Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 160 (11 Dec 2019)
Sequence version 3 (13 Sep 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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.PROSITE-ProRule annotationBy similarity EC:3.4.14.5

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by GPC3 and diprotin A.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei630Charge relay systemPROSITE-ProRule annotation1
Active sitei708Charge relay systemPROSITE-ProRule annotation1
Active sitei740Charge relay systemPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease, Serine protease
Biological processCell adhesion

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.14.5 6170

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
pig-dpp4 DPP4N_Peptidase_S9

MEROPS protease database

More...
MEROPSi
S09.003

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DPP4
Synonyms:CD26
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000314985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15
  • UP000008227 Componenti: Chromosome 15

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 6CytoplasmicSequence analysis6
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei7 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini28 – 766ExtracellularSequence analysisAdd BLAST739

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3813

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000272171 – 766Dipeptidyl peptidase 4 membrane formAdd BLAST766
ChainiPRO_000002721838 – 766Dipeptidyl peptidase 4 soluble formAdd BLAST729

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi85N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi92N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi150N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi179N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi219N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi229N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi279N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi321N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi385 ↔ 394
Disulfide bondi444 ↔ 447
Disulfide bondi454 ↔ 472
Disulfide bondi649 ↔ 762
Glycosylationi685N-linked (GlcNAc...) asparagine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.
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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22411

PeptideAtlas

More...
PeptideAtlasi
P22411

PRoteomics IDEntifications database

More...
PRIDEi
P22411

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22411

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSSSCG00000015894 Expressed in 6 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P22411 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P22411 SS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Homodimer (PubMed:12690074). Heterodimer with Seprase (FAP) (By similarity). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation (By similarity).

Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (By similarity). Associates with collagen (By similarity).

Interacts with PTPRC; the interaction is enhanced in an interleukin-12-dependent manner in activated lymphocytes (By similarity).

Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity (By similarity).

Interacts with CAV1 (via the N-terminus); the interaction is direct (By similarity).

Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11 (By similarity).

Interacts with IGF2R; the interaction is direct (By similarity).

Interacts with GPC3 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000028692

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22411

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1766
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22411

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22411

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2100 Eukaryota
COG1506 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231875

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22411

KEGG Orthology (KO)

More...
KOi
K01278

Identification of Orthologs from Complete Genome Data

More...
OMAi
QVGDIQY

Database of Orthologous Groups

More...
OrthoDBi
269253at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313309

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.140.10.30, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058 AB_hydrolase
IPR040522 DPPIV_rep
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00930 DPPIV_N, 1 hit
PF18811 DPPIV_rep, 1 hit
PF00326 Peptidase_S9, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53474 SSF53474, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00708 PRO_ENDOPEP_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22411-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTPWKVLLG LLGIAALVTV ITVPVVLLNK GTDDAAADSR RTYTLTDYLK
60 70 80 90 100
STFRVKFYTL QWISDHEYLY KQENNILLFN AEYGNSSIFL ENSTFDELGY
110 120 130 140 150
STNDYSVSPD RQFILFEYNY VKQWRHSYTA SYDIYDLNKR QLITEERIPN
160 170 180 190 200
NTQWITWSPV GHKLAYVWNN DIYVKNEPNL SSQRITWTGK ENVIYNGVTD
210 220 230 240 250
WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF YSDESLQYPK
260 270 280 290 300
TVRIPYPKAG AENPTVKFFV VDTRTLSPNA SVTSYQIVPP ASVLIGDHYL
310 320 330 340 350
CGVTWVTEER ISLQWIRRAQ NYSIIDICDY DESTGRWISS VARQHIEIST
360 370 380 390 400
TGWVGRFRPA EPHFTSDGNS FYKIISNEEG YKHICHFQTD KSNCTFITKG
410 420 430 440 450
AWEVIGIEAL TSDYLYYISN EHKGMPGGRN LYRIQLNDYT KVTCLSCELN
460 470 480 490 500
PERCQYYSAS FSNKAKYYQL RCFGPGLPLY TLHSSSSDKE LRVLEDNSAL
510 520 530 540 550
DKMLQDVQMP SKKLDVINLH GTKFWYQMIL PPHFDKSKKY PLLIEVYAGP
560 570 580 590 600
CSQKVDTVFR LSWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT
610 620 630 640 650
FEVEDQIEAT RQFSKMGFVD DKRIAIWGWS YGGYVTSMVL GAGSGVFKCG
660 670 680 690 700
IAVAPVSKWE YYDSVYTERY MGLPTPEDNL DYYRNSTVMS RAENFKQVEY
710 720 730 740 750
LLIHGTADDN VHFQQSAQLS KALVDAGVDF QTMWYTDEDH GIASNMAHQH
760
IYTHMSHFLK QCFSLP
Length:766
Mass (Da):88,242
Last modified:September 13, 2004 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8800D520BAEA856D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti32Missing (PubMed:7903569).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY198323 mRNA Translation: AAO43404.1
X73276 mRNA Translation: CAA51717.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I47134
S14746

NCBI Reference Sequences

More...
RefSeqi
NP_999422.1, NM_214257.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSSSCT00005069919; ENSSSCP00005043532; ENSSSCG00005043469
ENSSSCT00070051059; ENSSSCP00070043179; ENSSSCG00070025527

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
397492

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397492

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY198323 mRNA Translation: AAO43404.1
X73276 mRNA Translation: CAA51717.1
PIRiI47134
S14746
RefSeqiNP_999422.1, NM_214257.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
5LLSX-ray2.41A/B/C/D1-766[»]
SMRiP22411
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000028692

Chemistry databases

BindingDBiP22411
ChEMBLiCHEMBL3813

Protein family/group databases

ESTHERipig-dpp4 DPP4N_Peptidase_S9
MEROPSiS09.003

PTM databases

iPTMnetiP22411

Proteomic databases

PaxDbiP22411
PeptideAtlasiP22411
PRIDEiP22411

Genome annotation databases

EnsembliENSSSCT00005069919; ENSSSCP00005043532; ENSSSCG00005043469
ENSSSCT00070051059; ENSSSCP00070043179; ENSSSCG00070025527
GeneIDi397492
KEGGissc:397492

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1803

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA
HOGENOMiHOG000231875
InParanoidiP22411
KOiK01278
OMAiQVGDIQY
OrthoDBi269253at2759
TreeFamiTF313309

Enzyme and pathway databases

BRENDAi3.4.14.5 6170

Miscellaneous databases

EvolutionaryTraceiP22411

Protein Ontology

More...
PROi
PR:P22411

Gene expression databases

BgeeiENSSSCG00000015894 Expressed in 6 organ(s), highest expression level in kidney
ExpressionAtlasiP22411 baseline and differential
GenevisibleiP22411 SS

Family and domain databases

Gene3Di2.140.10.30, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR040522 DPPIV_rep
IPR002471 Pept_S9_AS
IPR001375 Peptidase_S9
IPR002469 Peptidase_S9B_N
IPR038554 Peptidase_S9B_N_sf
PfamiView protein in Pfam
PF00930 DPPIV_N, 1 hit
PF18811 DPPIV_rep, 1 hit
PF00326 Peptidase_S9, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00708 PRO_ENDOPEP_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDPP4_PIG
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22411
Secondary accession number(s): Q866G2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 13, 2004
Last modified: December 11, 2019
This is version 160 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again