase FAP investigated
with a full-length protein substrate.";
J. Biochem. 149:685-692(2011).
[29]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND CHARACTERIZATION OF VARIANT LEU-363.
PubMed=24371721; DOI=10.1016/j.fob.2013.12.001;
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., Bachovchin W.W.,
Gorrell M.D.;
"Quantitation of fibroblast activation protein (FAP)-specific protease
activity in mouse, baboon and human fluids and organs.";
FEBS Open Bio 4:43-54(2013).
[30]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT LEU-363.
PubMed=24717288; DOI=10.1016/j.bbapap.2014.03.015;
Osborne B., Yao T.W., Wang X.M., Chen Y., Kotan L.D., Nadvi N.A.,
Herdem M., McCaughan G.W., Allen J.D., Yu D.M., Topaloglu A.K.,
Gorrell M.D.;
"A rare variant in human fibroblast activation protein associated with
ER stress, loss of enzymatic function and loss of cell surface
localisation.";
Biochim. Biophys. Acta 1844:1248-1259(2014).
[31]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 39-757, SUBSTRATE BINDING,
SUBUNIT, DISULFIDE BONDS, ACTIVE SITE, AND GLYCOSYLATION AT ASN-49;
ASN-92; ASN-227 AND ASN-314.
PubMed=15809306; DOI=10.1074/jbc.C500092200;
Aertgeerts K., Levin I., Shi L., Snell G.P., Jennings A., Prasad G.S.,
Zhang Y., Kraus M.L., Salakian S., Sridhar V., Wijnands R.,
Tennant M.G.;
"Structural and kinetic analysis of the substrate specificity of human
fibroblast activation protein alpha.";
J. Biol. Chem. 280:19441-19444(2005).
-!- FUNCTION: Cell surface glycoprotein serine protease that
participates in extracellular matrix degradation and involved in
many cellular processes including tissue remodeling, fibrosis,
wound healing, inflammation and tumor growth. Both plasma membrane
and soluble forms exhibit post-proline cleaving endopeptidase
activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala
consensus sequences, on substrate such as alpha-2-antiplasmin
SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769,
PubMed:16480718, PubMed:16410248, PubMed:17381073,
PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also
gelatin, heat-denatured type I collagen, but not native collagen
type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin
or casein (PubMed:9065413, PubMed:2172980, PubMed:7923219,
PubMed:10347120, PubMed:10455171, PubMed:12376466,
PubMed:16223769, PubMed:16651416, PubMed:18095711). Have also
dipeptidyl peptidase activity, exhibiting the ability to hydrolyze
the prolyl bond two residues from the N-terminus of synthetic
dipeptide substrates provided that the penultimate residue is
proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro
and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601,
PubMed:16223769, PubMed:16651416, PubMed:16410248,
PubMed:17381073, PubMed:21314817, PubMed:24371721,
PubMed:24717288). Natural neuropeptide hormones for dipeptidyl
peptidase are the neuropeptide Y (NPY), peptide YY (PYY),
substance P (TAC1) and brain natriuretic peptide 32 (NPPB)
(PubMed:21314817). The plasma membrane form, in association with
either DPP4, PLAUR or integrins, is involved in the pericellular
proteolysis of the extracellular matrix (ECM), and hence promotes
cell adhesion, migration and invasion through the ECM. Plays a
role in tissue remodeling during development and wound healing.
Participates in the cell invasiveness towards the ECM in malignant
melanoma cancers. Enhances tumor growth progression by increasing
angiogenesis, collagen fiber degradation and apoptosis and by
reducing antitumor response of the immune system. Promotes glioma
cell invasion through the brain parenchyma by degrading the
proteoglycan brevican. Acts as a tumor suppressor in melanocytic
cells through regulation of cell proliferation and survival in a
serine protease activity-independent manner.
{ECO:0000250|UniProtKB:P97321, ECO:0000269|PubMed:10347120,
ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:10593948,
ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:14751930,
ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:16223769,
ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718,
ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646,
ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711,
ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:21288888,
ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:2172980,
ECO:0000269|PubMed:24371721, ECO:0000269|PubMed:24717288,
ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413}.
