ID   SEPR_MOUSE              Reviewed;         761 AA.
AC   P97321;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 189.
DE   RecName: Full=Prolyl endopeptidase FAP {ECO:0000250|UniProtKB:Q12884};
DE            EC=3.4.21.26 {ECO:0000269|PubMed:24371721};
DE   AltName: Full=Dipeptidyl peptidase FAP {ECO:0000250|UniProtKB:Q12884};
DE            EC=3.4.14.5 {ECO:0000269|PubMed:10629066, ECO:0000269|PubMed:11330865, ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:9688278};
DE   AltName: Full=Fibroblast activation protein alpha {ECO:0000250|UniProtKB:Q12884};
DE            Short=FAPalpha {ECO:0000303|PubMed:15133496};
DE   AltName: Full=Gelatine degradation protease FAP {ECO:0000250|UniProtKB:Q12884};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q12884};
DE   AltName: Full=Integral membrane serine protease {ECO:0000250|UniProtKB:Q12884};
DE   AltName: Full=Post-proline cleaving enzyme {ECO:0000305};
DE   AltName: Full=Serine integral membrane protease {ECO:0000250|UniProtKB:Q12884};
DE            Short=SIMP {ECO:0000250|UniProtKB:Q12884};
DE   AltName: Full=Surface-expressed protease {ECO:0000250|UniProtKB:Q12884};
DE            Short=Seprase {ECO:0000250|UniProtKB:Q12884};
DE   Contains:
DE     RecName: Full=Antiplasmin-cleaving enzyme FAP, soluble form {ECO:0000250|UniProtKB:Q12884};
DE              Short=APCE {ECO:0000250|UniProtKB:Q12884};
DE              EC=3.4.14.5 {ECO:0000250|UniProtKB:Q12884};
DE              EC=3.4.21.- {ECO:0000250|UniProtKB:Q12884};
DE              EC=3.4.21.26 {ECO:0000250|UniProtKB:Q12884};
GN   Name=Fap {ECO:0000312|MGI:MGI:109608};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=BALB/cJ; TISSUE=Embryo;
RX   PubMed=9139873;
RX   DOI=10.1002/(sici)1097-0215(19970502)71:3<383::aid-ijc14>3.0.co;2-h;
RA   Niedermeyer J., Scanlan M.J., Garin-Chesa P., Daiber C., Fiebig H.H.,
RA   Old L.J., Rettig W.J., Schnapp A.;
RT   "Mouse fibroblast activation protein: molecular cloning, alternative
RT   splicing and expression in the reactive stroma of epithelial cancers.";
RL   Int. J. Cancer 71:383-389(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=9688278; DOI=10.1046/j.1432-1327.1998.2540650.x;
RA   Niedermeyer J., Enenkel B., Park J.E., Lenter M., Rettig W.J., Damm K.,
RA   Schnapp A.;
RT   "Mouse fibroblast-activation protein--conserved Fap gene organization and
RT   biochemical function as a serine protease.";
RL   Eur. J. Biochem. 254:650-654(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=10629066; DOI=10.1128/mcb.20.3.1089-1094.2000;
RA   Niedermeyer J., Kriz M., Hilberg F., Garin-Chesa P., Bamberger U.,
RA   Lenter M.C., Park J., Viertel B., Puschner H., Mauz M., Rettig W.J.,
RA   Schnapp A.;
RT   "Targeted disruption of mouse fibroblast activation protein.";
RL   Mol. Cell. Biol. 20:1089-1094(2000).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11330865;
RA   Niedermeyer J., Garin-Chesa P., Kriz M., Hilberg F., Mueller E.,
RA   Bamberger U., Rettig W.J., Schnapp A.;
RT   "Expression of the fibroblast activation protein during mouse embryo
RT   development.";
RL   Int. J. Dev. Biol. 45:445-447(2001).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   SER-624.
RX   PubMed=15133496; DOI=10.1038/sj.onc.1207730;
RA   Ramirez-Montagut T., Blachere N.E., Sviderskaya E.V., Bennett D.C.,
RA   Rettig W.J., Garin-Chesa P., Houghton A.N.;
RT   "FAPalpha, a surface peptidase expressed during wound healing, is a tumor
RT   suppressor.";
RL   Oncogene 23:5435-5446(2004).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=21051638; DOI=10.1126/science.1195300;
RA   Kraman M., Bambrough P.J., Arnold J.N., Roberts E.W., Magiera L.,
RA   Jones J.O., Gopinathan A., Tuveson D.A., Fearon D.T.;
RT   "Suppression of antitumor immunity by stromal cells expressing fibroblast
RT   activation protein-alpha.";
RL   Science 330:827-830(2010).
RN   [8]
RP   FUNCTION.
RX   PubMed=23710635; DOI=10.5483/bmbrep.2013.46.5.172;
RA   Cai F., Li Z., Wang C., Xian S., Xu G., Peng F., Wei Y., Lu Y.;
RT   "Short hairpin RNA targeting of fibroblast activation protein inhibits
RT   tumor growth and improves the tumor microenvironment in a mouse model.";
RL   BMB Rep. 46:252-257(2013).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24371721; DOI=10.1016/j.fob.2013.12.001;
RA   Keane F.M., Yao T.W., Seelk S., Gall M.G., Chowdhury S., Poplawski S.E.,
RA   Lai J.H., Li Y., Wu W., Farrell P., Vieira de Ribeiro A.J., Osborne B.,
RA   Yu D.M., Seth D., Rahman K., Haber P., Topaloglu A.K., Wang C., Thomson S.,
RA   Hennessy A., Prins J., Twigg S.M., McLennan S.V., McCaughan G.W.,
RA   Bachovchin W.W., Gorrell M.D.;
RT   "Quantitation of fibroblast activation protein (FAP)-specific protease
RT   activity in mouse, baboon and human fluids and organs.";
RL   FEBS Open Bio 4:43-54(2013).
CC   -!- FUNCTION: Cell surface glycoprotein serine protease that participates
CC       in extracellular matrix degradation and involved in many cellular
CC       processes including tissue remodeling, fibrosis, wound healing,
CC       inflammation and tumor growth. Both plasma membrane and soluble forms
CC       exhibit post-proline cleaving endopeptidase activity, with a marked
CC       preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on
CC       substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also
CC       gelatin, heat-denatured type I collagen, but not native collagen type I
CC       and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein.
CC       Also has dipeptidyl peptidase activity, exhibiting the ability to
CC       hydrolyze the prolyl bond two residues from the N-terminus of synthetic
CC       dipeptide substrates provided that the penultimate residue is proline,
CC       with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro.
CC       Natural neuropeptide hormones for dipeptidyl peptidase are the
CC       neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain
CC       natriuretic peptide 32 (NPPB). The plasma membrane form, in association
CC       with either DPP4, PLAUR or integrins, is involved in the pericellular
CC       proteolysis of the extracellular matrix (ECM), and hence promotes cell
CC       adhesion, migration and invasion through the ECM. Plays a role in
CC       tissue remodeling during development and wound healing. Participates in
CC       the cell invasiveness towards the ECM in malignant melanoma cancers.
CC       Enhances tumor growth progression by increasing angiogenesis, collagen
CC       fiber degradation and apoptosis and by reducing antitumor response of
CC       the immune system. Promotes glioma cell invasion through the brain
CC       parenchyma by degrading the proteoglycan brevican. Acts as a tumor
CC       suppressor in melanocytic cells through regulation of cell
CC       proliferation and survival in a serine protease activity-independent
CC       manner. {ECO:0000269|PubMed:10629066, ECO:0000269|PubMed:11330865,
CC       ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:21051638,
CC       ECO:0000269|PubMed:23710635, ECO:0000269|PubMed:24371721,
CC       ECO:0000269|PubMed:9688278}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000269|PubMed:24371721};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084, ECO:0000269|PubMed:10629066,
CC         ECO:0000269|PubMed:11330865, ECO:0000269|PubMed:15133496,
CC         ECO:0000269|PubMed:9688278};
CC   -!- ACTIVITY REGULATION: Gelatinase activity is inhibited by serine-
CC       protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4-
CC       (2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4-
CC       amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate
CC       (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF).
CC       Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3-
CC       ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP).
CC       Prolyl endopeptidase activity is inhibited by the boronic acid peptide
CC       Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-
CC       chloromethyl ketone. {ECO:0000250|UniProtKB:Q12884}.
CC   -!- SUBUNIT: Homodimer; homodimerization is required for activity of both
CC       plasma membrane and soluble forms. The monomer is inactive. Heterodimer
CC       with DPP4. Interacts with PLAUR; the interaction occurs at the cell
CC       surface of invadopodia membranes. Interacts with ITGB1. Interacts with
CC       ITGA3. Associates with integrin alpha-3/beta-1; the association occurs
CC       in a collagen-dependent manner at the cell surface of invadopodia
CC       membranes. {ECO:0000250|UniProtKB:Q12884}.
CC   -!- SUBCELLULAR LOCATION: [Prolyl endopeptidase FAP]: Cell surface
CC       {ECO:0000269|PubMed:15133496}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein
CC       {ECO:0000255}. Cell projection, lamellipodium membrane
CC       {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein
CC       {ECO:0000255}. Cell projection, invadopodium membrane
CC       {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein
CC       {ECO:0000255}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein
CC       {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass
CC       type II membrane protein {ECO:0000255}. Note=Localized on cell surface
CC       with lamellipodia and invadopodia membranes and on shed vesicles.
CC       Colocalized with DPP4 at invadopodia and lamellipodia membranes of
CC       migratory activated endothelial cells in collagenous matrix.
CC       Colocalized with DPP4 on endothelial cells of capillary-like
CC       microvessels but not large vessels within invasive breast ductal
CC       carcinoma. Anchored and enriched preferentially by integrin alpha-
CC       3/beta-1 at invadopodia, plasma membrane protrusions that correspond to
CC       sites of cell invasion, in a collagen-dependent manner. Localized at
CC       plasma and ruffle membranes in a collagen-independent manner.
CC       Colocalized with PLAUR preferentially at the cell surface of
CC       invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-
CC       dependent manner. Concentrated at invadopodia membranes, specialized
CC       protrusions of the ventral plasma membrane in a fibrobectin-dependent
CC       manner. Colocalizes with extracellular components (ECM), such as
CC       collagen fibers and fibronectin. {ECO:0000250|UniProtKB:Q12884}.
CC   -!- SUBCELLULAR LOCATION: [Antiplasmin-cleaving enzyme FAP, soluble form]:
CC       Secreted {ECO:0000269|PubMed:24371721}. Note=Found in blood plasma and
CC       serum. {ECO:0000269|PubMed:24371721}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97321-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97321-2; Sequence=VSP_005368;
CC       Name=3;
CC         IsoId=P97321-3; Sequence=VSP_005369;
CC   -!- TISSUE SPECIFICITY: Expressed strongly in uterus, pancreas,
CC       submaxillary gland and skin, less in lymph node, ovary, skeletal
CC       muscle, adrenal and bone marrow. Expressed in reactive stromal
CC       fibroblast in epithelial cancers. Expressed in melanocytes but not
CC       melanomas (at protein level). Detected in fibroblasts, in placenta,
CC       uterus, embryos from day 7-19 and in newborn mice (P1).
CC       {ECO:0000269|PubMed:15133496, ECO:0000269|PubMed:21051638,
CC       ECO:0000269|PubMed:24371721}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing myotubes at 11.5 dpc.
CC       Expressed in the dermomyotome component of the somites at 12.5 dpc.
CC       Expressed in fibroblasts at 13 dpc. Expressed in the perichondrial
CC       mesenchymal cells from the cartilage primordium of the ribs and in the
CC       scattered developing intercostal muscle fibs at 16.5 dpc (at protein
CC       level). Expressed in the primitive mesenchymal condensation adjacent to
CC       the eye and in primitive mesenchymal cells surrounding the
CC       cartilaginous primordia of the bones at 13.5 dpc.
CC       {ECO:0000269|PubMed:10629066, ECO:0000269|PubMed:11330865}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q12884}.
CC   -!- PTM: The N-terminus may be blocked. {ECO:0000250|UniProtKB:Q12884}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and fertile
CC       and display no overt developmental defects and no general change in
CC       cancer susceptibility. {ECO:0000269|PubMed:10629066}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; Y10007; CAA71116.1; -; mRNA.
DR   EMBL; BC019190; AAH19190.1; -; mRNA.
DR   CCDS; CCDS16067.1; -. [P97321-1]
DR   RefSeq; NP_032012.1; NM_007986.3. [P97321-1]
DR   AlphaFoldDB; P97321; -.
DR   SMR; P97321; -.
DR   BioGRID; 199593; 2.
DR   FunCoup; P97321; 51.
DR   STRING; 10090.ENSMUSP00000099793; -.
DR   BindingDB; P97321; -.
DR   ChEMBL; CHEMBL5769; -.
DR   DrugCentral; P97321; -.
DR   ESTHER; mouse-FAP; DPP4N_Peptidase_S9.
DR   MEROPS; S09.007; -.
DR   GlyCosmos; P97321; 6 sites, No reported glycans.
DR   GlyGen; P97321; 7 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P97321; -.
DR   PhosphoSitePlus; P97321; -.
DR   CPTAC; non-CPTAC-3745; -.
DR   PaxDb; 10090-ENSMUSP00000099793; -.
DR   PeptideAtlas; P97321; -.
DR   ProteomicsDB; 256618; -. [P97321-1]
DR   ProteomicsDB; 256619; -. [P97321-2]
DR   ProteomicsDB; 256620; -. [P97321-3]
DR   ABCD; P97321; 1 sequenced antibody.
DR   Antibodypedia; 33750; 724 antibodies from 47 providers.
DR   DNASU; 14089; -.
DR   Ensembl; ENSMUST00000000402.16; ENSMUSP00000000402.10; ENSMUSG00000000392.18. [P97321-3]
DR   Ensembl; ENSMUST00000102732.10; ENSMUSP00000099793.4; ENSMUSG00000000392.18. [P97321-1]
DR   Ensembl; ENSMUST00000174448.8; ENSMUSP00000134386.2; ENSMUSG00000000392.18. [P97321-2]
DR   GeneID; 14089; -.
DR   KEGG; mmu:14089; -.
DR   UCSC; uc008jvk.2; mouse. [P97321-1]
DR   UCSC; uc008jvl.1; mouse. [P97321-3]
DR   AGR; MGI:109608; -.
DR   CTD; 2191; -.
DR   MGI; MGI:109608; Fap.
DR   VEuPathDB; HostDB:ENSMUSG00000000392; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   GeneTree; ENSGT00940000160454; -.
DR   HOGENOM; CLU_006105_4_3_1; -.
DR   InParanoid; P97321; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 16520at2759; -.
DR   PhylomeDB; P97321; -.
DR   BRENDA; 3.4.21.B28; 3474.
DR   BioGRID-ORCS; 14089; 2 hits in 79 CRISPR screens.
DR   PRO; PR:P97321; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P97321; protein.
DR   Bgee; ENSMUSG00000000392; Expressed in diaphysis of femur and 219 other cell types or tissues.
DR   ExpressionAtlas; P97321; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0045178; C:basal part of cell; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; EXP:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISO:GO_Central.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:1905368; C:peptidase complex; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; EXP:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0005178; F:integrin binding; ISO:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; EXP:UniProtKB.
DR   GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR   GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:1902362; P:melanocyte apoptotic process; IDA:UniProtKB.
DR   GO; GO:0097325; P:melanocyte proliferation; IDA:UniProtKB.
DR   GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IDA:UniProtKB.
DR   GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; ISS:UniProtKB.
DR   GO; GO:1903054; P:negative regulation of extracellular matrix organization; ISS:UniProtKB.
DR   GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
DR   FunFam; 2.140.10.30:FF:000001; Dipeptidyl peptidase 4; 1.
DR   FunFam; 3.40.50.1820:FF:000003; Dipeptidyl peptidase 4; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9_cat.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   InterPro; IPR050278; Serine_Prot_S9B/DPPIV.
DR   PANTHER; PTHR11731:SF136; PROLYL ENDOPEPTIDASE FAP; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Angiogenesis; Apoptosis; Cell adhesion;
KW   Cell junction; Cell membrane; Cell projection;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..761
FT                   /note="Prolyl endopeptidase FAP"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT                   /id="PRO_0000122425"
FT   CHAIN           24..761
FT                   /note="Antiplasmin-cleaving enzyme FAP, soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT                   /id="PRO_0000430644"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884, ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..761
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884, ECO:0000255"
FT   ACT_SITE        624
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        702
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   ACT_SITE        734
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   SITE            23..24
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12884,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        321..332
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   DISULFID        438..441
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   DISULFID        448..466
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   DISULFID        643..756
FT                   /evidence="ECO:0000250|UniProtKB:Q12884"
FT   VAR_SEQ         31..63
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9139873"
FT                   /id="VSP_005369"
FT   VAR_SEQ         31..35
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9139873"
FT                   /id="VSP_005368"
FT   MUTAGEN         624
FT                   /note="S->A: Localized at the cell surface, inhibits
FT                   gelatinase and dipeptidyl peptidase activities and
FT                   stimulates tumor suppression activity."
FT                   /evidence="ECO:0000269|PubMed:15133496"
FT   CONFLICT        737
FT                   /note="S -> L (in Ref. 3; AAH19190)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   761 AA;  87945 MW;  9174C3AEDA213B25 CRC64;
     MKTWLKTVFG VTTLAALALV VICIVLRPSR VYKPEGNTKR ALTLKDILNG TFSYKTYFPN
     WISEQEYLHQ SEDDNIVFYN IETRESYIIL SNSTMKSVNA TDYGLSPDRQ FVYLESDYSK
     LWRYSYTATY YIYDLQNGEF VRGYELPRPI QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP
     FQITYTGREN RIFNGIPDWV YEEEMLATKY ALWWSPDGKF LAYVEFNDSD IPIIAYSYYG
     DGQYPRTINI PYPKAGAKNP VVRVFIVDTT YPHHVGPMEV PVPEMIASSD YYFSWLTWVS
     SERVCLQWLK RVQNVSVLSI CDFREDWHAW ECPKNQEHVE ESRTGWAGGF FVSTPAFSQD
     ATSYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAIYI FRVTQDSLFY SSNEFEGYPG
     RRNIYRISIG NSPPSKKCVT CHLRKERCQY YTASFSYKAK YYALVCYGPG LPISTLHDGR
     TDQEIQVLEE NKELENSLRN IQLPKVEIKK LKDGGLTFWY KMILPPQFDR SKKYPLLIQV
     YGGPCSQSVK SVFAVNWITY LASKEGIVIA LVDGRGTAFQ GDKFLHAVYR KLGVYEVEDQ
     LTAVRKFIEM GFIDEERIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV SSWEYYASIY
     SERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT ADDNVHFQNS AQIAKALVNA
     QVDFQAMWYS DQNHGISSGR SQNHLYTHMT HFLKQCFSLS D
//