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Prolyl endopeptidase FAP (EC 3.4.21.26) (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) (Z-Pro-prolinal insensitive peptidase) (ZIP) [Cleaved into: Antiplasmin-cleaving enzyme FAP, soluble form (APCE) (EC 3.4.14.5) (EC 3.4.21.-) (EC 3.4.21.26)]

 SEPR_BOVIN              Reviewed;         760 AA.
A5D7B7;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
12-JUN-2007, sequence version 1.
23-MAY-2018, entry version 81.
RecName: Full=Prolyl endopeptidase FAP {ECO:0000250|UniProtKB:Q12884};
EC=3.4.21.26 {ECO:0000269|PubMed:15313476};
AltName: Full=Dipeptidyl peptidase FAP {ECO:0000250|UniProtKB:Q12884};
EC=3.4.14.5 {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Fibroblast activation protein alpha {ECO:0000250|UniProtKB:Q12884};
Short=FAPalpha {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Gelatine degradation protease FAP {ECO:0000250|UniProtKB:Q12884};
EC=3.4.21.- {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Integral membrane serine protease {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Post-proline cleaving enzyme {ECO:0000305};
AltName: Full=Serine integral membrane protease {ECO:0000250|UniProtKB:Q12884};
Short=SIMP {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Surface-expressed protease {ECO:0000250|UniProtKB:Q12884};
Short=Seprase {ECO:0000250|UniProtKB:Q12884};
AltName: Full=Z-Pro-prolinal insensitive peptidase {ECO:0000303|PubMed:15313476};
Short=ZIP {ECO:0000303|PubMed:15313476};
Contains:
RecName: Full=Antiplasmin-cleaving enzyme FAP, soluble form {ECO:0000250|UniProtKB:Q12884};
Short=APCE {ECO:0000250|UniProtKB:Q12884};
EC=3.4.14.5 {ECO:0000250|UniProtKB:Q12884};
EC=3.4.21.- {ECO:0000250|UniProtKB:Q12884};
EC=3.4.21.26 {ECO:0000250|UniProtKB:Q12884};
Name=FAP {ECO:0000250|UniProtKB:Q12884, ECO:0000312|EMBL:AAI40498.1,
ECO:0000312|Ensembl:ENSBTAP00000010702};
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hereford {ECO:0000312|EMBL:DAAA02004416};
PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
"A whole-genome assembly of the domestic cow, Bos taurus.";
Genome Biol. 10:R42.01-R42.10(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford {ECO:0000312|EMBL:AAI40498.1}; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[3]
PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=15313476; DOI=10.1016/j.biocel.2004.05.006;
Collins P.J., McMahon G., O'Brien P., O'Connor B.;
"Purification, identification and characterisation of seprase from
bovine serum.";
Int. J. Biochem. Cell Biol. 36:2320-2333(2004).
-!- 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. Degrade also gelatin, heat-denatured type I
collagen, but not native collagen type I and IV, vibronectin,
tenascin, laminin, fibronectin, fibrin or casein. 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. Natural neuropeptide hormones for dipeptidyl
peptidase are the neuropeptide Y (NPY), peptide YY (PYY),
substance P (TAC1) and brain natriuretic peptide 32 (NPPB). 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:Q12884, ECO:0000269|PubMed:15313476}.
-!- 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:0000250|UniProtKB:Q12884, ECO:0000255|PROSITE-
ProRule:PRU10084}.
-!- CATALYTIC ACTIVITY: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in
oligopeptides. {ECO:0000269|PubMed:15313476}.
-!- 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:0000250|UniProtKB:Q12884,
ECO:0000269|PubMed:15313476}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.270 mM for Gly-Pro (Prolyl endopeptidase activity)
{ECO:0000269|PubMed:15313476};
KM=0.206 mM for Gly-Pro-Phe-His (Prolyl endopeptidase activity)
{ECO:0000269|PubMed:15313476};
-!- 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:0000250|UniProtKB:Q12884}.
-!- SUBCELLULAR LOCATION: Prolyl endopeptidase FAP: Cell surface
{ECO:0000250|UniProtKB:Q12884}. Cell membrane
{ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane
protein {ECO:0000255}. Cell projection, lamellipodium membrane
{ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane
protein {ECO:0000255}. Cell projection, invadopodium membrane
{ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane
protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q12884};
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:0000250|UniProtKB:Q12884}.
-!- SUBCELLULAR LOCATION: Antiplasmin-cleaving enzyme FAP, soluble
form: Secreted {ECO:0000250|UniProtKB:Q12884}. Note=Found in blood
plasma and serum. {ECO:0000250|UniProtKB:Q12884}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q12884}.
-!- PTM: The N-terminus may be blocked.
{ECO:0000250|UniProtKB:Q12884}.
-!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; DAAA02004416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC140497; AAI40498.1; -; mRNA.
RefSeq; NP_001091470.1; NM_001098001.1.
UniGene; Bt.2717; -.
ProteinModelPortal; A5D7B7; -.
