Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5U2X4 (DPEP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:
Dipeptidase 3

EC=3.4.13.19
Gene names
Name:Dpep3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis By similarity.

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc By similarity.

Enzyme regulation

Inhibited by L-penicillamine By similarity.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Membrane; Lipid-anchorGPI-anchor By similarity.

Sequence similarities

Belongs to the peptidase M19 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 459424Dipeptidase 3
PRO_0000231615
Propeptide460 – 48728Removed in mature form Potential
PRO_0000231616

Sites

Metal binding941Zinc 1; catalytic By similarity
Metal binding961Zinc 1; catalytic By similarity
Metal binding1931Zinc 1; catalytic By similarity
Metal binding1931Zinc 2; catalytic By similarity
Metal binding2661Zinc 2; catalytic By similarity
Metal binding2871Zinc 2; catalytic By similarity

Amino acid modifications

Lipidation4591GPI-anchor amidated serine Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond143 ↔ 222 By similarity
Disulfide bond294 ↔ 326 By similarity
Disulfide bond431Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5U2X4 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: E22FCAC7902144C5

FASTA48853,370
        10         20         30         40         50         60 
MQPTGPEGPR ALSLRPLGHR LSLLGVLLII PSLWVTCNQT TPSLSSAPTS PGASSAMTTP 

        70         80         90        100        110        120 
GIPNDTTTSG VTSDPRLREQ ALALMRDFPL VDGHNDLPLL LRELFQNKLQ DVNLHNFTRG 

       130        140        150        160        170        180 
QTSLDRLRDG LVGAQFWSAY IPCQTQDRDA VRVALEQIDL IRRMCSAYPE LELVTSADGL 

       190        200        210        220        230        240 
NSTQKLACLI GLEGGHSLDT SLAVLRSFYE LGVRYLTLTF TCSTPWAESA TKFRHHFYTN 

       250        260        270        280        290        300 
ISGLTSFGEK VVEEMNRIGM MIDLSHASDT LVKQTLEASR APVIFSHSAA RSVCDNLLNV 

       310        320        330        340        350        360 
PDDILQLLKK NGGIVMVTLS MGVLQCSLLA NVSTVADHFD HIRTVIGSEF IGIGGSYDGS 

       370        380        390        400        410        420 
GRFPQGLEDV STYPVLLEEL LRRGWGEQEL QGVLRGNLLR VFRQVEQVRE KSLGQSPVEV 

       430        440        450        460        470        480 
VFPERQQSST CHSHLLPQSQ DAHLKVTKLP SSQVLQRASK APPCPLLGLV AAVTSPAFTL 


WLCCSGHR 

« Hide

References

[1]"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: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC085826 mRNA. Translation: AAH85826.1.
RefSeqNP_001008384.1. NM_001008383.1.
XP_006255579.1. XM_006255517.1.
UniGeneRn.111627.

3D structure databases

ProteinModelPortalQ5U2X4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026809.

Protein family/group databases

MEROPSM19.011.

Proteomic databases

PRIDEQ5U2X4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026809; ENSRNOP00000026809; ENSRNOG00000019757.
GeneID364994.
KEGGrno:364994.
UCSCRGD:1305484. rat.

Organism-specific databases

CTD64180.
RGD1305484. Dpep3.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidQ5U2X4.
OMAKFRHHFY.
OrthoDBEOG7SJD4N.
PhylomeDBQ5U2X4.
TreeFamTF324523.

Gene expression databases

GenevestigatorQ5U2X4.

Family and domain databases

InterProIPR028533. Dpep3.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF14. PTHR10443:SF14. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio686443.
PROQ5U2X4.

Entry information

Entry nameDPEP3_RAT
AccessionPrimary (citable) accession number: Q5U2X4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 70 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