SEPR_MOUSE
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 03-AUG-2022, entry version 172.
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 susceptibiliy. {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 RefSeq; XP_006498809.1; XM_006498746.3. [P97321-1]
DR AlphaFoldDB; P97321; -.
DR SMR; P97321; -.
DR BioGRID; 199593; 2.
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 GlyGen; P97321; 6 sites.
DR iPTMnet; P97321; -.
DR PhosphoSitePlus; P97321; -.
DR CPTAC; non-CPTAC-3745; -.
DR MaxQB; P97321; -.
DR PaxDb; P97321; -.
DR PeptideAtlas; P97321; -.
DR PRIDE; 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; 628 antibodies from 42 providers.
DR DNASU; 14089; -.
DR Ensembl; ENSMUST00000000402; ENSMUSP00000000402; ENSMUSG00000000392. [P97321-3]
DR Ensembl; ENSMUST00000102732; ENSMUSP00000099793; ENSMUSG00000000392. [P97321-1]
DR Ensembl; ENSMUST00000174448; ENSMUSP00000134386; ENSMUSG00000000392. [P97321-2]
DR GeneID; 14089; -.
DR KEGG; mmu:14089; -.
DR UCSC; uc008jvk.2; mouse. [P97321-1]
DR UCSC; uc008jvl.1; mouse. [P97321-3]
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; 269253at2759; -.
DR PhylomeDB; P97321; -.
DR TreeFam; TF313309; -.
DR BRENDA; 3.4.21.B28; 3474.
DR BioGRID-ORCS; 14089; 2 hits in 74 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 tissues.
DR ExpressionAtlas; P97321; baseline and differential.
DR Genevisible; P97321; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905368; C:peptidase complex; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; 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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR031245; FAP-alpha.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF136; PTHR11731:SF136; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 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
