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Entry version 91 (12 Aug 2020)
Sequence version 1 (12 Jun 2007)
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Protein

Prolyl endopeptidase FAP

Gene

FAP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Also has 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.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotationBy similarity EC:3.4.14.5
  • Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.1 Publication EC:3.4.21.26

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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.By similarity1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.270 mM for Gly-Pro (Prolyl endopeptidase activity)1 Publication
  2. KM=0.206 mM for Gly-Pro-Phe-His (Prolyl endopeptidase activity)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei203SubstrateBy similarity1
    Binding sitei204SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei624Charge relay systemPROSITE-ProRule annotationBy similarity1
    Active sitei702Charge relay systemBy similarity1
    Active sitei734Charge relay systemBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Protease, Serine protease
    Biological processAngiogenesis, Apoptosis, Cell adhesion

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    A5D7B7

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    bovin-a5d7b7, DPP4N_Peptidase_S9

    MEROPS protease database

    More...
    MEROPSi
    S09.007

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Prolyl endopeptidase FAPBy similarity (EC:3.4.21.261 Publication)
    Alternative name(s):
    Dipeptidyl peptidase FAPBy similarity (EC:3.4.14.5By similarity)
    Fibroblast activation protein alphaBy similarity
    Short name:
    FAPalphaBy similarity
    Gelatine degradation protease FAPBy similarity (EC:3.4.21.-By similarity)
    Integral membrane serine proteaseBy similarity
    Post-proline cleaving enzymeCurated
    Serine integral membrane proteaseBy similarity
    Short name:
    SIMPBy similarity
    Surface-expressed proteaseBy similarity
    Short name:
    SepraseBy similarity
    Z-Pro-prolinal insensitive peptidase1 Publication
    Short name:
    ZIP1 Publication
    Cleaved into the following chain:
    Antiplasmin-cleaving enzyme FAP, soluble formBy similarity (EC:3.4.14.5By similarity, EC:3.4.21.-By similarity, EC:3.4.21.26By similarity)
    Short name:
    APCEBy similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:FAPBy similarityImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000321980 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence
    • UP000009136 Componenti: Chromosome 2

    Organism-specific databases

    Vertebrate Gene Nomenclature Database

    More...
    VGNCi
    VGNC:28862, FAP

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4CytoplasmicSequence analysisBy similarity4
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei5 – 25Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini26 – 760ExtracellularSequence analysisBy similarityAdd BLAST735

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3734641

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004306451 – 760Prolyl endopeptidase FAPBy similarityAdd BLAST760
    ChainiPRO_000043064624 – 760Antiplasmin-cleaving enzyme FAP, soluble formBy similarityAdd BLAST737

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi49N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
    Glycosylationi92N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
    Glycosylationi99N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
    Glycosylationi227N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
    Glycosylationi314N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationBy similarity1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi321 ↔ 332By similarity
    Disulfide bondi438 ↔ 441By similarity
    Disulfide bondi448 ↔ 466By similarity
    Disulfide bondi643 ↔ 755By similarity
    Glycosylationi679N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    N-glycosylated.By similarity
    The N-terminus may be blocked.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei23 – 24CleavageBy similarity2

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    A5D7B7

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSBTAG00000008140, Expressed in endometrium and 15 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    A5D7B7, baseline

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    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.

    By similarity

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    9913.ENSBTAP00000010702

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    A5D7B7

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    A5D7B7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili481 – 512Sequence analysisAdd BLAST32

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase S9B family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2100, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000160454

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_006105_4_3_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    A5D7B7

    KEGG Orthology (KO)

    More...
    KOi
    K08674

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NHGIYGG

    Database of Orthologous Groups

    More...
    OrthoDBi
    269253at2759

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313309

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.140.10.30, 1 hit
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058, AB_hydrolase
    IPR031245, FAP/Dpf2
    IPR002471, Pept_S9_AS
    IPR001375, Peptidase_S9
    IPR002469, Peptidase_S9B_N
    IPR038554, Peptidase_S9B_N_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11731:SF136, PTHR11731:SF136, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00930, DPPIV_N, 1 hit
    PF00326, Peptidase_S9, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53474, SSF53474, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    A5D7B7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTWLKIVFG VATSAVLALL VMCIVLRPSR VHNSEESTTR ALTLKDILNG
    60 70 80 90 100
    TFSYKTFFPN WISGQEYLHQ STDNNVVFYN IETGESYTIL SNTTMKSVNA
    110 120 130 140 150
    SNYGLSPDRQ FAYLESDYSK LWRYSYTATY HIYDLTNGEF IRRNELPRPI
    160 170 180 190 200
    QYLCWSPVGS KLAYVYQNNI YLKQRPEDPP FQITYNGKEN KIFNGIPDWV
    210 220 230 240 250
    YEEEMLATKY ALWWSPNGKF LAYAEFNDTE IPVIAYSYYG DEQYPRTINI
    260 270 280 290 300
    PYPKAGAKNP VVRIFIIDAT YPEHIGPREV PVPAMIASSD YYFSWLTWVT
    310 320 330 340 350
    DDRICLQWLK RIQNVSVLST CDFREDWQTW NCPKTQEHIE ESRTGWAGGF
    360 370 380 390 400
    FVSTPVFSHD TISYYKIFSD KDGYKHIHYI RDTVENAIQI TSGKWEAINI
    410 420 430 440 450
    FRVTQDSLFY SSNEFEGYPG RRNIYRISIG SHSPSKKCIT CHLRKKRCQY
    460 470 480 490 500
    YTASFSDYAK YYALVCYGPG LPISTLHDGR TDQEIKILED NKELENALKN
    510 520 530 540 550
    IQLPKEEIKK LKVDDITLWY KMILPPQFDK SKKYPLLIQV YGGPCSQSVR
    560 570 580 590 600
    SIFAVSWISY LASKEGIVIA LVDGRGTAFQ GDKLLYAVYR KLGVYEVEDQ
    610 620 630 640 650
    ITAVRKFIEM GFIDEKRIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV
    660 670 680 690 700
    SSWEYYASIY TERFMGLPTK DDNLKHYKNS TVMARAEYFR NVDYLLIHGT
    710 720 730 740 750
    ADDNVHFQNS AQIAKALVNA QVDFQAMWYS DQNHGLSGLS TKHLYTHMTH
    760
    FLKQCFSLSD
    Length:760
    Mass (Da):87,734
    Last modified:June 12, 2007 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i94E57F1252BEA933
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A3Q1LPV3A0A3Q1LPV3_BOVIN
    Prolyl endopeptidase FAP
    FAP
    745Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    DAAA02004416 Genomic DNA No translation available.
    BC140497 mRNA Translation: AAI40498.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001091470.1, NM_001098001.1

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSBTAT00000010702; ENSBTAP00000010702; ENSBTAG00000008140

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    508882

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bta:508882

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DAAA02004416 Genomic DNA No translation available.
    BC140497 mRNA Translation: AAI40498.1
    RefSeqiNP_001091470.1, NM_001098001.1

    3D structure databases

    SMRiA5D7B7
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000010702

    Chemistry databases

    BindingDBiA5D7B7
    ChEMBLiCHEMBL3734641

    Protein family/group databases

    ESTHERibovin-a5d7b7, DPP4N_Peptidase_S9
    MEROPSiS09.007

    Proteomic databases

    PaxDbiA5D7B7

    Genome annotation databases

    EnsembliENSBTAT00000010702; ENSBTAP00000010702; ENSBTAG00000008140
    GeneIDi508882
    KEGGibta:508882

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2191
    VGNCiVGNC:28862, FAP

    Phylogenomic databases

    eggNOGiKOG2100, Eukaryota
    GeneTreeiENSGT00940000160454
    HOGENOMiCLU_006105_4_3_1
    InParanoidiA5D7B7
    KOiK08674
    OMAiNHGIYGG
    OrthoDBi269253at2759
    TreeFamiTF313309

    Enzyme and pathway databases

    SABIO-RKiA5D7B7

    Gene expression databases

    BgeeiENSBTAG00000008140, Expressed in endometrium and 15 other tissues
    ExpressionAtlasiA5D7B7, baseline

    Family and domain databases

    Gene3Di2.140.10.30, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058, AB_hydrolase
    IPR031245, FAP/Dpf2
    IPR002471, Pept_S9_AS
    IPR001375, Peptidase_S9
    IPR002469, Peptidase_S9B_N
    IPR038554, Peptidase_S9B_N_sf
    PANTHERiPTHR11731:SF136, PTHR11731:SF136, 1 hit
    PfamiView protein in Pfam
    PF00930, DPPIV_N, 1 hit
    PF00326, Peptidase_S9, 1 hit
    SUPFAMiSSF53474, SSF53474, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSEPR_BOVIN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A5D7B7
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: June 12, 2007
    Last modified: August 12, 2020
    This is version 91 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Peptidase families
      Classification of peptidase families and list of entries
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