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Entry version 165 (11 Dec 2019)
Sequence version 2 (07 Dec 2004)
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Protein

Dipeptidyl peptidase 4

Gene

Dpp4

Organism
Rattus norvegicus (Rat)
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. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.By similarity

<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.1 Publication

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 sitei631Charge relay systemPROSITE-ProRule annotation1
Active sitei709Charge relay systemPROSITE-ProRule annotation1
Active sitei741Charge 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 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-RNO-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)

Protein family/group databases

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

More...
ESTHERi
ratno-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):
Bile canaliculus domain-specific membrane glycoprotein
Dipeptidyl peptidase IV
Short name:
DPP IV
GP110 glycoprotein
T-cell activation antigen CD26
CD_antigen: CD26
Cleaved into the following 3 chains:
Alternative name(s):
Dipeptidyl peptidase IV membrane form
Alternative name(s):
Dipeptidyl peptidase IV soluble form
Alternative name(s):
Dipeptidyl peptidase IV 60 kDa 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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2515 Dpp4

<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 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST22
Topological domaini29 – 767ExtracellularSequence 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi629G → A: Reduced activity. 1 Publication1
Mutagenesisi629G → R: Reduced activity. 1 Publication1
Mutagenesisi630W → E: No effect on activity. 1 Publication1
Mutagenesisi631S → A: Reduced activity. 1 Publication1
Mutagenesisi632Y → F: No effect on activity. 1 Publication1
Mutagenesisi632Y → G: Reduced activity. 1 Publication1
Mutagenesisi632Y → L: Reduced activity. 1 Publication1
Mutagenesisi633G → A: Reduced activity. 1 Publication1
Mutagenesisi633G → S: Reduced activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4653

DrugCentral

More...
DrugCentrali
P14740

<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_00000272191 – 767Dipeptidyl peptidase 4 membrane formAdd BLAST767
ChainiPRO_000002722037 – 767Dipeptidyl peptidase 4 soluble formAdd BLAST731
ChainiPRO_0000027221281 – 767Dipeptidyl peptidase 4 60 kDa soluble formAdd BLAST487

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>Glycosylationi83N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi90N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi148N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi217N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi227N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi319N-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 bondi326 ↔ 3371 Publication
Disulfide bondi383 ↔ 3951 Publication
Disulfide bondi445 ↔ 4481 Publication
Disulfide bondi455 ↔ 4731 Publication
Glycosylationi521N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi650 ↔ 7631 Publication
Glycosylationi686N-linked (GlcNAc...) asparagineBy similarity1

<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.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

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

More...
PaxDbi
P14740

PRoteomics IDEntifications database

More...
PRIDEi
P14740

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P14740

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P14740

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P14740

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.1 Publication

<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. 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 an interleukin-12-dependent manner in activated lymphocytes.

Interacts (via 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

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P14740, 1 interactor

Molecular INTeraction database

More...
MINTi
P14740

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000045536

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P14740

<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

1767
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
P14740

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
P14740

<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
P14740

KEGG Orthology (KO)

More...
KOi
K01278

Database of Orthologous Groups

More...
OrthoDBi
269253at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14740