SMR; A5D7B7; -.
STRING; 9913.ENSBTAP00000010702; -.
BindingDB; A5D7B7; -.
ChEMBL; CHEMBL3734641; -.
ESTHER; bovin-a5d7b7; DPP4N_Peptidase_S9.
MEROPS; S09.007; -.
PaxDb; A5D7B7; -.
Ensembl; ENSBTAT00000010702; ENSBTAP00000010702; ENSBTAG00000008140.
GeneID; 508882; -.
KEGG; bta:508882; -.
CTD; 2191; -.
VGNC; VGNC:28862; FAP.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00760000119233; -.
HOGENOM; HOG000231875; -.
HOVERGEN; HBG005527; -.
InParanoid; A5D7B7; -.
KO; K08674; -.
OMA; NEFEGYP; -.
OrthoDB; EOG091G0BU5; -.
TreeFam; TF313309; -.
SABIO-RK; A5D7B7; -.
Proteomes; UP000009136; Chromosome 2.
Bgee; ENSBTAG00000008140; -.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0071438; C:invadopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:1902362; P:melanocyte apoptotic process; IEA:Ensembl.
GO; GO:0097325; P:melanocyte proliferation; IEA:Ensembl.
GO; GO:0071850; P:mitotic cell cycle arrest; IEA:Ensembl.
GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; IEA:Ensembl.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IEA:Ensembl.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
GO; GO:0010710; P:regulation of collagen catabolic process; IEA:Ensembl.
Gene3D; 2.140.10.30; -; 1.
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.
InterPro; IPR038554; Peptidase_S9B_N_sf.
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;
Angiogenesis; Apoptosis; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Cleavage on pair of basic residues; Coiled coil;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
Secreted; Serine protease; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 760 Prolyl endopeptidase FAP.
{ECO:0000250|UniProtKB:Q12884}.
/FTId=PRO_0000430645.
CHAIN 24 760 Antiplasmin-cleaving enzyme FAP, soluble
form. {ECO:0000250|UniProtKB:Q12884}.
/FTId=PRO_0000430646.
TOPO_DOM 1 4 Cytoplasmic.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255}.
TRANSMEM 5 25 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 26 760 Extracellular.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255}.
COILED 481 512 {ECO:0000255}.
ACT_SITE 624 624 Charge relay system.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 702 702 Charge relay system.
{ECO:0000250|UniProtKB:Q12884}.
ACT_SITE 734 734 Charge relay system.
{ECO:0000250|UniProtKB:Q12884}.
BINDING 203 203 Substrate.
{ECO:0000250|UniProtKB:Q12884}.
BINDING 204 204 Substrate.
{ECO:0000250|UniProtKB:Q12884}.
SITE 23 24 Cleavage. {ECO:0000250|UniProtKB:Q12884}.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q12884,
ECO:0000255|PROSITE-ProRule:PRU10084}.
CARBOHYD 679 679 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
DISULFID 321 332 {ECO:0000250|UniProtKB:Q12884}.
DISULFID 438 441 {ECO:0000250|UniProtKB:Q12884}.
DISULFID 448 466 {ECO:0000250|UniProtKB:Q12884}.
DISULFID 643 755 {ECO:0000250|UniProtKB:Q12884}.
SEQUENCE 760 AA; 87734 MW; 94E57F1252BEA933 CRC64;
MKTWLKIVFG VATSAVLALL VMCIVLRPSR VHNSEESTTR ALTLKDILNG TFSYKTFFPN
WISGQEYLHQ STDNNVVFYN IETGESYTIL SNTTMKSVNA SNYGLSPDRQ FAYLESDYSK
LWRYSYTATY HIYDLTNGEF IRRNELPRPI QYLCWSPVGS KLAYVYQNNI YLKQRPEDPP
FQITYNGKEN KIFNGIPDWV YEEEMLATKY ALWWSPNGKF LAYAEFNDTE IPVIAYSYYG
DEQYPRTINI PYPKAGAKNP VVRIFIIDAT YPEHIGPREV PVPAMIASSD YYFSWLTWVT
DDRICLQWLK RIQNVSVLST CDFREDWQTW NCPKTQEHIE ESRTGWAGGF FVSTPVFSHD
TISYYKIFSD KDGYKHIHYI RDTVENAIQI TSGKWEAINI FRVTQDSLFY SSNEFEGYPG
RRNIYRISIG SHSPSKKCIT CHLRKKRCQY YTASFSDYAK YYALVCYGPG LPISTLHDGR
TDQEIKILED NKELENALKN IQLPKEEIKK LKVDDITLWY KMILPPQFDK SKKYPLLIQV
YGGPCSQSVR SIFAVSWISY LASKEGIVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV SSWEYYASIY
TERFMGLPTK DDNLKHYKNS TVMARAEYFR NVDYLLIHGT ADDNVHFQNS AQIAKALVNA
QVDFQAMWYS DQNHGLSGLS TKHLYTHMTH FLKQCFSLSD


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