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Protein

Dipeptidase 1

Gene

DPEP1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Enzyme regulationi

Inhibited by L-penicillamine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi38 – 381Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi141 – 1411Zinc 1; catalyticPROSITE-ProRule annotation
Metal bindingi141 – 1411Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei168 – 1681SubstratePROSITE-ProRule annotation
Metal bindingi214 – 2141Zinc 2; catalyticPROSITE-ProRule annotation
Metal bindingi235 – 2351Zinc 2; catalyticPROSITE-ProRule annotation
Binding sitei246 – 2461SubstratePROSITE-ProRule annotation
Binding sitei304 – 3041SubstratePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
43 kDa renal band 3-related protein
Microsomal dipeptidase
Gene namesi
Name:DPEP1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018658Add
BLAST
Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)By similarity
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
Disulfide bondi377 – 377InterchainPROSITE-ProRule annotation
Lipidationi384 – 3841GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Miscellaneous databases

PMAP-CutDBP31429.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008950.

Structurei

3D structure databases

ProteinModelPortaliP31429.
SMRiP31429. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP31429.
KOiK01273.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 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.

P31429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTSWWLWPL VAVCTADSFL DQAVQILRVT PVIDGHNDLP WQLLNKFNNR
60 70 80 90 100
LQDSRANLTV LADTHTNIPK LRAGFVGGQF WSAYTPCDTQ NKDTVRRTLE
110 120 130 140 150
QMDVVHRMCQ LYPETFLCVT DSAGIQQAFR EGKVASLIGV EGGHSIDSSL
160 170 180 190 200
GVLRALYRLG MRYLTLTHNC NTPWADNWLV DRGDDEAQSG GLSVFGQRVV
210 220 230 240 250
REMNRLGVMI DLAHVSVATM KAALQLSTAP VIFSHSSAFT VCAHKRNVPD
260 270 280 290 300
DVLQLVKETG SLVMVNFYND YVSCASEATL SQVADHLDYI KNVAGAAAVR
310 320 330 340 350
FGGDFDGVTR LPVGLEDVSK YPDLVAELLR RGWTEAEVRG ALAENLLRVF
360 370 380 390 400
REVEQVSNQA QVPEEEPISL EQLGGSCRTQ YGYSEAPSLH RRPGALLASL
410
SLLLLSLGLL
Length:410
Mass (Da):45,305
Last modified:July 1, 1993 - v1
Checksum:i2033F7BFBBF2CC72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61503 mRNA. Translation: CAA43720.1.
PIRiS18442.
RefSeqiNP_001095167.1. NM_001101697.1.
UniGeneiOcu.3249.

Genome annotation databases

GeneIDi100009273.
KEGGiocu:100009273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61503 mRNA. Translation: CAA43720.1.
PIRiS18442.
RefSeqiNP_001095167.1. NM_001101697.1.
UniGeneiOcu.3249.

3D structure databases

ProteinModelPortaliP31429.
SMRiP31429. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008950.

Protein family/group databases

MEROPSiM19.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009273.
KEGGiocu:100009273.

Organism-specific databases

CTDi1800.

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP31429.
KOiK01273.

Miscellaneous databases

PMAP-CutDBP31429.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 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. "Cloning of cDNAs encoding a rabbit renal brush border membrane protein immunologically related to band 3. Sequence similarity with microsomal dipeptidase."
    Igarashi P., Karniski L.P.
    Biochem. J. 280:71-78(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-40.
    Tissue: Kidney.

Entry informationi

Entry nameiDPEP1_RABIT
AccessioniPrimary (citable) accession number: P31429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 4, 2015
This is version 114 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, Direct protein sequencing, 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.