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Reviewed, UniProtKB/Swiss-Prot P22411 (DPP4_PIG)

Last modified June 16, 2009. Version 83. 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
    CD_antigen=CD26
Cleaved into the following 2 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
Gene names
Name: DPP4
Synonyms: CD26
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length766 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. Ref.1

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. Ref.4

Subcellular location

Cell membrane; Single-pass type II membrane protein.

Dipeptidyl peptidase 4 soluble form: Secreted.

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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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 766766Dipeptidyl peptidase 4 membrane form
PRO_0000027217
Chain38 – 766729Dipeptidyl peptidase 4 soluble form
PRO_0000027218

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Signal-anchor for type II membrane protein Potential
Topological domain28 – 766739Extracellular Potential

Sites

Active site6301Charge relay system By similarity
Active site7081Charge relay system By similarity
Active site7401Charge relay system By similarity

Amino acid modifications

Glycosylation851N-linked (GlcNAc...) Ref.4
Glycosylation921N-linked (GlcNAc...) Ref.4
Glycosylation2291N-linked (GlcNAc...) Ref.4
Glycosylation2791N-linked (GlcNAc...) Ref.4
Glycosylation3211N-linked (GlcNAc...) Ref.4
Glycosylation6851N-linked (GlcNAc...) Ref.4
Disulfide bond385 ↔ 394
Disulfide bond444 ↔ 447
Disulfide bond454 ↔ 472
Disulfide bond649 ↔ 762

Experimental info

Sequence conflict321Missing Ref.2

Secondary structure

1 ........................................................................................................................................... 766
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22411-1 [UniParc].

Last modified September 13, 2004. Version 3.
Checksum: 8800D520BAEA856D

FASTA76688,242
        10         20         30         40         50         60 
MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GTDDAAADSR RTYTLTDYLK STFRVKFYTL 

        70         80         90        100        110        120 
QWISDHEYLY KQENNILLFN AEYGNSSIFL ENSTFDELGY STNDYSVSPD RQFILFEYNY 

       130        140        150        160        170        180 
VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWITWSPV GHKLAYVWNN DIYVKNEPNL 

       190        200        210        220        230        240 
SSQRITWTGK ENVIYNGVTD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF 

       250        260        270        280        290        300 
YSDESLQYPK TVRIPYPKAG AENPTVKFFV VDTRTLSPNA SVTSYQIVPP ASVLIGDHYL 

       310        320        330        340        350        360 
CGVTWVTEER ISLQWIRRAQ NYSIIDICDY DESTGRWISS VARQHIEIST TGWVGRFRPA 

       370        380        390        400        410        420 
EPHFTSDGNS FYKIISNEEG YKHICHFQTD KSNCTFITKG AWEVIGIEAL TSDYLYYISN 

       430        440        450        460        470        480 
EHKGMPGGRN LYRIQLNDYT KVTCLSCELN PERCQYYSAS FSNKAKYYQL RCFGPGLPLY 

       490        500        510        520        530        540 
TLHSSSSDKE LRVLEDNSAL DKMLQDVQMP SKKLDVINLH GTKFWYQMIL PPHFDKSKKY 

       550        560        570        580        590        600 
PLLIEVYAGP CSQKVDTVFR LSWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT 

       610        620        630        640        650        660 
FEVEDQIEAT RQFSKMGFVD DKRIAIWGWS YGGYVTSMVL GAGSGVFKCG IAVAPVSKWE 

       670        680        690        700        710        720 
YYDSVYTERY MGLPTPEDNL DYYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQLS 

       730        740        750        760 
KALVDAGVDF QTMWYTDEDH GIASNMAHQH IYTHMSHFLK QCFSLP

« Hide

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References

[1]"Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme."
Baer J., Weber A., Hoffmann T., Stork J., Wermann M., Wagner L., Aust S., Gerhartz B., Demuth H.-U.
Biol. Chem. 384:1553-1563(2003) [PubMed: 14719797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Kidney.
[2]"Assignment of the dipeptidylpeptidase IV (DPP4) gene to pig chromosome 15q21."
Thomsen P.D., Qvist H., Marklund L., Andersson L., Sjostrom H., Noren O.
Mamm. Genome 4:604-607(1993) [PubMed: 7903569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-67.
Tissue: Kidney.
[3]"N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV solubilized by autolysis."
Seidl R., Mann K., Schaeffer W.
Biol. Chem. Hoppe-Seyler 372:213-214(1991) [PubMed: 1675855] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-71.
Tissue: Kidney.
[4]"The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism."
Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., Huber R., Bode W., Demuth H.-U., Brandstetter H.
Proc. Natl. Acad. Sci. U.S.A. 100:5063-5068(2003) [PubMed: 12690074] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; ASN-92; ASN-229; ASN-279; ASN-321 AND ASN-685, HOMODIMERIZATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY198323 mRNA. Translation: AAO43404.1.
X73276 mRNA. Translation: CAA51717.1.
PIRI47134.
S14746.
RefSeqNP_999422.1.
UniGeneSsc.16236

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ORVX-ray1.80A/B/C/D39-766[»]
1ORWX-ray2.84A/B/C/D39-766[»]
2AJ8X-ray2.11A/B/C/D39-766[»]
2AJBX-ray2.75A/B/C/D39-766[»]
2AJCX-ray1.95A/B/C/D39-766[»]
2AJDX-ray2.56A/B/C/D39-766[»]
2BUAX-ray2.56A/B/C/D39-766[»]
2BUCX-ray2.50A/B/C/D39-766[»]
ModBaseSearch...

Protein family/group databases

MEROPSS09.003.

Genome annotation databases

GeneID397492.
KEGGssc:397492.

Phylogenomic databases

HOVERGENP22411.

Enzyme and pathway databases

BRENDA3.4.14.5. 249.

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...

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Entry information

Entry nameDPP4_PIG
AccessionPrimary (citable) accession number: P22411
Secondary accession number(s): Q866G2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 13, 2004
Last modified: June 16, 2009
This is version 83 of the entry and version 3 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