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P14740-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTPWKVLLG LLGVAALVTI ITVPVVLLNK DEAAADSRRT YTLADYLKNT
60 70 80 90 100
FRVKSYSLRW VSDSEYLYKQ ENNILLFNAE HGNSSIFLEN STFEIFGDSI
110 120 130 140 150
SDYSVSPDRL FVLLEYNYVK QWRHSYTASY SIYDLNKRQL ITEEKIPNNT
160 170 180 190 200
QWITWSQEGH KLAYVWKNDI YVKIEPHLPS HRITSTGKEN VIFNGINDWV
210 220 230 240 250
YEEEIFGAYS ALWWSPNGTF LAYAQFNDTG VPLIEYSFYS DESLQYPKTV
260 270 280 290 300
WIPYPKAGAV NPTVKFFIVN TDSLSSTTTT IPMQITAPAS VTTGDHYLCD
310 320 330 340 350
VAWVSEDRIS LQWLRRIQNY SVMAICDYDK TTLVWNCPTT QEHIETSATG
360 370 380 390 400
WCGRFRPAEP HFTSDGSSFY KIVSDKDGYK HICQFQKDRK PEQVCTFITK
410 420 430 440 450
GAWEVISIEA LTSDYLYYIS NEYKEMPGGR NLYKIQLTDH TNKKCLSCDL
460 470 480 490 500
NPERCQYYSV SLSKEAKYYQ LGCRGPGLPL YTLHRSTDQK ELRVLEDNSA
510 520 530 540 550
LDKMLQDVQM PSKKLDFIVL NETRFWYQMI LPPHFDKSKK YPLLIDVYAG
560 570 580 590 600
PCSQKADAAF RLNWATYLAS TENIIVASFD GRGSGYQGDK IMHAINKRLG
610 620 630 640 650
TLEVEDQIEA ARQFLKMGFV DSKRVAIWGW SYGGYVTSMV LGSGSGVFKC
660 670 680 690 700
GIAVAPVSRW EYYDSVYTER YMGLPTPEDN LDHYRNSTVM SRAENFKQVE
710 720 730 740 750
YLLIHGTADD NVHFQQSAQI SKALVDAGVD FQAMWYTDED HGIASSTAHQ
760
HIYSHMSHFL QQCFSLR
Length:767
Mass (Da):88,089
Last modified:December 7, 2004 - v2
<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:iED947174F1F3E440
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1M7X5F1M7X5_RAT
Dipeptidyl peptidase 4
Dpp4
767Annotation score:

Annotation score:1 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>
A0A0G2K238A0A0G2K238_RAT
Dipeptidyl peptidase 4
Dpp4
789Annotation score:

Annotation score:1 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>
A0A0G2JTX5A0A0G2JTX5_RAT
Dipeptidyl peptidase 4
Dpp4
767Annotation score:

Annotation score:1 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 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 conflicti38R → A in AAA41096 (PubMed:2563382).Curated1
Sequence conflicti54Missing AA sequence (PubMed:1970322).Curated1
Sequence conflicti183I → T in AAA41272 (PubMed:3479775).Curated1
Sequence conflicti332T → N in AAA41272 (PubMed:3479775).Curated1
Sequence conflicti352C → V in AAA41272 (PubMed:3479775).Curated1
Sequence conflicti394V → D in AAA41272 (PubMed:3479775).Curated1
Sequence conflicti562L → F in AAA41272 (PubMed:3479775).Curated1
Sequence conflicti624R → Q in AAA41272 (PubMed:3479775).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J04591 mRNA Translation: AAA41096.1
J02997 mRNA Translation: AAA41272.1

Protein sequence database of the Protein Information Resource

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PIRi
A39914

NCBI Reference Sequences

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RefSeqi
NP_036921.1, NM_012789.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
25253

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25253

UCSC genome browser

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UCSCi
RGD:2515 rat

<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
J04591 mRNA Translation: AAA41096.1
J02997 mRNA Translation: AAA41272.1
PIRiA39914
RefSeqiNP_036921.1, NM_012789.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
4FFVX-ray2.40A/B38-767[»]
4FFWX-ray2.90A/B38-767[»]
5VTAX-ray2.80A/B/C/D37-767[»]
SMRiP14740
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP14740, 1 interactor
MINTiP14740
STRINGi10116.ENSRNOP00000045536

Chemistry databases

BindingDBiP14740
ChEMBLiCHEMBL4653
DrugCentraliP14740

Protein family/group databases

ESTHERiratno-dpp4 DPP4N_Peptidase_S9
MEROPSiS09.003

PTM databases

iPTMnetiP14740
PhosphoSitePlusiP14740
SwissPalmiP14740

Proteomic databases

PaxDbiP14740
PRIDEiP14740

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P14740

Genome annotation databases

GeneIDi25253
KEGGirno:25253
UCSCiRGD:2515 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
1803
RGDi2515 Dpp4

Phylogenomic databases

eggNOGiKOG2100 Eukaryota
COG1506 LUCA
HOGENOMiHOG000231875
InParanoidiP14740
KOiK01278
OrthoDBi269253at2759
PhylomeDBiP14740

Enzyme and pathway databases

BRENDAi3.4.14.5 5301
ReactomeiR-RNO-381771 Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1)
R-RNO-400511 Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)

Miscellaneous databases

EvolutionaryTraceiP14740

Protein Ontology

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PROi
PR:P14740

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_RAT
<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: P14740
<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: April 1, 1990
Last sequence update: December 7, 2004
Last modified: December 11, 2019
This is version 165 of the entry and version 2 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
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