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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotationBy similarity

Enzyme regulationi

Inhibited by GPC3 and diprotin A.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei629Charge relay systemPROSITE-ProRule annotation1
Active sitei707Charge relay systemPROSITE-ProRule annotation1
Active sitei739Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease

Keywords - Biological processi

Cell adhesion

Protein family/group databases

ESTHERifelca-CD26. DPP4N_Peptidase_S9.
MEROPSiS09.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5By similarity)
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
Proteomesi
  • UP000011712 Componenti: Unplaced

Subcellular locationi

Dipeptidyl peptidase 4 soluble form :
  • Secreted

  • Note: Detected in the serum and the seminal fluid.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 765ExtracellularSequence analysisAdd BLAST736

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000272111 – 765Dipeptidyl peptidase 4 membrane formAdd BLAST765
ChainiPRO_000002721238 – 765Dipeptidyl peptidase 4 soluble formBy similarityAdd BLAST728

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84N-linked (GlcNAc...)By similarity1
Glycosylationi91N-linked (GlcNAc...)By similarity1
Glycosylationi149N-linked (GlcNAc...)By similarity1
Glycosylationi178N-linked (GlcNAc...)Sequence analysis1
Glycosylationi228N-linked (GlcNAc...)By similarity1
Glycosylationi280N-linked (GlcNAc...)By similarity1
Glycosylationi320N-linked (GlcNAc...)By similarity1
Glycosylationi330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi331N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi384 ↔ 393By similarity
Disulfide bondi443 ↔ 446By similarity
Disulfide bondi453 ↔ 471By similarity
Glycosylationi519N-linked (GlcNAc...)By similarity1
Disulfide bondi648 ↔ 761By similarity
Glycosylationi684N-linked (GlcNAc...)By similarity1

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

Proteomic databases

PRIDEiQ9N2I7.

Interactioni

Subunit structurei

Monomer. Homodimer. 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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000004117.

Structurei

3D structure databases

ProteinModelPortaliQ9N2I7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
HOVERGENiHBG005527.
InParanoidiQ9N2I7.
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_N.
[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

« Hide

        10         20         30         40         50
MKTPWKVLLG LLGLAALITI ITVPVVLLNK GNDAAADSRR TYTLTDYLKN
60 70 80 90 100
TFRVKFYSLR WVSDHDYLYK QDNNILLFNA EYGNSSIFLE NSTFDEFEHS
110 120 130 140 150
INDYSVSPDG QFILLEYNYV KQWRHSYTAS YDIYDLNKRQ LITEEKIPNN
160 170 180 190 200
TQWITWSPEG HKLAYVWKND VYVKNEPNSS SHRITWTGEE NAIYNGIADW
210 220 230 240 250
VYEEEIFSAY SALWWSPKGT FLAYAQFNDT QVPLIEYSFY SDESLQYPMT
260 270 280 290 300
MRIPYPKAGA ANPTVKLFVI KTDNLNPNTN ATSVEITPPA AMLTGDYYLC
310 320 330 340 350
DVTWANEERI SLQWLRRIQN YSVMDIRDYN NSTGKWISSA AQEHIEMSTT
360 370 380 390 400
GWVGRFRPAE PHFTSDGRNF YKIISNEDGY KHICRFQIDK KDCTFITKGA
410 420 430 440 450
WEVIGIEALT TDYLYYISNE YKGMPGGRNL YKIQLNDYTK VACLSCELKP
460 470 480 490 500
ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT LHRSSNDEEL RVLEDNSALD
510 520 530 540 550
KMLQEVQMPS KKLDFIILNE TKFWYQMILP PHFDTSKKYP LLIDVYAGPC
560 570 580 590 600
SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF
610 620 630 640 650
EVEDQIEAAR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI
660 670 680 690 700
AVAPVSRWEY YDSVYTERYM GLPTPQDNLD YYKNSTVMSR AENFKQVEYL
710 720 730 740 750
LIHGTADDNV HFQQSAQISK ALVDAGVDFQ AMWYTDEDHG IASGPAHQHI
760
YTHMSHFIKQ CFSLP
Length:765
Mass (Da):88,213
Last modified:October 1, 2000 - v1
Checksum:i3EFCE98A22B175D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB023952 mRNA. Translation: BAA92344.1.
RefSeqiNP_001009838.1. NM_001009838.1.

3D structure databases

ProteinModelPortaliQ9N2I7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000004117.

Protein family/group databases

ESTHERifelca-CD26. DPP4N_Peptidase_S9.
MEROPSiS09.003.

Proteomic databases

PRIDEiQ9N2I7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi493787.
KEGGifca:493787.

Organism-specific databases

CTDi1803.

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
HOVERGENiHBG005527.
InParanoidiQ9N2I7.
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_N.
[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]
ProtoNetiSearch...

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: November 2, 2016
This is version 102 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.