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P81425

- DPP4_BOVIN

UniProt

P81425 - DPP4_BOVIN

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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Bos taurus (Bovine)
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. 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.By similarityPROSITE-ProRule annotation

Enzyme regulationi

Inhibited by GPC3 and diprotin A.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei629 – 6291Charge relay systemPROSITE-ProRule annotation
Active sitei707 – 7071Charge relay systemPROSITE-ProRule annotation
Active sitei739 – 7391Charge 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. T cell costimulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease

Keywords - Biological processi

Cell adhesion

Protein family/group databases

MEROPSiS09.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5By similarity)
Alternative name(s):
Activation molecule 3
Short name:
ACT3
Adenosine deaminase complexing protein
Short name:
ADCP-I
Dipeptidyl peptidase IV
Short name:
DPP IV
T-cell activation antigen CD26
WC10
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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Chain Dipeptidyl peptidase 4 soluble form : Secreted
Note: Detected in the serum and the seminal fluid.By similarity
Cell membrane By similarity; Single-pass type II membrane protein By similarity. 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

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell surface Source: UniProtKB
  3. endocytic vesicle Source: UniProtKB
  4. extracellular region Source: UniProtKB-KW
  5. integral component of membrane Source: UniProtKB-KW
  6. invadopodium membrane Source: UniProtKB
  7. lamellipodium Source: UniProtKB
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 – 765765Dipeptidyl peptidase 4 membrane formPRO_0000027209Add
BLAST
Chaini38 – 765728Dipeptidyl peptidase 4 soluble formBy similarityPRO_0000027210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)By similarity
Glycosylationi91 – 911N-linked (GlcNAc...)By similarity
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)By similarity
Glycosylationi228 – 2281N-linked (GlcNAc...)By similarity
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)By similarity
Glycosylationi320 – 3201N-linked (GlcNAc...)By similarity
Disulfide bondi384 ↔ 393By similarity
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi443 ↔ 446By similarity
Disulfide bondi453 ↔ 471By similarity
Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi648 ↔ 761By similarity
Glycosylationi684 – 6841N-linked (GlcNAc...)By similarity

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

PRIDEiP81425.

Expressioni

Tissue specificityi

Intestinal epithelium, dendritic cells and several immune system tissues.

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

Structurei

3D structure databases

ProteinModelPortaliP81425.
SMRiP81425. Positions 38-764.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini30 – 765736ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP81425.
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.
[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.

P81425-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTPWKVLLG LLAIAALVTV ITVPVVLLTK GNDASTDSRR TYTLADYLKN
60 70 80 90 100
TFRMKFYNLR WVSDHEYLYK QENNILLFNA EYGNSSIFLE NSTFDEFGHS
110 120 130 140 150
INDYSVSPDR QYILFEYNYV KQWRHSYTAS YDIYDLNKRQ LITEERIPNN
160 170 180 190 200
TQWITWSSVG HKLAYVWNND IYVKNEPNSP SQRITWTGKK DVIYNGITDW
210 220 230 240 250
VYEEEVFSAY SALWWSPNST FLAYAQFNDT EVPLIEYSFY SDESLQYPKT
260 270 280 290 300
VKIPYPKAGA VNPTIKFFVV NISSLSPNIN ATSQQIVPPG SVLIGDHYLC
310 320 330 340 350
DVTWVTEERI SLQWLRRIQN YSIMDICDYD RSTGRWISSV GRQHIEISTT
360 370 380 390 400
GWVGRFRPAE PHFTSDGNSF YKIISNEEGY KHICHFQTDK RNCTFITKGA
410 420 430 440 450
WEVIGIEALT SDYLYYISNE YKGMPGARNL YKIQLNDYTK VTCLSCELNP
460 470 480 490 500
DRCQYYSVSF SQEAKYYQLR CSGPGLPLYT LHNSNNDKEL RVLENNSDLD
510 520 530 540 550
QVLQDVQMPS KKLDFIHLHG TKFWYQMILP PHFDKSKKYP LLLEVYAGPC
560 570 580 590 600
SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAINRRLGTF
610 620 630 640 650
EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI
660 670 680 690 700
AVAPVSKWEY YDSVYTERYM GLPTPEDNLD SYRNSTVMSR AENFKQVEYL
710 720 730 740 750
LIHGTADDNV HFQQSAQISK ALVDAGVDFQ SMWYTDEDHG IASSTAHQHI
760
YTHMSHFLKQ CFSLL
Length:765
Mass (Da):88,369
Last modified:July 26, 2002 - v3
Checksum:iE32165421F43E116
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF461806 mRNA. Translation: AAL67836.1.
AY056834 mRNA. Translation: AAL23628.1.
BC102523 mRNA. Translation: AAI02524.1.
RefSeqiNP_776464.1. NM_174039.2.
UniGeneiBt.8282.

Genome annotation databases

GeneIDi281122.
KEGGibta:281122.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF461806 mRNA. Translation: AAL67836.1 .
AY056834 mRNA. Translation: AAL23628.1 .
BC102523 mRNA. Translation: AAI02524.1 .
RefSeqi NP_776464.1. NM_174039.2.
UniGenei Bt.8282.

3D structure databases

ProteinModelPortali P81425.
SMRi P81425. Positions 38-764.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P81425.
ChEMBLi CHEMBL2559.

Protein family/group databases

MEROPSi S09.003.

Proteomic databases

PRIDEi P81425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281122.
KEGGi bta:281122.

Organism-specific databases

CTDi 1803.

Phylogenomic databases

eggNOGi COG1506.
HOGENOMi HOG000231875.
HOVERGENi HBG005527.
InParanoidi P81425.
KOi K01278.

Miscellaneous databases

NextBioi 20805190.

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

« Hide 'large scale' publications
  1. "Molecular characterization of bovine CD26 upregulated by a staphylococcal superantigen."
    Lee S.-U., Park Y.-H., Davis W.C., Hamilton M.J., Naessens J., Bohach G.A.
    Immunogenetics 54:216-220(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphocyte.
  2. "CD26 is expressed on a restricted subpopulation of dendritic cells in vivo."
    Gliddon D.R., Howard C.J.
    Eur. J. Immunol. 32:1472-1481(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17.
    Tissue: Thymus.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  4. "Identity of activation molecule 3 on superantigen-stimulated bovine cells is CD26."
    Lee S.-U., Ferens W., Davis W.C., Hamilton M.J., Park Y.-H., Fox L.K., Naessens J., Bohach G.A.
    Infect. Immun. 69:7190-7193(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-24.
    Tissue: T-cell.
  5. "The CP-I subunit of adenosine deaminase complexing protein from calf kidney is identical to human, mouse, and rat dipeptidyl peptidase IV."
    Ben-Shooshan I., Parola A.H.
    Comp. Biochem. Physiol. 119B:289-292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 537-546.
    Tissue: Kidney.

Entry informationi

Entry nameiDPP4_BOVIN
AccessioniPrimary (citable) accession number: P81425
Secondary accession number(s): Q3ZCC2, Q8WMG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 26, 2002
Last modified: October 29, 2014
This is version 110 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3