-!- CATALYTIC ACTIVITY: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in
oligopeptides. {ECO:0000269|PubMed:14751930,
ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248,
ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:18095711,
ECO:0000269|PubMed:21288888, ECO:0000269|PubMed:24371721}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
Zaa is neither Pro nor hydroxyproline. {ECO:0000255|PROSITE-
ProRule:PRU10084, ECO:0000269|PubMed:10347120,
ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601,
ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:16410248,
ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17381073,
ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:24371721,
ECO:0000269|PubMed:24717288}.
-!- ENZYME REGULATION: Gelatinase activity is inhibited by serine-
protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF),
4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF),
4-amidino phenylsulfonyl fluoride (APSF) and diisopropyl
fluorophosphate (DFP), N-ethylmaleimide (NEM) and
phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase
activity is inhibited by 2,2'-azino-bis(3-ethylbenzthiazoline-6-
sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl
endopeptidase activity is inhibited by the boronic acid peptide
Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-
chloromethyl ketone. {ECO:0000269|PubMed:10593948,
ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16480718,
ECO:0000269|PubMed:17381073, ECO:0000269|PubMed:2172980,
ECO:0000269|PubMed:9065413}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.46 mM for Ala-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:10593948};
KM=0.9 mM for Lys-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:10593948};
KM=1.15 mM for Gly-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:10593948};
KM=0.25 mM for Gly-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:17381073};
KM=0.24 mM for Ala-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:16410248};
KM=0.10 mM for Ile-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:16410248};
KM=0.24 mM for Phe-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:16410248};
KM=0.24 mM for Gly-Pro (Dipeptidyl peptidase activity)
{ECO:0000269|PubMed:16410248};
KM=0.33 mM for Ac-Gly-Pro (Prolyl endopeptidase activity)
{ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:17381073};
KM=1.3 uM for Thr-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=2.2 uM for Ala-Ser-Gly-Pro-Asn-Gln (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=0.7 uM for Thr-Ala-Gly-Pro-Asn-Gln (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=1.9 uM for Thr-Ser-Gly-Pro-Ser-Gln (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=2.2 uM for Thr-Ser-Gly-Pro-Asn-Ser (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=4.3 uM for Ala-Ser-Gly-Pro-Ser-Ser (Prolyl endopeptidase
activity) {ECO:0000269|PubMed:16480718};
KM=0.101 mM for Gly-Pro (FAP form, prolyl endopeptidase
activity) {ECO:0000269|PubMed:16223769};
KM=0.124 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble
form, prolyl endopeptidase activity)
{ECO:0000269|PubMed:16223769};
KM=0.323 mM for Gly-Pro (FAP form, dipeptidyl peptidase
activity) {ECO:0000269|PubMed:16223769};
KM=0.272 mM for Gly-Pro (Antiplasmin-cleaving enzyme FAP soluble
form, dipeptidyl peptidase activity)
{ECO:0000269|PubMed:16223769};
KM=0.029 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu (FAP
form, prolyl endopeptidase activity)
{ECO:0000269|PubMed:16223769};
KM=0.026 mM for Arg-Gly-Thr-Ser-Gly-Pro-Asn-Gln-Glu-Gln-Glu
(Antiplasmin-cleaving enzyme FAP soluble form, prolyl
endopeptidase activity) {ECO:0000269|PubMed:16223769};
pH dependence:
Optimum pH is 6-8.4 for gelatinase activity. At pH lower than 5
inhibited gelatinase activity. {ECO:0000269|PubMed:2172980,
ECO:0000269|PubMed:9065413};
Temperature dependence:
Optimum temperature is 37 degrees Celsius for gelatinase
activity. Temperatures above 50 degrees Celsius inhibit
gelatinase activity. {ECO:0000269|PubMed:2172980,
ECO:0000269|PubMed:9065413};
-!- SUBUNIT: Homodimer; homodimerization is required for activity of
both plasma membrane and soluble forms. The monomer is inactive.
