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P22411

- DPP4_PIG

UniProt

P22411 - DPP4_PIG

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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- 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.By similarityPROSITE-ProRule annotation

Enzyme regulationi

Inhibited by GPC3 and diprotin A.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei630 – 6301Charge relay systemPROSITE-ProRule annotation
Active sitei708 – 7081Charge relay systemPROSITE-ProRule annotation
Active sitei740 – 7401Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  1. dipeptidyl-peptidase activity Source: UniProtKB
  2. protease binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB
  4. receptor binding Source: UniProtKB
  5. 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. regulation of cell-cell adhesion mediated by integrin Source: Ensembl
  6. response to hypoxia Source: Ensembl
  7. T cell activation Source: Ensembl
  8. T cell costimulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BRENDAi3.4.14.5. 6170.
ReactomeiREACT_209721. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_225961. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).

Protein family/group databases

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
ProteomesiUP000008227: Chromosome 15

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 766739ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cell surface Source: UniProtKB
  3. endocytic vesicle Source: UniProtKB
  4. extracellular vesicular exosome Source: Ensembl
  5. integral component of membrane Source: UniProtKB-KW
  6. intercellular canaliculus Source: Ensembl
  7. invadopodium membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. lysosomal membrane Source: Ensembl
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 – 766766Dipeptidyl peptidase 4 membrane formPRO_0000027217Add
BLAST
Chaini38 – 766729Dipeptidyl peptidase 4 soluble formPRO_0000027218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)1 Publication
Glycosylationi92 – 921N-linked (GlcNAc...)1 Publication
Glycosylationi229 – 2291N-linked (GlcNAc...)1 Publication
Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
Glycosylationi321 – 3211N-linked (GlcNAc...)1 Publication
Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Disulfide bondi649 ↔ 762
Glycosylationi685 – 6851N-linked (GlcNAc...)1 Publication

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.

Interactioni

Subunit structurei

Monomer. 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). Homodimer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000016843.

Structurei

Secondary structure

1
766
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 506Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 729Combined sources
Beta strandi75 – 806Combined sources
Turni81 – 833Combined sources
Beta strandi87 – 904Combined sources
Helixi92 – 965Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi111 – 12212Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1369Combined sources
Turni137 – 1404Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi171 – 1777Combined sources
Turni191 – 1933Combined sources
Beta strandi194 – 1985Combined sources
Helixi201 – 2066Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi220 – 22910Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi265 – 2728Combined sources
Helixi273 – 2753Combined sources
Beta strandi283 – 2875Combined sources
Helixi291 – 2944Combined sources
Beta strandi298 – 30710Combined sources
Beta strandi310 – 3178Combined sources
Beta strandi320 – 33011Combined sources
Turni332 – 3343Combined sources
Helixi341 – 3433Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi368 – 3769Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi382 – 3887Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi400 – 4023Combined sources
Beta strandi404 – 4107Combined sources
Beta strandi412 – 4209Combined sources
Helixi422 – 4243Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi438 – 4469Combined sources
Turni447 – 4493Combined sources
Turni451 – 4533Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi465 – 4728Combined sources
Beta strandi474 – 4774Combined sources
Beta strandi479 – 4846Combined sources
Turni485 – 4884Combined sources
Beta strandi489 – 4957Combined sources
Helixi498 – 5047Combined sources
Beta strandi506 – 5083Combined sources
Beta strandi511 – 5199Combined sources
Beta strandi522 – 5309Combined sources
Beta strandi536 – 5383Combined sources
Beta strandi540 – 5467Combined sources
Helixi563 – 5697Combined sources
Beta strandi574 – 5785Combined sources
Beta strandi584 – 5863Combined sources
Helixi588 – 5914Combined sources
Helixi592 – 5943Combined sources
Turni598 – 6003Combined sources
Helixi601 – 61414Combined sources
Beta strandi619 – 62911Combined sources
Helixi631 – 64010Combined sources
Turni641 – 6433Combined sources
Beta strandi648 – 6547Combined sources
Helixi659 – 6613Combined sources
Helixi664 – 6718Combined sources
Turni676 – 6794Combined sources
Helixi680 – 6845Combined sources
Helixi689 – 6979Combined sources
Beta strandi698 – 7058Combined sources
Beta strandi709 – 7113Combined sources
Helixi713 – 72513Combined sources
Beta strandi731 – 7355Combined sources
Helixi745 – 76218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP22411.
SMRiP22411. Positions 39-766.
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

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP22411.
KOiK01278.
OMAiETKFWYQ.
OrthoDBiEOG761BT2.
TreeFamiTF313309.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321Missing(PubMed:7903569)Curated

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.
ENSSSCT00000035225; ENSSSCP00000028692; ENSSSCG00000015894.
GeneIDi397492.
KEGGissc:397492.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY198323 mRNA. Translation: AAO43404.1 .
X73276 mRNA. Translation: CAA51717.1 .
PIRi I47134.
S14746.
RefSeqi NP_999422.1. NM_214257.1.
UniGenei Ssc.16236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ORV X-ray 1.80 A/B/C/D 39-766 [» ]
1ORW X-ray 2.84 A/B/C/D 39-766 [» ]
2AJ8 X-ray 2.11 A/B/C/D 39-766 [» ]
2AJB X-ray 2.75 A/B/C/D 39-766 [» ]
2AJC X-ray 1.95 A/B/C/D 39-766 [» ]
2AJD X-ray 2.56 A/B/C/D 39-766 [» ]
2BUA X-ray 2.56 A/B/C/D 39-766 [» ]
2BUC X-ray 2.50 A/B/C/D 39-766 [» ]
ProteinModelPortali P22411.
SMRi P22411. Positions 39-766.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000016843.

Chemistry

BindingDBi P22411.
ChEMBLi CHEMBL3813.

Protein family/group databases

MEROPSi S09.003.

Proteomic databases

PaxDbi P22411.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000017306 ; ENSSSCP00000016843 ; ENSSSCG00000015894 .
ENSSSCT00000035225 ; ENSSSCP00000028692 ; ENSSSCG00000015894 .
GeneIDi 397492.
KEGGi ssc:397492.

Organism-specific databases

CTDi 1803.

Phylogenomic databases

eggNOGi COG1506.
GeneTreei ENSGT00760000119233.
HOGENOMi HOG000231875.
HOVERGENi HBG005527.
InParanoidi P22411.
KOi K01278.
OMAi ETKFWYQ.
OrthoDBi EOG761BT2.
TreeFami TF313309.

Enzyme and pathway databases

BRENDAi 3.4.14.5. 6170.
Reactomei REACT_209721. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
REACT_225961. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).

Miscellaneous databases

EvolutionaryTracei P22411.

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. "Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme."
    Baer J., Weber A., Hoffmann T., Stork J., Wermann M., Wagner L., Aust S., Gerhartz B., Demuth H.-U.
    Biol. Chem. 384:1553-1563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Kidney.
  2. "Assignment of the dipeptidylpeptidase IV (DPP4) gene to pig chromosome 15q21."
    Thomsen P.D., Qvist H., Marklund L., Andersson L., Sjostrom H., Noren O.
    Mamm. Genome 4:604-607(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-67.
    Tissue: Kidney.
  3. "N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV solubilized by autolysis."
    Seidl R., Mann K., Schaeffer W.
    Biol. Chem. Hoppe-Seyler 372:213-214(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-71.
    Tissue: Kidney.
  4. "The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism."
    Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., Huber R., Bode W., Demuth H.-U., Brandstetter H.
    Proc. Natl. Acad. Sci. U.S.A. 100:5063-5068(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; ASN-92; ASN-229; ASN-279; ASN-321 AND ASN-685, HOMODIMERIZATION.

Entry informationi

Entry nameiDPP4_PIG
AccessioniPrimary (citable) accession number: P22411
Secondary accession number(s): Q866G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 13, 2004
Last modified: November 26, 2014
This is version 123 of the entry and version 3 of the sequence. [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

External Data

Dasty 3