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Protein

Dipeptidase 2

Gene

Dpep2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi90Zinc 1; catalyticPROSITE-ProRule annotation1
Metal bindingi92Zinc 1; catalyticPROSITE-ProRule annotation1
Metal bindingi189Zinc 1; catalyticPROSITE-ProRule annotation1
Metal bindingi189Zinc 2; catalyticPROSITE-ProRule annotation1
Binding sitei216SubstratePROSITE-ProRule annotation1
Metal bindingi262Zinc 2; catalyticPROSITE-ProRule annotation1
Metal bindingi283Zinc 2; catalyticPROSITE-ProRule annotation1
Binding sitei294SubstratePROSITE-ProRule annotation1
Binding sitei352SubstratePROSITE-ProRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionDipeptidase, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-2142691 Synthesis of Leukotrienes (LT) and Eoxins (EX)
R-RNO-5423646 Aflatoxin activation and detoxification

Protein family/group databases

MEROPSiM19.002

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 2 (EC:3.4.13.19)
Gene namesi
Name:Dpep2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi

Organism-specific databases

RGDi1305746 Dpep2

Subcellular locationi

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000023160731 – 462Dipeptidase 2Add BLAST432
PropeptideiPRO_0000231608463 – 481Removed in mature formSequence analysisAdd BLAST19

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi112N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi139 ↔ 218PROSITE-ProRule annotation
Glycosylationi177N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi290 ↔ 322PROSITE-ProRule annotation
Disulfide bondi427InterchainPROSITE-ProRule annotation
Lipidationi462GPI-anchor amidated serineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ5M872
PRIDEiQ5M872

Expressioni

Gene expression databases

BgeeiENSRNOG00000023303
GenevisibleiQ5M872 RN

Interactioni

Subunit structurei

Homodimer; disulfide-linked.PROSITE-ProRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000031955

Structurei

3D structure databases

ProteinModelPortaliQ5M872
SMRiQ5M872
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4127 Eukaryota
COG2355 LUCA
GeneTreeiENSGT00390000017920
HOGENOMiHOG000072016
HOVERGENiHBG002339
InParanoidiQ5M872
KOiK01273
OMAiVDGHNDM
OrthoDBiEOG091G09CU
PhylomeDBiQ5M872
TreeFamiTF324523

Family and domain databases

CDDicd01301 rDP_like, 1 hit
InterProiView protein in InterPro
IPR000180 Dipep_AS
IPR028531 Dpep2
IPR032466 Metal_Hydrolase
IPR008257 Pept_M19
PANTHERiPTHR10443 PTHR10443, 1 hit
PTHR10443:SF9 PTHR10443:SF9, 1 hit
PfamiView protein in Pfam
PF01244 Peptidase_M19, 1 hit
SUPFAMiSSF51556 SSF51556, 1 hit
PROSITEiView protein in PROSITE
PS00869 RENAL_DIPEPTIDASE_1, 1 hit
PS51365 RENAL_DIPEPTIDASE_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiDPEP2_RAT
AccessioniPrimary (citable) accession number: Q5M872
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 1, 2005
Last modified: May 23, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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