UniProtKB - P14740 (DPP4_RAT)
Dipeptidyl peptidase 4
Dpp4
Functioni
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
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 631 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 709 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 741 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- chemorepellent activity Source: RGD
- collagen binding Source: RGD
- dipeptidyl-peptidase activity Source: RGD
- identical protein binding Source: RGD
- peptide binding Source: RGD
- protease binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- serine-type endopeptidase activity Source: RGD
- serine-type peptidase activity Source: RGD
- signaling receptor binding Source: UniProtKB
- virus receptor activity Source: RGD
GO - Biological processi
- behavioral fear response Source: RGD
- cell adhesion Source: UniProtKB-KW
- endothelial cell migration Source: UniProtKB
- establishment of localization Source: RGD
- locomotory exploration behavior Source: RGD
- negative regulation of extracellular matrix disassembly Source: UniProtKB
- negative regulation of neutrophil chemotaxis Source: RGD
- positive regulation of cell population proliferation Source: UniProtKB
- proteolysis Source: RGD
- psychomotor behavior Source: RGD
- regulation of cell-cell adhesion mediated by integrin Source: RGD
- regulation of T cell mediated immunity Source: RGD
- response to hypoxia Source: RGD
- T cell activation Source: RGD
- T cell costimulation Source: UniProtKB
Keywordsi
Molecular function | Aminopeptidase, Hydrolase, Protease, Serine protease |
Biological process | Cell adhesion |
Enzyme and pathway databases
BRENDAi | 3.4.14.5, 5301 |
Reactomei | R-RNO-381771, Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) R-RNO-400511, Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) |
Protein family/group databases
ESTHERi | ratno-dpp4, DPP4N_Peptidase_S9 |
MEROPSi | S09.003 |
Names & Taxonomyi
Protein namesi | Recommended name: Dipeptidyl peptidase 4 (EC:3.4.14.5By similarity)Alternative name(s): Bile canaliculus domain-specific membrane glycoprotein Dipeptidyl peptidase IV Short name: DPP IV GP110 glycoprotein T-cell activation antigen CD26 CD_antigen: CD26 Cleaved into the following 3 chains: Alternative name(s): Dipeptidyl peptidase IV membrane form Alternative name(s): Dipeptidyl peptidase IV soluble form Alternative name(s): Dipeptidyl peptidase IV 60 kDa soluble form |
Gene namesi | Name:Dpp4 Synonyms:Cd26 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2515, Dpp4 |
Subcellular locationi
Extracellular region or secreted
Note: Detected in the serum and the seminal fluid.By similarity
Plasma membrane
- Cell membrane ; Single-pass type II membrane protein
- Apical cell membrane By similarity; Single-pass type II membrane protein By similarity
- invadopodium membrane By similarity; Single-pass type II membrane protein By similarity
- lamellipodium membrane By similarity; Single-pass type II membrane protein By similarity
Other locations
- 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 an 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
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: RGD
Plasma Membrane
- apical plasma membrane Source: RGD
- invadopodium membrane Source: UniProtKB
- lamellipodium membrane Source: UniProtKB-SubCell
- plasma membrane Source: RGD
Other locations
- cell surface Source: RGD
- endocytic vesicle Source: UniProtKB
- integral component of membrane Source: UniProtKB-KW
- intercellular canaliculus Source: RGD
- lamellipodium Source: UniProtKB
- membrane raft Source: UniProtKB-SubCell
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 6 | CytoplasmicSequence analysis | 6 | |
Transmembranei | 7 – 28 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 22 | |
Topological domaini | 29 – 767 | ExtracellularSequence analysisAdd BLAST | 739 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Membrane, SecretedPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 629 | G → A: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 629 | G → R: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 630 | W → E: No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 631 | S → A: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 632 | Y → F: No effect on activity. 1 Publication | 1 | |
Mutagenesisi | 632 | Y → G: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 632 | Y → L: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 633 | G → A: Reduced activity. 1 Publication | 1 | |
Mutagenesisi | 633 | G → S: Reduced activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4653 |
DrugCentrali | P14740 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000027219 | 1 – 767 | Dipeptidyl peptidase 4 membrane formAdd BLAST | 767 | |
ChainiPRO_0000027220 | 37 – 767 | Dipeptidyl peptidase 4 soluble formAdd BLAST | 731 | |
ChainiPRO_0000027221 | 281 – 767 | Dipeptidyl peptidase 4 60 kDa soluble formAdd BLAST | 487 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 83 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 90 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 148 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 217 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 227 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 319 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 326 ↔ 337 | 1 Publication | ||
Disulfide bondi | 383 ↔ 395 | 1 Publication | ||
Disulfide bondi | 445 ↔ 448 | 1 Publication | ||
Disulfide bondi | 455 ↔ 473 | 1 Publication | ||
Glycosylationi | 521 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 650 ↔ 763 | 1 Publication | ||
Glycosylationi | 686 | N-linked (GlcNAc...) asparagineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | P14740 |
PRIDEi | P14740 |
PTM databases
GlyGeni | P14740, 8 sites |
iPTMneti | P14740 |
PhosphoSitePlusi | P14740 |
SwissPalmi | P14740 |
Expressioni
Tissue specificityi
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 an interleukin-12-dependent manner in activated lymphocytes.
Interacts (via 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 similarityGO - Molecular functioni
- chemorepellent activity Source: RGD
- identical protein binding Source: RGD
- protease binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- signaling receptor binding Source: UniProtKB
Protein-protein interaction databases
IntActi | P14740, 1 interactor |
MINTi | P14740 |
STRINGi | 10116.ENSRNOP00000045536 |
Chemistry databases
BindingDBi | P14740 |
Structurei
Secondary structure
3D structure databases
SMRi | P14740 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14740 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2100, Eukaryota |
InParanoidi | P14740 |
OrthoDBi | 269253at2759 |
PhylomeDBi | P14740 |
Family and domain databases
Gene3Di | 2.140.10.30, 1 hit 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR040522, DPPIV_rep IPR002471, Pept_S9_AS IPR001375, Peptidase_S9 IPR002469, Peptidase_S9B_N IPR038554, Peptidase_S9B_N_sf |
Pfami | View protein in Pfam PF00930, DPPIV_N, 1 hit PF18811, DPPIV_rep, 1 hit PF00326, Peptidase_S9, 1 hit |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00708, PRO_ENDOPEP_SER, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT
60 70 80 90 100
FRVKSYSLRW VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI
110 120 130 140 150
SDYSVSPDRL FVLLEYNYVK QWRHSYTASY SIYDLNKRQL ITEEKIPNNT
160 170 180 190 200
QWITWSQEGH KLAYVWKNDI YVKIEPHLPS HRITSTGKEN VIFNGINDWV
210 220 230 240 250
YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS DESLQYPKTV
260 270 280 290 300
WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD
310 320 330 340 350
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG
360 370 380 390 400
WCGRFRPAEP HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK
410 420 430 440 450
GAWEVISIEA LTSDYLYYIS NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL
460 470 480 490 500
NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL YTLHRSTDQK ELRVLEDNSA
510 520 530 540 550
LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK YPLLIDVYAG
560 570 580 590 600
PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG
610 620 630 640 650
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC
660 670 680 690 700
GIAVAPVSRW EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE
710 720 730 740 750
YLLIHGTADD NVHFQQSAQI SKALVDAGVD FQAMWYTDED HGIASSTAHQ
760
HIYSHMSHFL QQCFSLR
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1M7X5 | F1M7X5_RAT | Dipeptidyl peptidase 4 | Dpp4 | 767 | Annotation score: | ||
A0A0G2K238 | A0A0G2K238_RAT | Dipeptidyl peptidase 4 | Dpp4 | 789 | Annotation score: | ||
A0A0G2JTX5 | A0A0G2JTX5_RAT | Dipeptidyl peptidase 4 | Dpp4 | 767 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 38 | R → A in AAA41096 (PubMed:2563382).Curated | 1 | |
Sequence conflicti | 54 | Missing AA sequence (PubMed:1970322).Curated | 1 | |
Sequence conflicti | 183 | I → T in AAA41272 (PubMed:3479775).Curated | 1 | |
Sequence conflicti | 332 | T → N in AAA41272 (PubMed:3479775).Curated | 1 | |
Sequence conflicti | 352 | C → V in AAA41272 (PubMed:3479775).Curated | 1 | |
Sequence conflicti | 394 | V → D in AAA41272 (PubMed:3479775).Curated | 1 | |
Sequence conflicti | 562 | L → F in AAA41272 (PubMed:3479775).Curated | 1 | |
Sequence conflicti | 624 | R → Q in AAA41272 (PubMed:3479775).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J04591 mRNA Translation: AAA41096.1 J02997 mRNA Translation: AAA41272.1 |
PIRi | A39914 |
RefSeqi | NP_036921.1, NM_012789.1 |
Genome annotation databases
GeneIDi | 25253 |
KEGGi | rno:25253 |
UCSCi | RGD:2515, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J04591 mRNA Translation: AAA41096.1 J02997 mRNA Translation: AAA41272.1 |
PIRi | A39914 |
RefSeqi | NP_036921.1, NM_012789.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2GBC | X-ray | 2.80 | A/B | 38-767 | [»] | |
2GBF | X-ray | 3.10 | A/B | 38-767 | [»] | |
2GBG | X-ray | 3.00 | A/B | 38-767 | [»] | |
2GBI | X-ray | 3.30 | A/B | 38-767 | [»] | |
2I3Z | X-ray | 2.90 | A/B | 38-767 | [»] | |
2OAE | X-ray | 3.00 | A/B | 38-767 | [»] | |
4FFV | X-ray | 2.40 | A/B | 38-767 | [»] | |
4FFW | X-ray | 2.90 | A/B | 38-767 | [»] | |
5VTA | X-ray | 2.80 | A/B/C/D | 37-767 | [»] | |
SMRi | P14740 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P14740, 1 interactor |
MINTi | P14740 |
STRINGi | 10116.ENSRNOP00000045536 |
Chemistry databases
BindingDBi | P14740 |
ChEMBLi | CHEMBL4653 |
DrugCentrali | P14740 |
Protein family/group databases
ESTHERi | ratno-dpp4, DPP4N_Peptidase_S9 |
MEROPSi | S09.003 |
PTM databases
GlyGeni | P14740, 8 sites |
iPTMneti | P14740 |
PhosphoSitePlusi | P14740 |
SwissPalmi | P14740 |
Proteomic databases
PaxDbi | P14740 |
PRIDEi | P14740 |
Protocols and materials databases
ABCDi | P14740, 2 sequenced antibodies |
Genome annotation databases
GeneIDi | 25253 |
KEGGi | rno:25253 |
UCSCi | RGD:2515, rat |
Organism-specific databases
CTDi | 1803 |
RGDi | 2515, Dpp4 |
Phylogenomic databases
eggNOGi | KOG2100, Eukaryota |
InParanoidi | P14740 |
OrthoDBi | 269253at2759 |
PhylomeDBi | P14740 |
Enzyme and pathway databases
BRENDAi | 3.4.14.5, 5301 |
Reactomei | R-RNO-381771, Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) R-RNO-400511, Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) |
Miscellaneous databases
EvolutionaryTracei | P14740 |
PROi | PR:P14740 |
Family and domain databases
Gene3Di | 2.140.10.30, 1 hit 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR040522, DPPIV_rep IPR002471, Pept_S9_AS IPR001375, Peptidase_S9 IPR002469, Peptidase_S9B_N IPR038554, Peptidase_S9B_N_sf |
Pfami | View protein in Pfam PF00930, DPPIV_N, 1 hit PF18811, DPPIV_rep, 1 hit PF00326, Peptidase_S9, 1 hit |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00708, PRO_ENDOPEP_SER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DPP4_RAT | |
Accessioni | P14740Primary (citable) accession number: P14740 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | December 7, 2004 | |
Last modified: | December 2, 2020 | |
This is version 170 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries