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Q5M872 (DPEP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. 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 2

EC=3.4.13.19
Gene names
Name:Dpep2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length481 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 leukotriene D4 (LTD4) into leukotriene E4 (LTE4) 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 – 3030 Potential
Chain31 – 462432Dipeptidase 2
PRO_0000231607
Propeptide463 – 48119Removed in mature form Potential
PRO_0000231608

Sites

Metal binding901Zinc 1; catalytic By similarity
Metal binding921Zinc 1; catalytic By similarity
Metal binding1891Zinc 1; catalytic By similarity
Metal binding1891Zinc 2; catalytic By similarity
Metal binding2621Zinc 2; catalytic By similarity
Metal binding2831Zinc 2; catalytic By similarity
Binding site2161Substrate By similarity
Binding site2941Substrate By similarity
Binding site3521Substrate By similarity

Amino acid modifications

Lipidation4621GPI-anchor amidated serine Potential
Glycosylation1121N-linked (GlcNAc...) By similarity
Glycosylation1771N-linked (GlcNAc...) Potential
Disulfide bond139 ↔ 218 By similarity
Disulfide bond290 ↔ 322 By similarity
Disulfide bond427Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M872 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: DC39B50C10A96AC1

FASTA48153,285
        10         20         30         40         50         60 
MSLKGLEGHW VLSQVFLLVV VLLLLGPSEP LIRAQTKPGI ADASTAPSPL RTLTKPAIFS 

        70         80         90        100        110        120 
IPTTPGNPNF PDLRDRTRAL MQDFPLIDGH NDLPLVLRQF YQNGLQDTNL RNFTHGQTSL 

       130        140        150        160        170        180 
NRLKDGFVGA QFWSAYVPCQ TQDRDALRLT LEQIDLIRRM CASYSELELV TSVQALNSTQ 

       190        200        210        220        230        240 
KLACLIGVEG GHSLDNSLAV LRSFYLLGVR YLTLTHTCNT PWAESSSKDV HSFYSSVKGL 

       250        260        270        280        290        300 
TSFGEKVVAE MNRLGMMIDL SHVSDATARQ ALEVSQAPVI FSHSAARAVC PNARNLPDDI 

       310        320        330        340        350        360 
LQLLKKNGGI VMVTFAVGVL PCNPLANVST VADHFDHIRT VIGSEFIGVG GDYDGTKQFP 

       370        380        390        400        410        420 
QGLEDVSTYP VLIEELLRRG WGEQELQGVL RGNLLRVFRQ VEQVREKNKW QSPLEDMIPE 

       430        440        450        460        470        480 
EQLDSACHSV LPHRRQYPEK DPPETPDSHT HKLSPKMPYS KSSPLRASSL TIMATFLGLL 


I 

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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: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC088195 mRNA. Translation: AAH88195.1.
RefSeqNP_001011928.1. NM_001011928.1.
UniGeneRn.20731.

3D structure databases

ProteinModelPortalQ5M872.
SMRQ5M872. Positions 72-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000031955.

Protein family/group databases

MEROPSM19.004.

Proteomic databases

PRIDEQ5M872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000034722; ENSRNOP00000031955; ENSRNOG00000023303.
GeneID291984.
KEGGrno:291984.
UCSCRGD:1305746. rat.

Organism-specific databases

CTD64174.
RGD1305746. Dpep2.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidQ5M872.
OMADTQKLAC.
OrthoDBEOG7SJD4N.
PhylomeDBQ5M872.
TreeFamTF324523.

Gene expression databases

GenevestigatorQ5M872.

Family and domain databases

InterProIPR028531. Dpep2.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF9. PTHR10443:SF9. 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

NextBio633560.
PROQ5M872.

Entry information

Entry nameDPEP2_RAT
AccessionPrimary (citable) accession number: Q5M872
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 65 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