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P28843

- DPP4_MOUSE

UniProt

P28843 - DPP4_MOUSE

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Protein

Dipeptidyl peptidase 4

Gene

Dpp4

Organism
Mus musculus (Mouse)
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 sitei624 – 6241Charge relay systemPROSITE-ProRule annotation
Active sitei702 – 7021Charge relay systemPROSITE-ProRule annotation
Active sitei734 – 7341Charge 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, 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
Thymocyte-activating molecule
Short name:
THAM
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:94919. Dpp4.

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

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: MGI
  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 – 760760Dipeptidyl peptidase 4 membrane formPRO_0000027215Add
BLAST
Chaini37 – 760724Dipeptidyl peptidase 4 soluble formBy similarityPRO_0000027216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)By similarity
Glycosylationi90 – 901N-linked (GlcNAc...)By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...); atypical1 Publication
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi223 – 2231N-linked (GlcNAc...)By similarity
Glycosylationi315 – 3151N-linked (GlcNAc...)By similarity
Disulfide bondi322 ↔ 333By similarity
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi379 ↔ 388By similarity
Disulfide bondi438 ↔ 441By similarity
Disulfide bondi448 ↔ 466By similarity
Glycosylationi514 – 5141N-linked (GlcNAc...)1 Publication
Disulfide bondi643 ↔ 756By similarity
Glycosylationi679 – 6791N-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

MaxQBiP28843.
PaxDbiP28843.
PRIDEiP28843.

PTM databases

PhosphoSiteiP28843.

Expressioni

Gene expression databases

BgeeiP28843.
CleanExiMM_DPP4.
GenevestigatoriP28843.

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

BioGridi199300. 1 interaction.
IntActiP28843. 5 interactions.
MINTiMINT-1857814.
STRINGi10090.ENSMUSP00000044050.

Structurei

3D structure databases

ProteinModelPortaliP28843.
SMRiP28843. Positions 39-759.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini29 – 760732ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi295 – 466172Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP28843.
KOiK01278.
OMAiETKFWYQ.
OrthoDBiEOG761BT2.
PhylomeDBiP28843.
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.

P28843-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTPWKVLLG LLGVAALVTI ITVPIVLLSK DEAAADSRRT YSLADYLKST
60 70 80 90 100
FRVKSYSLWW VSDFEYLYKQ ENNILLLNAE HGNSSIFLEN STFESFGYHS
110 120 130 140 150
VSPDRLFVLL EYNYVKQWRH SYTASYNIYD VNKRQLITEE KIPNNTQWIT
160 170 180 190 200
WSPEGHKLAY VWKNDIYVKV EPHLPSHRIT STGEENVIYN GITDWVYEEE
210 220 230 240 250
VFGAYSALWW SPNNTFLAYA QFNDTGVPLI EYSFYSDESL QYPKTVWIPY
260 270 280 290 300
PKAGAVNPTV KFFIVNIDSL SSSSSAAPIQ IPAPASVARG DHYLCDVVWA
310 320 330 340 350
TEERISLQWL RRIQNYSVMA ICDYDKINLT WNCPSEQQHV EMSTTGWVGR
360 370 380 390 400
FRPAEPHFTS DGSSFYKIIS DKDGYKHICH FPKDKKDCTF ITKGAWEVIS
410 420 430 440 450
IEALTSDYLY YISNQYKEMP GGRNLYKIQL TDHTNVKCLS CDLNPERCQY
460 470 480 490 500
YAVSFSKEAK YYQLGCWGPG LPLYTLHRST DHKELRVLED NSALDRMLQD
510 520 530 540 550
VQMPSKKLDF IVLNETRFWY QMILPPHFDK SKKYPLLLDV YAGPCSQKAD
560 570 580 590 600
ASFRLNWATY LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTLEVEDQ
610 620 630 640 650
IEAARQFVKM GFVDSKRVAI WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV
660 670 680 690 700
SRWEYYDSVY TERYMGLPIP EDNLDHYRNS TVMSRAEHFK QVEYLLIHGT
710 720 730 740 750
ADDNVHFQQS AQISKALVDA GVDFQAMWYT DEDHGIASST AHQHIYSHMS
760
HFLQQCFSLH
Length:760
Mass (Da):87,437
Last modified:February 1, 1996 - v3
Checksum:iA5F644B46E4A3DF8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58384 mRNA. Translation: CAA41274.1.
U12620
, U12599, U12600, U12601, U12602, U12603, U12604, U12605, U12606, U12607, U12608, U12609, U12610, U12611, U12612, U12613, U12614, U12615, U12616, U12617, U12618, U12619 Genomic DNA. Translation: AAA82213.1.
AK085370 mRNA. Translation: BAC39434.1.
AK153939 mRNA. Translation: BAE32266.1.
BC022183 mRNA. Translation: AAH22183.1.
CCDSiCCDS16065.1.
PIRiS23752.
RefSeqiNP_001153015.1. NM_001159543.1.
NP_034204.1. NM_010074.3.
XP_006498753.1. XM_006498690.1.
UniGeneiMm.1151.