Heterodimer with DPP4. Interacts with PLAUR; the interaction
occurs at the cell surface of invadopodia membranes. Interacts
with ITGB1. Interacts with ITGA3. Associates with integrin alpha-
3/beta-1; the association occurs in a collagen-dependent manner at
the cell surface of invadopodia membranes.
{ECO:0000269|PubMed:10455171, ECO:0000269|PubMed:12376466,
ECO:0000269|PubMed:15809306, ECO:0000269|PubMed:16223769,
ECO:0000269|PubMed:16410248, ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:9065413}.
-!- INTERACTION:
P01275:GCG; NbExp=4; IntAct=EBI-4319803, EBI-7629173;
P01282:VIP; NbExp=2; IntAct=EBI-4319803, EBI-751454;
-!- SUBCELLULAR LOCATION: Prolyl endopeptidase FAP: Cell surface
{ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:16175601,
ECO:0000269|PubMed:17105646, ECO:0000269|PubMed:24717288,
ECO:0000269|PubMed:7911242}. Cell membrane
{ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}; Single-
pass type II membrane protein {ECO:0000255}. Cell projection,
lamellipodium membrane {ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:9065413}; Single-pass type II membrane protein
{ECO:0000255}. Cell projection, invadopodium membrane
{ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16651416,
ECO:0000269|PubMed:7923219, ECO:0000269|PubMed:9065413,
ECO:0000303|PubMed:10455171}; Single-pass type II membrane protein
{ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000303|PubMed:10455171}; Single-pass type II membrane
protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:2172980};
Single-pass type II membrane protein {ECO:0000255}. Note=Localized
on cell surface with lamellipodia and invadopodia membranes and on
shed vesicles. Colocalized with DPP4 at invadopodia and
lamellipodia membranes of migratory activated endothelial cells in
collagenous matrix. Colocalized with DPP4 on endothelial cells of
capillary-like microvessels but not large vessels within invasive
breast ductal carcinoma. Anchored and enriched preferentially by
integrin alpha-3/beta-1 at invadopodia, plasma membrane
protrusions that correspond to sites of cell invasion, in a
collagen-dependent manner. Localized at plasma and ruffle
membranes in a collagen-independent manner. Colocalized with PLAUR
preferentially at the cell surface of invadopodia membranes in a
cytoskeleton-, integrin- and vitronectin-dependent manner.
Concentrated at invadopodia membranes, specialized protrusions of
the ventral plasma membrane in a fibrobectin-dependent manner.
Colocalizes with extracellular components (ECM), such as collagen
fibers and fibronectin. {ECO:0000269|PubMed:10593948,
ECO:0000269|PubMed:12376466, ECO:0000269|PubMed:16175601,
ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17105646,
ECO:0000269|PubMed:2172980, ECO:0000269|PubMed:24717288,
ECO:0000269|PubMed:7911242, ECO:0000269|PubMed:7923219,
ECO:0000269|PubMed:9065413, ECO:0000303|PubMed:10455171}.
-!- SUBCELLULAR LOCATION: Antiplasmin-cleaving enzyme FAP, soluble
form: Secreted {ECO:0000269|PubMed:14751930,
ECO:0000269|PubMed:16223769, ECO:0000269|PubMed:24371721}.
Note=Found in blood plasma and serum.
{ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769,
ECO:0000269|PubMed:24371721}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000303|PubMed:10644713}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=L, seprase-I {ECO:0000303|PubMed:10644713};
IsoId=Q12884-1; Sequence=Displayed;
Note=Major isoform.;
Name=2 {ECO:0000269|PubMed:10644713}; Synonyms=S, Truncated,
seprase-s {ECO:0000303|PubMed:10644713};
IsoId=Q12884-2; Sequence=VSP_005367;
Note=Upstream open reading frames ORF(s)-containing region
inhibits the translation of its downstream ORF.
