Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.By similarity1 Publication

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 sitei630Charge relay systemPROSITE-ProRule annotation1
Active sitei708Charge relay systemPROSITE-ProRule annotation1
Active sitei740Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease, Serine protease
Biological processCell adhesion

Enzyme and pathway databases

BRENDAi3.4.14.5 6170
ReactomeiR-SSC-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-SSC-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)

Protein family/group databases

ESTHERisussc-dpp4 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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 15

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini28 – 766ExtracellularSequence analysisAdd BLAST739

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3813

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000272171 – 766Dipeptidyl peptidase 4 membrane formAdd BLAST766
ChainiPRO_000002721838 – 766Dipeptidyl peptidase 4 soluble formAdd BLAST729

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi85N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi92N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi229N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi279N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi321N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Disulfide bondi649 ↔ 762
Glycosylationi685N-linked (GlcNAc...) asparagine1 Publication1

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.
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

PaxDbiP22411
PeptideAtlasiP22411
PRIDEiP22411

PTM databases

iPTMnetiP22411

Expressioni

Gene expression databases

BgeeiENSSSCG00000015894
ExpressionAtlasiP22411 baseline and differential
GenevisibleiP22411 SS

Interactioni

Subunit structurei

Monomer. Homodimer (PubMed:12690074). Heterodimer with Seprase (FAP) (By similarity). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation (By similarity). Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (By similarity). Associates with collagen (By similarity). Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes (By similarity). Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity (By similarity). Interacts with CAV1 (via the N-terminus); the interaction is direct (By similarity). Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11 (By similarity). Interacts with IGF2R; the interaction is direct (By similarity). Interacts with GPC3 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028692

Chemistry databases

BindingDBiP22411

Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 50Combined sources6
Beta strandi60 – 62Combined sources3
Beta strandi64 – 72Combined sources9
Beta strandi75 – 80Combined sources6
Turni81 – 83Combined sources3
Beta strandi87 – 90Combined sources4
Helixi92 – 96Combined sources5
Beta strandi98 – 100Combined sources3
Beta strandi104 – 107Combined sources4
Beta strandi111 – 122Combined sources12
Beta strandi124 – 126Combined sources3
Beta strandi128 – 136Combined sources9
Turni137 – 140Combined sources4
Beta strandi152 – 157Combined sources6
Beta strandi159 – 162Combined sources4
Beta strandi164 – 168Combined sources5
Beta strandi171 – 177Combined sources7
Turni191 – 193Combined sources3
Beta strandi194 – 198Combined sources5
Helixi201 – 206Combined sources6
Beta strandi209 – 212Combined sources4
Beta strandi214 – 216Combined sources3
Beta strandi220 – 229Combined sources10
Beta strandi235 – 240Combined sources6
Beta strandi250 – 255Combined sources6
Beta strandi265 – 272Combined sources8
Helixi273 – 275Combined sources3
Beta strandi283 – 287Combined sources5
Helixi291 – 294Combined sources4
Beta strandi298 – 307Combined sources10
Beta strandi310 – 317Combined sources8
Beta strandi320 – 330Combined sources11
Turni332 – 334Combined sources3
Helixi341 – 343Combined sources3
Beta strandi344 – 348Combined sources5
Beta strandi350 – 352Combined sources3
Beta strandi354 – 358Combined sources5
Beta strandi368 – 376Combined sources9
Beta strandi378 – 380Combined sources3
Beta strandi382 – 388Combined sources7
Beta strandi394 – 397Combined sources4
Beta strandi400 – 402Combined sources3
Beta strandi404 – 410Combined sources7
Beta strandi412 – 420Combined sources9
Helixi422 – 424Combined sources3
Beta strandi429 – 435Combined sources7
Beta strandi438 – 446Combined sources9
Turni447 – 449Combined sources3
Turni451 – 453Combined sources3
Beta strandi456 – 461Combined sources6
Beta strandi465 – 472Combined sources8
Beta strandi474 – 477Combined sources4
Beta strandi479 – 484Combined sources6
Turni485 – 488Combined sources4
Beta strandi489 – 495Combined sources7
Helixi498 – 504Combined sources7
Beta strandi506 – 508Combined sources3
Beta strandi511 – 519Combined sources9
Beta strandi522 – 530Combined sources9
Beta strandi536 – 538Combined sources3
Beta strandi540 – 546Combined sources7
Helixi563 – 569Combined sources7
Beta strandi574 – 578Combined sources5
Beta strandi584 – 586Combined sources3
Helixi588 – 591Combined sources4
Helixi592 – 594Combined sources3
Turni598 – 600Combined sources3
Helixi601 – 614Combined sources14
Beta strandi619 – 629Combined sources11
Helixi631 – 640Combined sources10
Turni641 – 643Combined sources3
Beta strandi648 – 654Combined sources7
Helixi659 – 661Combined sources3
Helixi664 – 671Combined sources8
Turni676 – 679Combined sources4
Helixi680 – 684Combined sources5
Helixi689 – 697Combined sources9
Beta strandi698 – 705Combined sources8
Beta strandi709 – 711Combined sources3
Helixi713 – 725Combined sources13
Beta strandi731 – 735Combined sources5
Helixi745 – 762Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ORVX-ray1.80A/B/C/D39-766[»]
1ORWX-ray2.84A/B/C/D39-766[»]
2AJ8X-ray2.11A/B/C/D39-766[»]
2AJBX-ray2.75A/B/C/D39-766[»]
2AJCX-ray1.95A/B/C/D39-766[»]
2AJDX-ray2.56A/B/C/D39-766[»]
2BUAX-ray2.56A/B/C/D39-766[»]
2BUCX-ray2.50A/B/C/D39-766[»]
5LLSX-ray2.41A/B/C/D1-766[»]
ProteinModelPortaliP22411
SMRiP22411
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22411

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
GeneTreeiENSGT00760000119233
HOGENOMiHOG000231875
HOVERGENiHBG005527
InParanoidiP22411
KOiK01278
OMAiQFILLEY
OrthoDBiEOG091G0BU5
TreeFamiTF313309

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00708 PRO_ENDOPEP_SER, 1 hit

Sequencei

Sequence statusi: Complete.

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

P22411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GTDDAAADSR RTYTLTDYLK
60 70 80 90 100
STFRVKFYTL QWISDHEYLY KQENNILLFN AEYGNSSIFL ENSTFDELGY
110 120 130 140 150
STNDYSVSPD RQFILFEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN
160 170 180 190 200
NTQWITWSPV GHKLAYVWNN DIYVKNEPNL SSQRITWTGK ENVIYNGVTD
210 220 230 240 250
WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK
260 270 280 290 300
TVRIPYPKAG AENPTVKFFV VDTRTLSPNA SVTSYQIVPP ASVLIGDHYL
310 320 330 340 350
CGVTWVTEER ISLQWIRRAQ NYSIIDICDY DESTGRWISS VARQHIEIST
360 370 380 390 400
TGWVGRFRPA EPHFTSDGNS FYKIISNEEG YKHICHFQTD KSNCTFITKG
410 420 430 440 450
AWEVIGIEAL TSDYLYYISN EHKGMPGGRN LYRIQLNDYT KVTCLSCELN
460 470 480 490 500
PERCQYYSAS FSNKAKYYQL RCFGPGLPLY TLHSSSSDKE LRVLEDNSAL
510 520 530 540 550
DKMLQDVQMP SKKLDVINLH GTKFWYQMIL PPHFDKSKKY PLLIEVYAGP
560 570 580 590 600
CSQKVDTVFR LSWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
610 620 630 640 650
FEVEDQIEAT RQFSKMGFVD DKRIAIWGWS YGGYVTSMVL GAGSGVFKCG
660 670 680 690 700
IAVAPVSKWE YYDSVYTERY MGLPTPEDNL DYYRNSTVMS RAENFKQVEY
710 720 730 740 750
LLIHGTADDN VHFQQSAQLS KALVDAGVDF QTMWYTDEDH GIASNMAHQH
760
IYTHMSHFLK QCFSLP
Length:766
Mass (Da):88,242
Last modified:September 13, 2004 - v3
Checksum:i8800D520BAEA856D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32Missing (PubMed:7903569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY198323 mRNA Translation: AAO43404.1
X73276 mRNA Translation: CAA51717.1
PIRiI47134
S14746
RefSeqiNP_999422.1, NM_214257.1
UniGeneiSsc.16236

Genome annotation databases

EnsembliENSSSCT00000017306; ENSSSCP00000016843; ENSSSCG00000015894
GeneIDi397492
KEGGissc:397492

Similar proteinsi

Entry informationi

Entry nameiDPP4_PIG
AccessioniPrimary (citable) accession number: P22411
Secondary accession number(s): Q866G2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 13, 2004
Last modified: May 23, 2018
This is version 150 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health