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P81425

- DPP4_BOVIN

UniProt

P81425 - DPP4_BOVIN

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Protein
Dipeptidyl peptidase 4
Gene
DPP4, CD26
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.

Enzyme regulationi

Inhibited by GPC3 and diprotin A By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei629 – 6291Charge relay system By similarity
Active sitei707 – 7071Charge relay system By similarity
Active sitei739 – 7391Charge relay system By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. dipeptidyl-peptidase activity Source: UniProtKB
  3. protease binding Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB
  5. receptor binding Source: UniProtKB
  6. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. T cell costimulation Source: UniProtKB
  2. cell adhesion Source: UniProtKB-KW
  3. endothelial cell migration Source: UniProtKB
  4. negative regulation of extracellular matrix disassembly Source: UniProtKB
  5. positive regulation of cell proliferation 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:3.4.14.5)
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; Single-pass type II membrane protein By similarity. Apical cell membrane; Single-pass type II membrane protein By similarity. Cell projectioninvadopodium membrane; Single-pass type II membrane protein By similarity. Cell projectionlamellipodium membrane; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini30 – 765736Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. cell junction Source: UniProtKB-SubCell
  3. cell surface Source: UniProtKB
  4. endocytic vesicle Source: UniProtKB
  5. extracellular region Source: UniProtKB-SubCell
  6. integral component of membrane Source: UniProtKB-KW
  7. invadopodium membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. lamellipodium membrane Source: UniProtKB-SubCell
  10. membrane raft Source: UniProtKB-SubCell
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 form
PRO_0000027209Add
BLAST
Chaini38 – 765728Dipeptidyl peptidase 4 soluble form By similarity
PRO_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...) Reviewed prediction
Glycosylationi218 – 2181N-linked (GlcNAc...) By similarity
Glycosylationi228 – 2281N-linked (GlcNAc...) By similarity
Glycosylationi271 – 2711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi280 – 2801N-linked (GlcNAc...) By similarity
Glycosylationi320 – 3201N-linked (GlcNAc...) By similarity
Disulfide bondi384 ↔ 393 By similarity
Glycosylationi392 – 3921N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi443 ↔ 446 By similarity
Disulfide bondi453 ↔ 471 By similarity
Glycosylationi495 – 4951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi648 ↔ 761 By 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.

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.

Structurei

3D structure databases

ProteinModelPortaliP81425.
SMRiP81425. Positions 38-764.

Family & Domainsi

Sequence similaritiesi

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

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MKTPWKVLLG LLAIAALVTV ITVPVVLLTK GNDASTDSRR TYTLADYLKN    50
TFRMKFYNLR WVSDHEYLYK QENNILLFNA EYGNSSIFLE NSTFDEFGHS 100
INDYSVSPDR QYILFEYNYV KQWRHSYTAS YDIYDLNKRQ LITEERIPNN 150
TQWITWSSVG HKLAYVWNND IYVKNEPNSP SQRITWTGKK DVIYNGITDW 200
VYEEEVFSAY SALWWSPNST FLAYAQFNDT EVPLIEYSFY SDESLQYPKT 250
VKIPYPKAGA VNPTIKFFVV NISSLSPNIN ATSQQIVPPG SVLIGDHYLC 300
DVTWVTEERI SLQWLRRIQN YSIMDICDYD RSTGRWISSV GRQHIEISTT 350
GWVGRFRPAE PHFTSDGNSF YKIISNEEGY KHICHFQTDK RNCTFITKGA 400
WEVIGIEALT SDYLYYISNE YKGMPGARNL YKIQLNDYTK VTCLSCELNP 450
DRCQYYSVSF SQEAKYYQLR CSGPGLPLYT LHNSNNDKEL RVLENNSDLD 500
QVLQDVQMPS KKLDFIHLHG TKFWYQMILP PHFDKSKKYP LLLEVYAGPC 550
SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAINRRLGTF 600
EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI 650
AVAPVSKWEY YDSVYTERYM GLPTPEDNLD SYRNSTVMSR AENFKQVEYL 700
LIHGTADDNV HFQQSAQISK ALVDAGVDFQ SMWYTDEDHG IASSTAHQHI 750
YTHMSHFLKQ CFSLL 765
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: June 11, 2014
This is version 108 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

Similar proteinsi