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Reviewed, UniProtKB/Swiss-Prot P14740 (DPP4_RAT)

Last modified October 13, 2009. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    GP110 glycoprotein
    Bile canaliculus domain-specific membrane glycoprotein
    CD_antigen=CD26
Cleaved into the following 3 chains:
    1- Recommended name:
            Dipeptidyl peptidase 4 membrane form
        Alternative name(s):
            Dipeptidyl peptidase IV membrane form
    2- Recommended name:
            Dipeptidyl peptidase 4 soluble form
        Alternative name(s):
            Dipeptidyl peptidase IV soluble form
    3- Recommended name:
            Dipeptidyl peptidase 4 60 kDa soluble form
        Alternative name(s):
            Dipeptidyl peptidase IV 60 kDa soluble form
Gene names
Name: Dpp4
Synonyms: Cd26
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

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.

Subunit structure

Homodimer.

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Dipeptidyl peptidase 4 soluble form: Secreted.

Tissue specificity

Expressed in bile ducts and other epithelial brush borders (small intestine, kidney, colon, pancreatic duct); acinar structures in salivary glands; endothelial structures and T cell areas in thymus, spleen and lymph node. Ref.4

Post-translational modification

The soluble form (SDPP) derives from the membrane form (MDPP) by proteolytic processing.

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   DomainSignal-anchor
Transmembrane
   Molecular functionAminopeptidase
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processestablishment of localization

Inferred from mutant phenotype. Source: RGD

proteolysis

Inferred from direct assay. Source: RGD

regulation of T cell mediated immunity

Inferred from mutant phenotype. Source: RGD

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: RGD

cell surface

Inferred from direct assay. Source: RGD

endoplasmic reticulum

Inferred from direct assay. Source: RGD

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction Ref.1

Inferred from direct assay. Source: RGD

plasma membrane

Inferred from direct assay. Source: RGD

soluble fraction Ref.1

Inferred from direct assay. Source: RGD

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

collagen binding

Inferred from direct assay. Source: RGD

dipeptidyl-peptidase activity

Inferred from direct assay. Source: RGD

peptide binding

Inferred from direct assay. Source: RGD

protein homodimerization activity

Inferred from direct assay. Source: RGD

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767Dipeptidyl peptidase 4 membrane form
PRO_0000027219
Chain37 – 767731Dipeptidyl peptidase 4 soluble form
PRO_0000027220
Chain281 – 767487Dipeptidyl peptidase 4 60 kDa soluble form
PRO_0000027221

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2822Signal-anchor for type II membrane protein Potential
Topological domain29 – 767739Extracellular Potential

Sites

Active site6311Charge relay system By similarity
Active site7091Charge relay system By similarity
Active site7411Charge relay system By similarity

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) By similarity
Glycosylation901N-linked (GlcNAc...) By similarity
Glycosylation1481N-linked (GlcNAc...) By similarity
Glycosylation2171N-linked (GlcNAc...) By similarity
Glycosylation2271N-linked (GlcNAc...) By similarity
Glycosylation3191N-linked (GlcNAc...) By similarity
Glycosylation5211N-linked (GlcNAc...) By similarity
Glycosylation6861N-linked (GlcNAc...) By similarity
Disulfide bond383 ↔ 395 By similarity
Disulfide bond445 ↔ 448 By similarity
Disulfide bond455 ↔ 473 By similarity
Disulfide bond650 ↔ 763 By similarity

Experimental info

Mutagenesis6291G → A: Reduced activity. Ref.5
Mutagenesis6291G → R: Reduced activity. Ref.5
Mutagenesis6301W → E: No effect on activity. Ref.5
Mutagenesis6311S → A: Reduced activity. Ref.5
Mutagenesis6321Y → F: No effect on activity. Ref.5
Mutagenesis6321Y → G: Reduced activity. Ref.5
Mutagenesis6321Y → L: Reduced activity. Ref.5
Mutagenesis6331G → A: Reduced activity. Ref.5
Mutagenesis6331G → S: Reduced activity. Ref.5
Sequence conflict381R → A in AAA41096. Ref.1
Sequence conflict541Missing AA sequence Ref.4
Sequence conflict1831I → T in AAA41272. Ref.2
Sequence conflict3321T → N in AAA41272. Ref.2
Sequence conflict3521C → V in AAA41272. Ref.2
Sequence conflict3941V → D in AAA41272. Ref.2
Sequence conflict5621L → F in AAA41272. Ref.2
Sequence conflict6241R → Q in AAA41272. Ref.2

Secondary structure

1 ............................................................................................................................................... 767
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14740-1 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: ED947174F1F3E440

FASTA76788,089
        10         20         30         40         50         60 
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT FRVKSYSLRW 

        70         80         90        100        110        120 
VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI SDYSVSPDRL FVLLEYNYVK 

       130        140        150        160        170        180 
QWRHSYTASY SIYDLNKRQL ITEEKIPNNT QWITWSQEGH KLAYVWKNDI YVKIEPHLPS 

       190        200        210        220        230        240 
HRITSTGKEN VIFNGINDWV YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS 

       250        260        270        280        290        300 
DESLQYPKTV WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD 

       310        320        330        340        350        360 
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG WCGRFRPAEP 

       370        380        390        400        410        420 
HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK GAWEVISIEA LTSDYLYYIS 

       430        440        450        460        470        480 
NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL 

       490        500        510        520        530        540 
YTLHRSTDQK ELRVLEDNSA LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK 

       550        560        570        580        590        600 
YPLLIDVYAG PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG 

       610        620        630        640        650        660 
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC GIAVAPVSRW 

       670        680        690        700        710        720 
EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE YLLIHGTADD NVHFQQSAQI 

       730        740        750        760 
SKALVDAGVD FQAMWYTDED HGIASSTAHQ HIYSHMSHFL QQCFSLR

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References

[1]"Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain."
Ogata S., Misumi Y., Ikehara Y.
J. Biol. Chem. 264:3596-3601(1989) [PubMed: 2563382] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes."
Hong W., Doyle D.
Proc. Natl. Acad. Sci. U.S.A. 84:7962-7966(1987) [PubMed: 3479775] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Membrane orientation of rat gp110 as studied by in vitro translation."
Hong W.J., Doyle D.
J. Biol. Chem. 263:16892-16898(1988) [PubMed: 3182821] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40.
[4]"Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence."
McCaughan G.W., Wickson J.E., Creswick P.F., Gorrell M.D.
Hepatology 11:534-544(1990) [PubMed: 1970322] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-58, TISSUE SPECIFICITY.
[5]"N-terminal amino acid sequence of the 60-kDa protein of rat kidney dipeptidyl peptidase IV."
Iwaki-Egawa S., Watanabe Y., Fujimoto Y.
Biol. Chem. Hoppe-Seyler 374:973-975(1993) [PubMed: 7905271] [Abstract]
Cited for: PROTEIN SEQUENCE OF 281-302, MUTAGENESIS OF GLY-629; TRP-630; SER-631; TRY-632 AND GLY-633.
Tissue: Kidney.
[6]"Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis."
Ogata S., Misumi Y., Tsuji E., Takami N., Oda K., Ikehara Y.
Biochemistry 31:2582-2587(1992) [PubMed: 1347701] [Abstract]
Cited for: PROTEIN SEQUENCE OF 624-648.
[7]"Molecular dissection of the NH2-terminal signal/anchor sequence of rat dipeptidyl peptidase IV."
Hong W., Doyle D.
J. Cell Biol. 111:323-328(1990) [PubMed: 1974258] [Abstract]
Cited for: SIGNAL-ANCHOR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

J04591 mRNA. Translation: AAA41096.1.
J02997 mRNA. Translation: AAA41272.1.
IPIIPI00208422.
PIRA39914.
RefSeqNP_036921.1.
UniGeneRn.91364

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GBCX-ray2.80A/B38-767[»]
2GBFX-ray3.10A/B38-767[»]
2GBGX-ray3.00A/B38-767[»]
2GBIX-ray3.30A/B38-767[»]
2I3ZX-ray2.90A/B38-767[»]
2OAEX-ray3.00A/B38-767[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP14740.

Protein family/group databases

MEROPSS09.003.

Proteomic databases

PRIDEP14740.

Genome annotation databases

EnsemblENSRNOT00000040482; ENSRNOP00000045536; ENSRNOG00000030763; Rattus norvegicus. [Genome view]
GeneID25253.
KEGGrno:25253.

Organism-specific databases

CTD25253.
RGD2515. Dpp4.

Phylogenomic databases

HOVERGENP14740.

Enzyme and pathway databases

BRENDA3.4.14.5. 248.

Gene expression databases

GenevestigatorP14740.
GermOnlineENSRNOG00000030763. Rattus norvegicus.

Family and domain databases

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...

Other Resources

NextBio605879.

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Entry information

Entry nameDPP4_RAT
AccessionPrimary (citable) accession number: P14740
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 7, 2004
Last modified: October 13, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents