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Q9EPB1 (DPP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidyl peptidase 2

EC=3.4.14.2
Alternative name(s):
Dipeptidyl aminopeptidase II
Dipeptidyl peptidase 7
Dipeptidyl peptidase II
Short name=DPP II
Quiescent cell proline dipeptidase
Gene names
Name:Dpp7
Synonyms:Dpp2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the degradation of some oligopeptides.

Catalytic activity

Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.

Subunit structure

Homodimer.

Subcellular location

Lysosome. Cytoplasmic vesicle By similarity. Secreted By similarity.

Tissue specificity

Predominantly expressed in kidney, but also expressed in a variety of tissues.

Sequence similarities

Belongs to the peptidase S28 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Propeptide34 – 363
PRO_0000027318
Chain37 – 500464Dipeptidyl peptidase 2
PRO_0000027319

Sites

Active site1721Charge relay system Potential
Active site4281Charge relay system Potential
Active site4531Charge relay system Potential

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9EPB1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 401089D282CE1514

FASTA50055,114
        10         20         30         40         50         60 
MGLHPCSPVD HGVPSWVLVL LLTLGLCSLQ ATADSVLDPD FRENYFEQYM DHFNFESFSN 

        70         80         90        100        110        120 
KTFGQRFLVS DKFWKMGEGP IFFYTGNEGD IWSLANNSGF IVELAAQQEA LLVFAEHRYY 

       130        140        150        160        170        180 
GKSLPFGVQS TQRGYTQLLT VEQALADFAV LLQALRHNLG VQDAPTIAFG GSYGGMLSAY 

       190        200        210        220        230        240 
MRMKYPHLVA GALAASAPVI AVAGLGNPDQ FFRDVTADFY GQSPKCAQAV RDAFQQIKDL 

       250        260        270        280        290        300 
FLQGAYDTIS QNFGTCQSLS SPKDLTQLFG FARNAFTVLA MMDYPYPTNF LGPLPANPVK 

       310        320        330        340        350        360 
VGCERLLSEG QRIMGLRALA GLVYNSSGME PCFDIYQMYQ SCADPTGCGT GSNARAWDYQ 

       370        380        390        400        410        420 
ACTEINLTFD SNNVTDMFPE IPFSDELRQQ YCLDTWGVWP RPDWLQTSFW GGDLKAASNI 

       430        440        450        460        470        480 
IFSNGDLDPW AGGGIQRNLS TSIIAVTIQG GAHHLDLRAS NSEDPPSVVE VRKLEATLIR 

       490        500 
EWVAAARLKQ PAEAQWPGPK 

« Hide

References

« Hide 'large scale' references
[1]"Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase."
Araki H., Li Y.-H., Yamamoto Y., Haneda M., Nishi K., Kikkawa R., Ohkubo I.
J. Biochem. 129:279-288(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: Wistar.
Tissue: Kidney.
[2]"Cloning and functional expression of rat kidney dipeptidyl peptidase II."
Fukasawa K.M., Fukasawa K., Higaki K., Shiina N., Ohno M., Ito S., Otogoto J., Ota N.
Biochem. J. 353:283-290(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: Wistar.
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]Lubec G., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 67-72; 123-133; 157-184; 214-225; 264-273; 416-437 AND 459-480, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB048711 mRNA. Translation: BAB13500.1.
AB038232 mRNA. Translation: BAB11691.1.
BC078783 mRNA. Translation: AAH78783.1.
PIRJC7668.
RefSeqNP_114179.1. NM_031973.1.
UniGeneRn.3363.

3D structure databases

ProteinModelPortalQ9EPB1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9EPB1. 1 interaction.
STRING10116.ENSRNOP00000017271.

Chemistry

BindingDBQ9EPB1.
ChEMBLCHEMBL4352.

Protein family/group databases

MEROPSS28.002.

Proteomic databases

PaxDbQ9EPB1.
PRIDEQ9EPB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017271; ENSRNOP00000017271; ENSRNOG00000012640.
GeneID83799.
KEGGrno:83799.
UCSCRGD:71073. rat.

Organism-specific databases

CTD29952.
RGD71073. Dpp7.

Phylogenomic databases

eggNOGNOG290141.
GeneTreeENSGT00530000063027.
HOGENOMHOG000238311.
HOVERGENHBG005526.
InParanoidQ9EPB1.
KOK01276.
OMAVWPRPDW.
OrthoDBEOG78WKRN.
PhylomeDBQ9EPB1.
TreeFamTF314414.

Gene expression databases

GenevestigatorQ9EPB1.

Family and domain databases

InterProIPR008758. Peptidase_S28.
[Graphical view]
PANTHERPTHR11010. PTHR11010. 1 hit.
PfamPF05577. Peptidase_S28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616381.
PROQ9EPB1.

Entry information

Entry nameDPP2_RAT
AccessionPrimary (citable) accession number: Q9EPB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries