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Q9N2I7

- DPP4_FELCA

UniProt

Q9N2I7 - DPP4_FELCA

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Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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):
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
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 765736ExtracellularSequence AnalysisAdd
BLAST

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_0000027211Add
BLAST
Chaini38 – 765728Dipeptidyl peptidase 4 soluble formBy similarityPRO_0000027212Add
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...)By similarity
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)By similarity
Glycosylationi280 – 2801N-linked (GlcNAc...)By similarity
Glycosylationi320 – 3201N-linked (GlcNAc...)By similarity
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi384 ↔ 393By similarity
Disulfide bondi443 ↔ 446By similarity
Disulfide bondi453 ↔ 471By similarity
Glycosylationi519 – 5191N-linked (GlcNAc...)By similarity
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

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9N2I7.
SMRiQ9N2I7. Positions 37-765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG005527.
InParanoidiQ9N2I7.
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.

Q9N2I7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTPWKVLLG LLGLAALITI ITVPVVLLNK GNDAAADSRR TYTLTDYLKN
60 70 80 90 100
TFRVKFYSLR WVSDHDYLYK QDNNILLFNA EYGNSSIFLE NSTFDEFEHS
110 120 130 140 150
INDYSVSPDG QFILLEYNYV KQWRHSYTAS YDIYDLNKRQ LITEEKIPNN
160 170 180 190 200
TQWITWSPEG HKLAYVWKND VYVKNEPNSS SHRITWTGEE NAIYNGIADW
210 220 230 240 250
VYEEEIFSAY SALWWSPKGT FLAYAQFNDT QVPLIEYSFY SDESLQYPMT
260 270 280 290 300
MRIPYPKAGA ANPTVKLFVI KTDNLNPNTN ATSVEITPPA AMLTGDYYLC
310 320 330 340 350
DVTWANEERI SLQWLRRIQN YSVMDIRDYN NSTGKWISSA AQEHIEMSTT
360 370 380 390 400
GWVGRFRPAE PHFTSDGRNF YKIISNEDGY KHICRFQIDK KDCTFITKGA
410 420 430 440 450
WEVIGIEALT TDYLYYISNE YKGMPGGRNL YKIQLNDYTK VACLSCELKP
460 470 480 490 500
ERCQYYSVSF SKEAKYYQLR CSGPGLPLYT LHRSSNDEEL RVLEDNSALD
510 520 530 540 550
KMLQEVQMPS KKLDFIILNE TKFWYQMILP PHFDTSKKYP LLIDVYAGPC
560 570 580 590 600
SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAVNRRLGTF
610 620 630 640 650
EVEDQIEAAR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI
660 670 680 690 700
AVAPVSRWEY YDSVYTERYM GLPTPQDNLD YYKNSTVMSR AENFKQVEYL
710 720 730 740 750
LIHGTADDNV HFQQSAQISK ALVDAGVDFQ AMWYTDEDHG IASGPAHQHI
760
YTHMSHFIKQ CFSLP
Length:765
Mass (Da):88,213
Last modified:October 1, 2000 - v1
Checksum:i3EFCE98A22B175D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023952 mRNA. Translation: BAA92344.1.
RefSeqiNP_001009838.1. NM_001009838.1.

Genome annotation databases

GeneIDi493787.
KEGGifca:493787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023952 mRNA. Translation: BAA92344.1 .
RefSeqi NP_001009838.1. NM_001009838.1.

3D structure databases

ProteinModelPortali Q9N2I7.
SMRi Q9N2I7. Positions 37-765.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 493787.
KEGGi fca:493787.

Organism-specific databases

CTDi 1803.

Phylogenomic databases

HOVERGENi HBG005527.
InParanoidi Q9N2I7.
KOi K01278.

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. "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.

Entry informationi

Entry nameiDPP4_FELCA
AccessioniPrimary (citable) accession number: Q9N2I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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