{ECO:0000269|PubMed:10644713};
-!- TISSUE SPECIFICITY: Expressed in adipose tissue. Expressed in the
dermal fibroblasts in the fetal skin. Expressed in the granulation
tissue of healing wounds and on reactive stromal fibroblast in
epithelial cancers. Expressed in activated fibroblast-like
synoviocytes from inflamed synovial tissues. Expressed in
activated hepatic stellate cells (HSC) and myofibroblasts from
cirrhotic liver, but not detected in normal liver. Expressed in
glioma cells (at protein level). Expressed in glioblastomas and
glioma cells. Isoform 1 and isoform 2 are expressed in melanoma,
carcinoma and fibroblast cell lines. {ECO:0000269|PubMed:10347120,
ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10644713,
ECO:0000269|PubMed:16175601, ECO:0000269|PubMed:17105646,
ECO:0000269|PubMed:20707604, ECO:0000269|PubMed:24371721,
ECO:0000269|PubMed:7911242}.
-!- INDUCTION: In fibroblasts at times and sites of tissue remodeling
during development, tissue repair and carcinogenesis. Up-regulated
upon tumor stem cell differentiation. Up-regulated by transforming
growth factor-beta, 12-O-tetradecanoyl phorbol-13-acetate and
retinoids. {ECO:0000269|PubMed:20707604,
ECO:0000269|PubMed:7519584}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15809306,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7911242,
ECO:0000269|PubMed:9065413}.
-!- PTM: The N-terminus may be blocked.
-!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U09278; AAB49652.1; -; mRNA.
EMBL; U76833; AAC51668.1; -; mRNA.
EMBL; AF007822; AAF21600.1; -; mRNA.
EMBL; AC007750; AAY24205.1; -; Genomic_DNA.
EMBL; CH471058; EAX11353.1; -; Genomic_DNA.
EMBL; BC026250; AAH26250.1; -; mRNA.
CCDS; CCDS33311.1; -. [Q12884-1]
RefSeq; NP_001278736.1; NM_001291807.2.
RefSeq; NP_004451.2; NM_004460.4. [Q12884-1]
UniGene; Hs.654370; -.
PDB; 1Z68; X-ray; 2.60 A; A/B=39-757.
PDBsum; 1Z68; -.
ProteinModelPortal; Q12884; -.
SMR; Q12884; -.
BioGrid; 108485; 16.
IntAct; Q12884; 10.
MINT; MINT-4778828; -.
STRING; 9606.ENSP00000188790; -.
BindingDB; Q12884; -.
ChEMBL; CHEMBL4683; -.
GuidetoPHARMACOLOGY; 2365; -.
ESTHER; human-FAP; DPP4N_Peptidase_S9.
MEROPS; S09.007; -.
iPTMnet; Q12884; -.
PhosphoSitePlus; Q12884; -.
SwissPalm; Q12884; -.
BioMuta; FAP; -.
DMDM; 292495099; -.
PaxDb; Q12884; -.
PeptideAtlas; Q12884; -.
PRIDE; Q12884; -.
Ensembl; ENST00000188790; ENSP00000188790; ENSG00000078098. [Q12884-1]
GeneID; 2191; -.
KEGG; hsa:2191; -.
UCSC; uc002ucd.3; human. [Q12884-1]
CTD; 2191; -.
DisGeNET; 2191; -.
EuPathDB; HostDB:ENSG00000078098.13; -.
GeneCards; FAP; -.
H-InvDB; HIX0002548; -.
HGNC; HGNC:3590; FAP.
HPA; HPA059739; -.
MIM; 600403; gene.
neXtProt; NX_Q12884; -.
OpenTargets; ENSG00000078098; -.
PharmGKB; PA28003; -.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00760000119233; -.
HOGENOM; HOG000231875; -.
HOVERGEN; HBG005527; -.
InParanoid; Q12884; -.
KO; K08674; -.
OMA; NEFEGYP; -.
OrthoDB; EOG091G0BU5; -.
PhylomeDB; Q12884; -.
TreeFam; TF313309; -.
BRENDA; 3.4.21.B28; 2681.
SABIO-RK; Q12884; -.
SIGNOR; Q12884; -.
ChiTaRS; FAP; human.
EvolutionaryTrace; Q12884; -.
GeneWiki; Fibroblast_activation_protein,_alpha; -.
GenomeRNAi; 2191; -.
PRO; PR:Q12884; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000078098; -.
CleanEx; HS_FAP; -.
ExpressionAtlas; Q12884; baseline and differential.
