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Q9N2I7

- DPP4_FELCA

UniProt

Q9N2I7 - DPP4_FELCA

Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the. penultimate residue is proline By similarity.By similarity

    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 annotation

    Enzyme regulationi

    Inhibited by GPC3 and diprotin A.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei629 – 6291Charge relay systemPROSITE-ProRule annotation
    Active sitei707 – 7071Charge relay systemPROSITE-ProRule annotation
    Active sitei739 – 7391Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. dipeptidyl-peptidase activity Source: UniProtKB
    2. protease binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. receptor binding Source: UniProtKB
    5. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. endothelial cell migration Source: UniProtKB
    3. negative regulation of extracellular matrix disassembly Source: UniProtKB
    4. positive regulation of cell proliferation Source: UniProtKB
    5. T cell costimulation Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease

    Keywords - Biological processi

    Cell adhesion

    Protein family/group databases

    MEROPSiS09.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 4 (EC:3.4.14.5)
    Alternative name(s):
    Dipeptidyl peptidase IV
    Short name:
    DPP IV
    T-cell activation antigen CD26
    CD_antigen: CD26
    Cleaved into the following 2 chains:
    Alternative name(s):
    Dipeptidyl peptidase IV membrane form
    Alternative name(s):
    Dipeptidyl peptidase IV soluble form
    Gene namesi
    Name:DPP4
    Synonyms:CD26
    OrganismiFelis catus (Cat) (Felis silvestris catus)
    Taxonomic identifieri9685 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
    ProteomesiUP000011712: Unplaced

    Subcellular locationi

    Chain Dipeptidyl peptidase 4 soluble form : Secreted
    Note: Detected in the serum and the seminal fluid.By similarity
    Cell membrane By similarity; Single-pass type II membrane protein By similarity. Apical cell membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectioninvadopodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectionlamellipodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell junction By similarity. Membrane raft By similarity
    Note: Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface By similarity.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. cell junction Source: UniProtKB-SubCell
    3. cell surface Source: UniProtKB
    4. endocytic vesicle Source: UniProtKB
    5. extracellular region Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW
    7. invadopodium membrane Source: UniProtKB
    8. lamellipodium Source: UniProtKB
    9. lamellipodium membrane Source: UniProtKB-SubCell
    10. membrane raft Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 765765Dipeptidyl peptidase 4 membrane formPRO_0000027211Add
    BLAST
    Chaini38 – 765728Dipeptidyl peptidase 4 soluble formBy similarityPRO_0000027212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)By similarity
    Glycosylationi91 – 911N-linked (GlcNAc...)By similarity
    Glycosylationi149 – 1491N-linked (GlcNAc...)By similarity
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi228 – 2281N-linked (GlcNAc...)By similarity
    Glycosylationi280 – 2801N-linked (GlcNAc...)By similarity
    Glycosylationi320 – 3201N-linked (GlcNAc...)By similarity
    Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi384 ↔ 393By similarity
    Disulfide bondi443 ↔ 446By similarity
    Disulfide bondi453 ↔ 471By similarity
    Glycosylationi519 – 5191N-linked (GlcNAc...)By similarity
    Disulfide bondi648 ↔ 761By similarity
    Glycosylationi684 – 6841N-linked (GlcNAc...)By similarity

    Post-translational modificationi

    The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.By similarity
    N- and O-Glycosylated.By similarity
    Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer. Homodimer or heterodimer with Seprase (FAP). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Associates with collagen. Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts (extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts with CAV1 (via the N-terminus); the interaction is direct. Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11. Interacts with IGF2R; the interaction is direct. Interacts with GPC3 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9N2I7.
    SMRiQ9N2I7. Positions 37-765.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 765736ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family. DPPIV subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG005527.
    KOiK01278.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9N2I7-1 [UniParc]FASTAAdd to Basket

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    MKTPWKVLLG LLGLAALITI ITVPVVLLNK GNDAAADSRR TYTLTDYLKN    50
    TFRVKFYSLR WVSDHDYLYK QDNNILLFNA EYGNSSIFLE NSTFDEFEHS 100
    INDYSVSPDG QFILLEYNYV KQWRHSYTAS YDIYDLNKRQ LITEEKIPNN 150
    TQWITWSPEG HKLAYVWKND VYVKNEPNSS SHRITWTGEE NAIYNGIADW 200
    VYEEEIFSAY SALWWSPKGT FLAYAQFNDT QVPLIEYSFY SDESLQYPMT 250
    MRIPYPKAGA ANPTVKLFVI KTDNLNPNTN ATSVEITPPA AMLTGDYYLC 300
    DVTWANEERI SLQWLRRIQN YSVMDIRDYN NSTGKWISSA AQEHIEMSTT 350
    GWVGRFRPAE PHFTSDGRNF YKIISNEDGY KHICRFQIDK KDCTFITKGA 400
    WEVIGIEALT TDYLYYISNE YKGMPGGRNL YKIQLNDYTK VACLSCELKP 450
    ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT LHRSSNDEEL RVLEDNSALD 500
    KMLQEVQMPS KKLDFIILNE TKFWYQMILP PHFDTSKKYP LLIDVYAGPC 550
    SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF 600
    EVEDQIEAAR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI 650
    AVAPVSRWEY YDSVYTERYM GLPTPQDNLD YYKNSTVMSR AENFKQVEYL 700
    LIHGTADDNV HFQQSAQISK ALVDAGVDFQ AMWYTDEDHG IASGPAHQHI 750
    YTHMSHFIKQ CFSLP 765
    Length:765
    Mass (Da):88,213
    Last modified:October 1, 2000 - v1
    Checksum:i3EFCE98A22B175D9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023952 mRNA. Translation: BAA92344.1.
    RefSeqiNP_001009838.1. NM_001009838.1.

    Genome annotation databases

    GeneIDi493787.
    KEGGifca:493787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023952 mRNA. Translation: BAA92344.1 .
    RefSeqi NP_001009838.1. NM_001009838.1.

    3D structure databases

    ProteinModelPortali Q9N2I7.
    SMRi Q9N2I7. Positions 37-765.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S09.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 493787.
    KEGGi fca:493787.

    Organism-specific databases

    CTDi 1803.

    Phylogenomic databases

    HOVERGENi HBG005527.
    KOi K01278.

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view ]
    Pfami PF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequencing of a cDNA encoding the feline T-cell activation antigen CD26 homologue."
      Nishimura Y., Miyazawa T., Ikeda Y., Izumiya Y., Nakamura K., Sato E., Mikami T., Takahashi E.
      Immunogenetics 50:366-368(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peripheral blood.

    Entry informationi

    Entry nameiDPP4_FELCA
    AccessioniPrimary (citable) accession number: Q9N2I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3