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Q9N2I7

- DPP4_FELCA

UniProt

Q9N2I7 - DPP4_FELCA

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Protein

Dipeptidyl peptidase 4

Gene
DPP4, CD26
Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

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.

Enzyme regulationi

Inhibited by GPC3 and diprotin A By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei629 – 6291Charge relay system By similarity
Active sitei707 – 7071Charge relay system By similarity
Active sitei739 – 7391Charge relay system By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. dipeptidyl-peptidase activity Source: UniProtKB
  3. protease binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. receptor binding Source: UniProtKB
  6. 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
Complete GO annotation...

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; Single-pass type II membrane protein By similarity. Apical cell membrane; Single-pass type II membrane protein By similarity. Cell projectioninvadopodium membrane; Single-pass type II membrane protein By similarity. Cell projectionlamellipodium membrane; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini30 – 765736Extracellular Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 form By 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...) Reviewed prediction
Glycosylationi228 – 2281N-linked (GlcNAc...) By similarity
Glycosylationi280 – 2801N-linked (GlcNAc...) By similarity
Glycosylationi320 – 3201N-linked (GlcNAc...) By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi331 – 3311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi384 ↔ 393 By similarity
Disulfide bondi443 ↔ 446 By similarity
Disulfide bondi453 ↔ 471 By similarity
Glycosylationi519 – 5191N-linked (GlcNAc...) By similarity
Disulfide bondi648 ↔ 761 By 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.

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.

Structurei

3D structure databases

ProteinModelPortaliQ9N2I7.
SMRiQ9N2I7. Positions 37-765.

Family & Domainsi

Sequence similaritiesi

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: June 11, 2014
This is version 93 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

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