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UniProtKB/Swiss-Prot entry P22411

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DPP4_PIG
Primary accession number P22411
Secondary accession number Q866G2
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on September 13, 2004 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 80)
Name and origin of the protein
Protein name Dipeptidyl peptidase 4
Synonyms EC 3.4.14.5
Dipeptidyl peptidase IV
DPP IV
T-cell activation antigen CD26
CD26 antigen
Contains Dipeptidyl peptidase 4 membrane form
     (Dipeptidyl peptidase IV membrane form)
Dipeptidyl peptidase 4 soluble form
     (Dipeptidyl peptidase IV soluble form)
Gene name
Name: DPP4
Synonyms: CD26
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Kidney;
DOI=10.1515/BC.2003.172; PubMed=14719797 [NCBI, ExPASy, EBI, Israel, Japan]
Baer J., Weber A., Hoffmann T., Stork J., Wermann M., Wagner L., Aust S., Gerhartz B., Demuth H.-U.;
"Characterisation of human dipeptidyl peptidase IV expressed in Pichia pastoris. A structural and mechanistic comparison between the recombinant human and the purified porcine enzyme.";
Biol. Chem. 384:1553-1563(2003).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] OF 2-67.
TISSUE=Kidney;
DOI=10.1007/BF00361393; PubMed=7903569 [NCBI, ExPASy, EBI, Israel, Japan]
Thomsen P.D., Qvist H., Marklund L., Andersson L., Sjostrom H., Noren O.;
"Assignment of the dipeptidylpeptidase IV (DPP4) gene to pig chromosome 15q21.";
Mamm. Genome 4:604-607(1993).
[3]
 PROTEIN SEQUENCE OF 38-71.
TISSUE=Kidney;
PubMed=1675855 [NCBI, ExPASy, EBI, Israel, Japan]
Seidl R., Mann K., Schaeffer W.;
"N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV solubilized by autolysis.";
Biol. Chem. Hoppe-Seyler 372:213-214(1991).
[4]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-766, GLYCOSYLATION AT ASN-85; ASN-92; ASN-229; ASN-279; ASN-321 AND ASN-685, AND HOMODIMERIZATION.
DOI=10.1073/pnas.0230620100; PubMed=12690074 [NCBI, ExPASy, EBI, Israel, Japan]
Engel M., Hoffmann T., Wagner L., Wermann M., Heiser U., Kiefersauer R., Huber R., Bode W., Demuth H.-U., Brandstetter H.;
"The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 100:5063-5068(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY198323; AAO43404.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X73276; CAA51717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I47134; I47134.
S14746; S14746.
RefSeq NP_999422.1; -.
UniGene Ssc.16236
3D structure databases
PDB
1ORV; X-ray; 1.80 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
1ORW; X-ray; 2.84 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2AJ8; X-ray; 2.11 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2AJB; X-ray; 2.75 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2AJC; X-ray; 1.95 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2AJD; X-ray; 2.56 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2BUA; X-ray; 2.56 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
2BUC; X-ray; 2.50 A; A/B/C/D=39-766.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ORV; -.
1ORW; -.
2AJ8; -.
2AJB; -.
2AJC; -.
2AJD; -.
2BUA; -.
2BUC; -.
ModBase P22411.
Protein family/group databases
MEROPS S09.003; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004177; Molecular function: aminopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002469; Peptidase_S9B.
Graphical view of domain structure.
Pfam PF00930; DPPIV_N; 1.
PF00326; Peptidase_S9; 1.
Pfam graphical view of domain structure.
PROSITE PS00708; PRO_ENDOPEP_SER; 1.
ProtoNet P22411.
Genome annotation databases
GeneID 397492; -.
KEGG ssc:397492; -.
Phylogenomic databases
HOVERGEN P22411; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminopeptidase; Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Protease; Secreted; Serine protease; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   766  766     Dipeptidyl peptidase 4 membrane form. PRO_0000027217
CHAIN   38   766  729     Dipeptidyl peptidase 4 soluble form. PRO_0000027218
TOPO_DOM   1     6  6     Cytoplasmic (Potential). 
TRANSMEM   7    27  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   28   766  739     Extracellular (Potential). 
ACT_SITE   630   630        Charge relay system (By similarity). 
ACT_SITE   708   708        Charge relay system (By similarity). 
ACT_SITE   740   740        Charge relay system (By similarity). 
CARBOHYD   85    85        N-linked (GlcNAc...). 
CARBOHYD   92    92        N-linked (GlcNAc...). 
CARBOHYD   229   229        N-linked (GlcNAc...). 
CARBOHYD   279   279        N-linked (GlcNAc...). 
CARBOHYD   321   321        N-linked (GlcNAc...). 
CARBOHYD   685   685        N-linked (GlcNAc...). 
DISULFID   385   394         
DISULFID   444   447         
DISULFID   454   472         
DISULFID   649   762         
CONFLICT   32    32        Missing (in Ref. 2). 
HELIX   45    50  6      
STRAND   60    62  3      
STRAND   64    72  9      
STRAND   75    80  6      
TURN   81    83  3      
STRAND   87    90  4      
STRAND   104   107  4      
STRAND   111   122  12      
STRAND   124   126  3      
STRAND   128   136  9      
TURN   137   140  4      
STRAND   152   157  6      
STRAND   164   168  5      
STRAND   171   177  7      
TURN   191   193  3      
STRAND   194   198  5      
HELIX   201   206  6      
STRAND   209   212  4      
STRAND   214   216  3      
STRAND   220   229  10      
STRAND   235   240  6      
STRAND   250   255  6      
STRAND   265   272  8      
HELIX   273   275  3      
STRAND   283   287  5      
HELIX   291   294  4      
STRAND   298   307  10      
STRAND   310   317  8      
STRAND   320   330  11      
TURN   332   334  3      
HELIX   341   343  3      
STRAND   344   348  5      
STRAND   350   352  3      
STRAND   354   358  5      
STRAND   368   376  9      
STRAND   382   388  7      
STRAND   394   397  4      
STRAND   400   402  3      
STRAND   404   410  7      
STRAND   412   420  9      
HELIX   422   424  3      
STRAND   429   435  7      
STRAND   438   446  9      
TURN   447   449  3      
TURN   451   453  3      
STRAND   456   461  6      
STRAND   465   472  8      
STRAND   474   477  4      
STRAND   479   484  6      
TURN   485   488  4      
STRAND   489   495  7      
HELIX   498   504  7      
STRAND   511   519  9      
STRAND   522   530  9      
STRAND   540   546  7      
HELIX   563   569  7      
STRAND   574   578  5      
STRAND   584   586  3      
HELIX   588   591  4      
HELIX   592   594  3      
HELIX   601   614  14      
STRAND   619   629  11      
HELIX   631   640  10      
TURN   641   643  3      
STRAND   648   654  7      
HELIX   659   661  3      
HELIX   664   671  8      
TURN   676   679  4      
HELIX   680   684  5      
HELIX   689   697  9      
STRAND   698   705  8      
STRAND   709   711  3      
HELIX   713   725  13      
STRAND   731   735  5      
HELIX   745   762  18      
Sequence information
Length: 766 AA [This is the length of the unprocessed precursor] Molecular weight: 88242 Da [This is the MW of the unprocessed precursor] CRC64: 8800D520BAEA856D [This is a checksum on the sequence] 
        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
P22411 in FASTA format

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View entry in raw text format (no links)
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