Genevisible; Q12884; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0071438; C:invadopodium membrane; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; NAS:UniProtKB.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; IDA:UniProtKB.
GO; GO:1902362; P:melanocyte apoptotic process; ISS:UniProtKB.
GO; GO:0097325; P:melanocyte proliferation; ISS:UniProtKB.
GO; GO:0071850; P:mitotic cell cycle arrest; ISS:UniProtKB.
GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; ISS:UniProtKB.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IDA:UniProtKB.
GO; GO:1903054; P:negative regulation of extracellular matrix organization; IDA:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0010710; P:regulation of collagen catabolic process; IDA:UniProtKB.
GO; GO:0051917; P:regulation of fibrinolysis; IC:BHF-UCL.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR031245; FAP/Dpf2.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
InterPro; IPR002469; Peptidase_S9B_N.
PANTHER; PTHR11731:SF136; PTHR11731:SF136; 1.
Pfam; PF00930; DPPIV_N; 1.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Apoptosis;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Cleavage on pair of basic residues; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Polymorphism; Protease; Reference proteome; Secreted;
Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 760 Prolyl endopeptidase FAP. {ECO:0000305}.
/FTId=PRO_0000122424.
CHAIN 24 760 Antiplasmin-cleaving enzyme FAP, soluble
form. {ECO:0000303|PubMed:14751930}.
/FTId=PRO_0000430643.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255,
ECO:0000303|PubMed:14751930}.
TRANSMEM 5 25 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 26 760 Extracellular. {ECO:0000255,
ECO:0000303|PubMed:14751930}.
ACT_SITE 624 624 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:15809306}.
ACT_SITE 702 702 Charge relay system.
{ECO:0000269|PubMed:15809306}.
ACT_SITE 734 734 Charge relay system.
{ECO:0000269|PubMed:15809306}.
BINDING 203 203 Substrate. {ECO:0000303|PubMed:15809306}.
BINDING 204 204 Substrate. {ECO:0000303|PubMed:15809306}.
SITE 23 24 Cleavage. {ECO:0000303|PubMed:14751930}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:15809306}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:15809306}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:16335952}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:15809306,
ECO:0000269|PubMed:16335952}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498,
ECO:0000269|PubMed:15809306}.
CARBOHYD 679 679 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 321 332 {ECO:0000269|PubMed:15809306}.
DISULFID 438 441 {ECO:0000269|PubMed:15809306}.
DISULFID 448 466 {ECO:0000269|PubMed:15809306}.
DISULFID 643 755 {ECO:0000269|PubMed:15809306}.
VAR_SEQ 1 521 Missing (in isoform 2).
{ECO:0000303|PubMed:10644713}.
/FTId=VSP_005367.
VARIANT 363 363 S -> L (decreased plasma membrane
expression; loss of homodimerization and
dipeptidyl peptidase activity;
mislocalized with the calnexin in the
endoplasmic reticulum; causes induction
of the unfolded protein response (UPR);
dbSNP:rs762738740).
{ECO:0000269|PubMed:24371721,
ECO:0000269|PubMed:24717288}.
/FTId=VAR_071264.
MUTAGEN 123 123 R->A,M,E: Reduces dipeptidyl peptidase
and endopeptidase activities.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 203 203 E->A,D,Q: Reduces dipeptidyl peptidase
and endopeptidase activities. Does not
inhibit cell adhesion, migration and
invasion. Inhibits dipeptidyl peptidase
and endopeptidase activities; when
associated with A-204.
{ECO:0000269|PubMed:16175601,
ECO:0000269|PubMed:17381073}.
MUTAGEN 204 204 E->A,D,Q: Reduces dipeptidyl peptidase
and endopeptidase activities. Does not
inhibit cell adhesion, migration and
invasion. Inhibits dipeptidyl peptidase
and endopeptidase activities; when
associated with A-203.
{ECO:0000269|PubMed:16175601,
ECO:0000269|PubMed:17381073}.
MUTAGEN 624 624 S->A: Reduces dipeptidyl peptidase and
gelatinolytic activities. Does not
inhibit cell adhesion, migration and
invasion. {ECO:0000269|PubMed:10593948,
ECO:0000269|PubMed:16175601}.
MUTAGEN 656 656 Y->F: Reduces dipeptidyl peptidase and
endopeptidase activities.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 657 657 A->D,N: Inhibits endopeptidase activity.
Increases dipeptidyl peptidase activity.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 657 657 A->F,V: Reduces dipeptidyl peptidase and
endopeptidase activities.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 657 657 A->Q: Inhibits endopeptidase activity. No
change in dipeptidyl peptidase activity.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 657 657 A->S,T: Reduces strongly endopeptidase
activity. No change in dipeptidyl
peptidase activity.
{ECO:0000269|PubMed:17381073}.
MUTAGEN 704 704 N->A: Reduces dipeptidyl peptidase and
endopeptidase activities.
{ECO:0000269|PubMed:17381073}.
CONFLICT 207 207 A -> P (in Ref. 1; AAB49652).
{ECO:0000305}.
CONFLICT 229 229 T -> K (in Ref. 1; AAB49652).
{ECO:0000305}.
CONFLICT 354 354 T -> R (in Ref. 1; AAB49652).
{ECO:0000305}.
HELIX 44 49 {ECO:0000244|PDB:1Z68}.
TURN 50 52 {ECO:0000244|PDB:1Z68}.
STRAND 60 70 {ECO:0000244|PDB:1Z68}.
STRAND 76 83 {ECO:0000244|PDB:1Z68}.
STRAND 86 90 {ECO:0000244|PDB:1Z68}.
HELIX 92 96 {ECO:0000244|PDB:1Z68}.
TURN 97 99 {ECO:0000244|PDB:1Z68}.
STRAND 101 105 {ECO:0000244|PDB:1Z68}.
STRAND 109 120 {ECO:0000244|PDB:1Z68}.
STRAND 122 124 {ECO:0000244|PDB:1Z68}.
STRAND 126 134 {ECO:0000244|PDB:1Z68}.
TURN 135 138 {ECO:0000244|PDB:1Z68}.
STRAND 148 150 {ECO:0000244|PDB:1Z68}.
STRAND 153 155 {ECO:0000244|PDB:1Z68}.
STRAND 162 166 {ECO:0000244|PDB:1Z68}.
STRAND 169 175 {ECO:0000244|PDB:1Z68}.
TURN 189 191 {ECO:0000244|PDB:1Z68}.
STRAND 192 196 {ECO:0000244|PDB:1Z68}.
HELIX 199 204 {ECO:0000244|PDB:1Z68}.
STRAND 212 214 {ECO:0000244|PDB:1Z68}.
STRAND 218 227 {ECO:0000244|PDB:1Z68}.
STRAND 233 238 {ECO:0000244|PDB:1Z68}.
STRAND 241 244 {ECO:0000244|PDB:1Z68}.
STRAND 246 251 {ECO:0000244|PDB:1Z68}.
STRAND 261 270 {ECO:0000244|PDB:1Z68}.
HELIX 272 275 {ECO:0000244|PDB:1Z68}.
HELIX 284 287 {ECO:0000244|PDB:1Z68}.
STRAND 291 312 {ECO:0000244|PDB:1Z68}.
STRAND 315 323 {ECO:0000244|PDB:1Z68}.
STRAND 325 331 {ECO:0000244|PDB:1Z68}.
HELIX 334 336 {ECO:0000244|PDB:1Z68}.
STRAND 337 341 {ECO:0000244|PDB:1Z68}.
STRAND 343 345 {ECO:0000244|PDB:1Z68}.
STRAND 347 351 {ECO:0000244|PDB:1Z68}.
STRAND 364 369 {ECO:0000244|PDB:1Z68}.
STRAND 375 382 {ECO:0000244|PDB:1Z68}.
STRAND 393 395 {ECO:0000244|PDB:1Z68}.
STRAND 397 403 {ECO:0000244|PDB:1Z68}.
STRAND 405 413 {ECO:0000244|PDB:1Z68}.
HELIX 415 417 {ECO:0000244|PDB:1Z68}.
STRAND 422 428 {ECO:0000244|PDB:1Z68}.
STRAND 430 433 {ECO:0000244|PDB:1Z68}.
STRAND 436 440 {ECO:0000244|PDB:1Z68}.
TURN 441 447 {ECO:0000244|PDB:1Z68}.
STRAND 450 455 {ECO:0000244|PDB:1Z68}.
HELIX 457 459 {ECO:0000244|PDB:1Z68}.
STRAND 460 466 {ECO:0000244|PDB:1Z68}.
STRAND 469 471 {ECO:0000244|PDB:1Z68}.
STRAND 473 477 {ECO:0000244|PDB:1Z68}.
STRAND 479 481 {ECO:0000244|PDB:1Z68}.
STRAND 484 489 {ECO:0000244|PDB:1Z68}.
HELIX 492 497 {ECO:0000244|PDB:1Z68}.
STRAND 505 513 {ECO:0000244|PDB:1Z68}.
STRAND 516 524 {ECO:0000244|PDB:1Z68}.
STRAND 530 532 {ECO:0000244|PDB:1Z68}.
STRAND 534 540 {ECO:0000244|PDB:1Z68}.
HELIX 557 563 {ECO:0000244|PDB:1Z68}.
STRAND 568 573 {ECO:0000244|PDB:1Z68}.
STRAND 577 580 {ECO:0000244|PDB:1Z68}.
HELIX 582 585 {ECO:0000244|PDB:1Z68}.
HELIX 586 588 {ECO:0000244|PDB:1Z68}.
HELIX 594 608 {ECO:0000244|PDB:1Z68}.
STRAND 613 623 {ECO:0000244|PDB:1Z68}.
HELIX 625 634 {ECO:0000244|PDB:1Z68}.
STRAND 637 639 {ECO:0000244|PDB:1Z68}.
STRAND 642 648 {ECO:0000244|PDB:1Z68}.
TURN 653 655 {ECO:0000244|PDB:1Z68}.
HELIX 658 665 {ECO:0000244|PDB:1Z68}.
TURN 670 673 {ECO:0000244|PDB:1Z68}.
HELIX 674 679 {ECO:0000244|PDB:1Z68}.
HELIX 683 689 {ECO:0000244|PDB:1Z68}.
STRAND 692 699 {ECO:0000244|PDB:1Z68}.
STRAND 703 705 {ECO:0000244|PDB:1Z68}.
HELIX 708 719 {ECO:0000244|PDB:1Z68}.
STRAND 725 729 {ECO:0000244|PDB:1Z68}.
HELIX 739 756 {ECO:0000244|PDB:1Z68}.
SEQUENCE 760 AA; 87713 MW; 7FF817B5A4F75142 CRC64;
MKTWVKIVFG VATSAVLALL VMCIVLRPSR VHNSEENTMR ALTLKDILNG TFSYKTFFPN
WISGQEYLHQ SADNNIVLYN IETGQSYTIL SNRTMKSVNA SNYGLSPDRQ FVYLESDYSK
LWRYSYTATY YIYDLSNGEF VRGNELPRPI QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP
FQITFNGREN KIFNGIPDWV YEEEMLATKY ALWWSPNGKF LAYAEFNDTD IPVIAYSYYG
DEQYPRTINI PYPKAGAKNP VVRIFIIDTT YPAYVGPQEV PVPAMIASSD YYFSWLTWVT
DERVCLQWLK RVQNVSVLSI CDFREDWQTW DCPKTQEHIE ESRTGWAGGF FVSTPVFSYD
AISYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAINI FRVTQDSLFY SSNEFEEYPG
RRNIYRISIG SYPPSKKCVT CHLRKERCQY YTASFSDYAK YYALVCYGPG IPISTLHDGR
TDQEIKILEE NKELENALKN IQLPKEEIKK LEVDEITLWY KMILPPQFDR SKKYPLLIQV
YGGPCSQSVR SVFAVNWISY LASKEGMVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV SSWEYYASVY
TERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT ADDNVHFQNS AQIAKALVNA
QVDFQAMWYS DQNHGLSGLS TNHLYTHMTH FLKQCFSLSD


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