Protein detail

DPP4

Dipeptidyl peptidase 4 (EC 3.4.14.5) (ADABP) (Adenosine deaminase complexing protein 2) (ADCP-2) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]

Protein symbol
DPP4
UniProt ID
EVMP score
0.38
Frequency
Transmembrane count
1
Protein classification
CD markersEnzymesFDA approved drug targetsPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters
Basic Information
Protein Names
Dipeptidyl peptidase 4 (EC 3.4.14.5) (ADABP) (Adenosine deaminase complexing protein 2) (ADCP-2) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidase IV soluble form)]
Protein Class
CD markersEnzymesFDA approved drug targetsPlasma proteinsPredicted intracellular proteinsPredicted secreted proteinsTransporters
Protein Function
  • Predicted intracellular proteins
  • CD markers
  • Peptidases:Serine-type peptidases
  • Enzymes
  • Predicted secreted proteins
  • ENZYME proteins:Hydrolases
  • Transporters:Accessory Factors Involved in Transport
  • FDA approved drug targets:Small molecule drugs
Transmembrane
7..28; Helical; Signal-anchor for type II membrane protein
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
ADCP2CD26DPPIV
Gene Description
Dipeptidyl peptidase 4
Chromosome
2
Position
161992245-162074394
EVMP Score
0.38
Fluorescence & Localization
Tissue Specificsalivary glandBrain Regional SpecificcerebellumCell SpecificBreast hormone-responsive cellsSingle-Nuclei Brain Specificupper rhombic lipBlood Cell Specificplasmacytoid DCBlood Lineage Specificdendritic cells
Function & Pathway
Protein Function
  • Predicted intracellular proteins
  • CD markers
  • Peptidases:Serine-type peptidases
  • Enzymes
  • Predicted secreted proteins
  • ENZYME proteins:Hydrolases
  • Transporters:Accessory Factors Involved in Transport
  • FDA approved drug targets:Small molecule drugs
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

41 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorCellPhoneDBNoYesYesNoNo
receptorreceptorGO_IntercellNoYesYesNoNo
receptorreceptorCellTalkDBNoYesYesNoNo
receptorreceptorRamilowski2015NoYesYesNoNo
receptorreceptorLRdbNoYesYesNoNo
receptorreceptorBaccin2019NoYesYesNoNo
receptorreceptorOmniPathNoYesYesNoNo
extracellularextracellularOmniPathNoNoYesNoNo
intracellularintracellularComPPINoNoYesNoNo
intracellularintracellularGO_IntercellNoNoYesNoNo
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Regulatory Interaction Network

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
GPC3P51654DPP4P27487YesNoYesSIGNORSIGNOR:17549790

Protein Complex Composition

2 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
DPP4IGHG1P01857P274871:2PDBPDB:9jmm
DPP4P274872PDBPDB:4a5sPDB:2jidPDB:1tkrPDB:3opmPDB:2p8sPDB:3kwfPDB:3eioPDB:3q8wPDB:5t4fPDB:5j3jPDB:2ajlPDB:3habPDB:2oqiPDB:2iitPDB:4dsaPDB:3vjkPDB:4n8ePDB:3bjmPDB:3vjlPDB:4dszPDB:1x70PDB:3swwPDB:2oqvPDB:3wqhPDB:1tk3PDB:9carPDB:1wcyPDB:3oc0PDB:5t4hPDB:3o95PDB:2g5pPDB:4pnzPDB:3o9vPDB:2g5tPDB:5y7hPDB:3d4lPDB:3vjmPDB:2ogzPDB:3c43PDB:3g0cPDB:5t4bPDB:4dtcPDB:3g0gPDB:2qoePDB:4n8dPDB:9gohPDB:1r9mPDB:3w2tPDB:3c45PDB:1j2ePDB:2qkyPDB:2oagPDB:3sx4PDB:5kbyPDB:3q0tPDB:2i78PDB:3h0cPDB:3cccPDB:3qbjPDB:5y7kPDB:9lbtPDB:2bubPDB:6b1ePDB:5t4ePDB:4jh0PDB:4pv7PDB:4g1fPDB:4j3jPDB:2i03PDB:9d56PDB:1u8ePDB:2qjrPDB:2rguPDB:3g0bPDB:3g0dPDB:3ccbPDB:1rwqPDB:2fjpPDB:2iivPDB:2qt9PDB:2hhaPDB:4lkoPDB:1pfqPDB:5ismPDB:5y7jPDB:2qtbPDB:2g63PDB:1nu8PDB:1nu6PDB:6b1oPDB:3hacPDB:1n1mPDB:5zidPDB:2olePDB:2oncPDB:2ophPDB:3kwjPDB:3noxPDB:5i7uPDB:3f8s

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Mass spectrometry [LTQ-FT Ultra]Mass spectrometry0
Sequence, Structure & Domains

Sequences

Length
766
Mass
88,279
Sequence
MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP

3D Structural Models

Turn
81..83; 92..97; 137..140; 191..193; 332..334; 447..449; 451..453; 485..488; 598..600; 615..617; 641..643; 676..679
Helix
45..50; 201..206; 273..275; 291..294; 341..343; 422..424; 498..504; 563..569; 588..591; 592..594; 601..614; 631..640; 659..661; 664..671; 680..685; 689..697; 714..725; 745..762
Beta Strand
40..42; 60..62; 64..72; 75..80; 86..90; 98..100; 104..107; 111..122; 124..126; 128..136; 141..143; 152..157; 159..162; 164..168; 171..177; 194..198; 208..212; 214..216; 220..229; 231..233; 235..240; 243..245; 250..255; 265..272; 278..280; 284..287; 298..307; 310..319; 322..330; 337..339; 345..348; 350..352; 354..358; 362..364; 368..376; 378..380; 382..388; 391..393; 395..397; 400..402; 404..410; 412..420; 429..435; 438..446; 456..461; 465..472; 474..477; 479..484; 489..495; 506..508; 511..519; 522..530; 536..538; 540..545; 574..578; 584..586; 619..629; 648..654; 698..705; 709..711; 731..735
3D Structure
Electron microscopy (5); X-ray crystallography (109)

Domain & Motif Annotations

Domain (CC)
The extracellular cysteine-rich region is necessary for association with collagen, dimer formation and optimal dipeptidyl peptidase activity.
Protein Families
  • Peptidase S9B family
  • DPPIV subfamily
Sequence Similarities
Belongs to the peptidase S9B family. DPPIV subfamily.
Clinical Relevance