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Q9N2I7 (DPP4_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidyl peptidase 4

EC=3.4.14.5
Alternative name(s):
Dipeptidyl peptidase IV
Short name=DPP IV
T-cell activation antigen CD26
CD_antigen=CD26

Cleaved into the following 2 chains:

  1. Dipeptidyl peptidase 4 membrane form
    Alternative name(s):
    Dipeptidyl peptidase IV membrane form
  2. Dipeptidyl peptidase 4 soluble form
    Alternative name(s):
    Dipeptidyl peptidase IV soluble form
Gene names
Name:DPP4
Synonyms:CD26
OrganismFelis catus (Cat) (Felis silvestris catus) [Reference proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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 regulation

Inhibited by GPC3 and diprotin A By similarity.

Subunit structure

Monomer. Homodimer or 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.

Subcellular location

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.

Post-translational modification

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.

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Secreted
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionAminopeptidase
Hydrolase
Protease
Receptor
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of extracellular matrix disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

invadopodium membrane

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

dipeptidyl-peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protease binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 765765Dipeptidyl peptidase 4 membrane form
PRO_0000027211
Chain38 – 765728Dipeptidyl peptidase 4 soluble form By similarity
PRO_0000027212

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 765736Extracellular Potential

Sites

Active site6291Charge relay system By similarity
Active site7071Charge relay system By similarity
Active site7391Charge relay system By similarity

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) By similarity
Glycosylation911N-linked (GlcNAc...) By similarity
Glycosylation1491N-linked (GlcNAc...) By similarity
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) By similarity
Glycosylation2801N-linked (GlcNAc...) By similarity
Glycosylation3201N-linked (GlcNAc...) By similarity
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) By similarity
Glycosylation6841N-linked (GlcNAc...) By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond443 ↔ 446 By similarity
Disulfide bond453 ↔ 471 By similarity
Disulfide bond648 ↔ 761 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N2I7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3EFCE98A22B175D9

FASTA76588,213
        10         20         30         40         50         60 
MKTPWKVLLG LLGLAALITI ITVPVVLLNK GNDAAADSRR TYTLTDYLKN TFRVKFYSLR 

        70         80         90        100        110        120 
WVSDHDYLYK QDNNILLFNA EYGNSSIFLE NSTFDEFEHS INDYSVSPDG QFILLEYNYV 

       130        140        150        160        170        180 
KQWRHSYTAS YDIYDLNKRQ LITEEKIPNN TQWITWSPEG HKLAYVWKND VYVKNEPNSS 

       190        200        210        220        230        240 
SHRITWTGEE NAIYNGIADW VYEEEIFSAY SALWWSPKGT FLAYAQFNDT QVPLIEYSFY 

       250        260        270        280        290        300 
SDESLQYPMT MRIPYPKAGA ANPTVKLFVI KTDNLNPNTN ATSVEITPPA AMLTGDYYLC 

       310        320        330        340        350        360 
DVTWANEERI SLQWLRRIQN YSVMDIRDYN NSTGKWISSA AQEHIEMSTT GWVGRFRPAE 

       370        380        390        400        410        420 
PHFTSDGRNF YKIISNEDGY KHICRFQIDK KDCTFITKGA WEVIGIEALT TDYLYYISNE 

       430        440        450        460        470        480 
YKGMPGGRNL YKIQLNDYTK VACLSCELKP ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT 

       490        500        510        520        530        540 
LHRSSNDEEL RVLEDNSALD KMLQEVQMPS KKLDFIILNE TKFWYQMILP PHFDTSKKYP 

       550        560        570        580        590        600 
LLIDVYAGPC SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF 

       610        620        630        640        650        660 
EVEDQIEAAR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSRWEY 

       670        680        690        700        710        720 
YDSVYTERYM GLPTPQDNLD YYKNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK 

       730        740        750        760 
ALVDAGVDFQ AMWYTDEDHG IASGPAHQHI YTHMSHFIKQ CFSLP 

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References

[1]"Molecular cloning and sequencing of a cDNA encoding the feline T-cell activation antigen CD26 homologue."
Nishimura Y., Miyazawa T., Ikeda Y., Izumiya Y., Nakamura K., Sato E., Mikami T., Takahashi E.
Immunogenetics 50:366-368(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023952 mRNA. Translation: BAA92344.1.
RefSeqNP_001009838.1. NM_001009838.1.

3D structure databases

ProteinModelPortalQ9N2I7.
SMRQ9N2I7. Positions 37-765.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493787.
KEGGfca:493787.

Organism-specific databases

CTD1803.

Phylogenomic databases

HOVERGENHBG005527.
KOK01278.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
InterProIPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPP4_FELCA
AccessionPrimary (citable) accession number: Q9N2I7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries