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Protein

Dipeptidase 2

Gene

Dpep2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).By similarity

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+PROSITE-ProRule annotation

Enzyme regulationi

Inhibited by L-penicillamine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi92 – 921Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi189 – 1891Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi189 – 1891Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei216 – 2161SubstratePROSITE-ProRule annotation
Metal bindingi262 – 2621Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi283 – 2831Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei294 – 2941SubstratePROSITE-ProRule annotation
Binding sitei352 – 3521SubstratePROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM19.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 2 (EC:3.4.13.19)
Gene namesi
Name:Dpep2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1305746. Dpep2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 462432Dipeptidase 2PRO_0000231607Add
BLAST
Propeptidei463 – 48119Removed in mature formSequence AnalysisPRO_0000231608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)By similarity
Disulfide bondi139 ↔ 218PROSITE-ProRule annotation
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi290 ↔ 322PROSITE-ProRule annotation
Disulfide bondi427 – 427InterchainPROSITE-ProRule annotation
Lipidationi462 – 4621GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiQ5M872.

Expressioni

Gene expression databases

GenevisibleiQ5M872. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.PROSITE-ProRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000031955.

Structurei

3D structure databases

ProteinModelPortaliQ5M872.
SMRiQ5M872. Positions 72-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ5M872.
KOiK01273.
OMAiRALMRNF.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ5M872.
TreeFamiTF324523.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028531. Dpep2.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF9. PTHR10443:SF9. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5M872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKGLEGHW VLSQVFLLVV VLLLLGPSEP LIRAQTKPGI ADASTAPSPL
60 70 80 90 100
RTLTKPAIFS IPTTPGNPNF PDLRDRTRAL MQDFPLIDGH NDLPLVLRQF
110 120 130 140 150
YQNGLQDTNL RNFTHGQTSL NRLKDGFVGA QFWSAYVPCQ TQDRDALRLT
160 170 180 190 200
LEQIDLIRRM CASYSELELV TSVQALNSTQ KLACLIGVEG GHSLDNSLAV
210 220 230 240 250
LRSFYLLGVR YLTLTHTCNT PWAESSSKDV HSFYSSVKGL TSFGEKVVAE
260 270 280 290 300
MNRLGMMIDL SHVSDATARQ ALEVSQAPVI FSHSAARAVC PNARNLPDDI
310 320 330 340 350
LQLLKKNGGI VMVTFAVGVL PCNPLANVST VADHFDHIRT VIGSEFIGVG
360 370 380 390 400
GDYDGTKQFP QGLEDVSTYP VLIEELLRRG WGEQELQGVL RGNLLRVFRQ
410 420 430 440 450
VEQVREKNKW QSPLEDMIPE EQLDSACHSV LPHRRQYPEK DPPETPDSHT
460 470 480
HKLSPKMPYS KSSPLRASSL TIMATFLGLL I
Length:481
Mass (Da):53,285
Last modified:February 1, 2005 - v1
Checksum:iDC39B50C10A96AC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088195 mRNA. Translation: AAH88195.1.
RefSeqiNP_001011928.1. NM_001011928.1.
UniGeneiRn.20731.

Genome annotation databases

EnsembliENSRNOT00000034722; ENSRNOP00000031955; ENSRNOG00000023303.
GeneIDi291984.
KEGGirno:291984.
UCSCiRGD:1305746. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088195 mRNA. Translation: AAH88195.1.
RefSeqiNP_001011928.1. NM_001011928.1.
UniGeneiRn.20731.

3D structure databases

ProteinModelPortaliQ5M872.
SMRiQ5M872. Positions 72-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000031955.

Protein family/group databases

MEROPSiM19.004.

Proteomic databases

PRIDEiQ5M872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000034722; ENSRNOP00000031955; ENSRNOG00000023303.
GeneIDi291984.
KEGGirno:291984.
UCSCiRGD:1305746. rat.

Organism-specific databases

CTDi64174.
RGDi1305746. Dpep2.

Phylogenomic databases

eggNOGiCOG2355.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiQ5M872.
KOiK01273.
OMAiRALMRNF.
OrthoDBiEOG7SJD4N.
PhylomeDBiQ5M872.
TreeFamiTF324523.

Miscellaneous databases

NextBioi633560.
PROiQ5M872.

Gene expression databases

GenevisibleiQ5M872. RN.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028531. Dpep2.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF9. PTHR10443:SF9. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiDPEP2_RAT
AccessioniPrimary (citable) accession number: Q5M872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 1, 2005
Last modified: July 22, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.