Genome annotation databases

EnsembliENSMUST00000047812; ENSMUSP00000044050; ENSMUSG00000035000.
GeneIDi13482.
KEGGimmu:13482.
UCSCiuc008jvg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58384 mRNA. Translation: CAA41274.1 .
U12620
, U12599 , U12600 , U12601 , U12602 , U12603 , U12604 , U12605 , U12606 , U12607 , U12608 , U12609 , U12610 , U12611 , U12612 , U12613 , U12614 , U12615 , U12616 , U12617 , U12618 , U12619 Genomic DNA. Translation: AAA82213.1 .
AK085370 mRNA. Translation: BAC39434.1 .
AK153939 mRNA. Translation: BAE32266.1 .
BC022183 mRNA. Translation: AAH22183.1 .
CCDSi CCDS16065.1.
PIRi S23752.
RefSeqi NP_001153015.1. NM_001159543.1.
NP_034204.1. NM_010074.3.
XP_006498753.1. XM_006498690.1.
UniGenei Mm.1151.

3D structure databases

ProteinModelPortali P28843.
SMRi P28843. Positions 39-759.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199300. 1 interaction.
IntActi P28843. 5 interactions.
MINTi MINT-1857814.
STRINGi 10090.ENSMUSP00000044050.

Chemistry

BindingDBi P28843.
ChEMBLi CHEMBL3883.

Protein family/group databases

MEROPSi S09.003.

PTM databases

PhosphoSitei P28843.

Proteomic databases

MaxQBi P28843.
PaxDbi P28843.
PRIDEi P28843.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047812 ; ENSMUSP00000044050 ; ENSMUSG00000035000 .
GeneIDi 13482.
KEGGi mmu:13482.
UCSCi uc008jvg.2. mouse.

Organism-specific databases

CTDi 1803.
MGIi MGI:94919. Dpp4.

Phylogenomic databases

eggNOGi COG1506.
GeneTreei ENSGT00760000119233.
HOGENOMi HOG000231875.
HOVERGENi HBG005527.
InParanoidi P28843.
KOi K01278.
OMAi ETKFWYQ.
OrthoDBi EOG761BT2.
PhylomeDBi P28843.
TreeFami TF313309.

Miscellaneous databases

ChiTaRSi DPP4. mouse.
NextBioi 283979.
PROi P28843.
SOURCEi Search...

Gene expression databases

Bgeei P28843.
CleanExi MM_DPP4.
Genevestigatori P28843.

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. "cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases."
    Marguet D.A., Bernard A.-M., Vivier I., Darmoul D., Naquet P., Pierres M.
    J. Biol. Chem. 267:2200-2208(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss.
    Tissue: Thymus.
  2. Marguet D.A.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Structure of the mouse dipeptidyl peptidase IV (CD26) gene."
    Bernard A.-M., Mattei M.-G., Pierres M., Marguet D.
    Biochemistry 33:15204-15214(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: B10.A.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Kidney and Thymus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV)."
    Vivier I., Marguet D.A., Naquet P., Bonicel J., Black D., Li C.X.-Y., Bernard A.-M., Gorvel J.-P., Pierres M.
    J. Immunol. 147:447-454(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
  7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-514.

Entry informationi

Entry nameiDPP4_MOUSE
AccessioniPrimary (citable) accession number: P28843
Secondary accession number(s): Q3U514
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 139 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3