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P31430

- DPEP1_RAT

UniProt

P31430 - DPEP1_RAT

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Protein

Dipeptidase 1

Gene

Dpep1

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

Zinc.

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

  1. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  2. dipeptidase activity Source: RGD
  3. dipeptidyl-peptidase activity Source: InterPro
  4. GPI anchor binding Source: UniProtKB
  5. metallodipeptidase activity Source: UniProtKB
  6. modified amino acid binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. antibiotic metabolic process Source: UniProtKB
  2. cellular response to calcium ion Source: UniProtKB
  3. cellular response to drug Source: UniProtKB
  4. cellular response to nitric oxide Source: UniProtKB
  5. homocysteine metabolic process Source: UniProtKB
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cell migration Source: UniProtKB
  8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_197237. Synthesis of Leukotrienes (LT) and Eoxins (EX).
SABIO-RKP31430.

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Microsomal dipeptidase
Renal dipeptidase
Gene namesi
Name:Dpep1
Synonyms:Rdp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 19

Organism-specific databases

RGDi620324. Dpep1.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. apical part of cell Source: UniProtKB
  3. cell projection Source: UniProtKB-KW
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: Ensembl
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018660Add
BLAST
Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)By similarity
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
Glycosylationi332 – 3321N-linked (GlcNAc...)By similarity
Disulfide bondi377 – 377InterchainPROSITE-ProRule annotation
Lipidationi384 – 3841GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP31430.
PRIDEiP31430.

PTM databases

PhosphoSiteiP31430.

Expressioni

Gene expression databases

GenevestigatoriP31430.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021397.

Structurei

3D structure databases

ProteinModelPortaliP31430.
SMRiP31430. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP31430.
KOiK01273.
OMAiGHYATAM.
OrthoDBiEOG7SJD4N.
PhylomeDBiP31430.
TreeFamiTF324523.

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.

P31430-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLIIWWFWSL LAICASDSFR NQAENIMRTT PVIDGHNDLP WQMLTLFNNQ
60 70 80 90 100
LRKSEANLSA LAETHTNIPK LRAGFVGGQF WSAYMPCDTQ NKDAVKRILE
110 120 130 140 150
QIDVIHRMCQ LYPETFECVT NSSDILQAFR RGKVASLIGV EGGHLIDSSL
160 170 180 190 200
GVLRTLYHLG MRYLTLTHNC NTPWADNWLV DKGDDEAESQ GLSPFGKLVL
210 220 230 240 250
NEMNRLGVMI DLSHVSVATM KDALQLSKAP VIFSHSSAYS VCPHRRNVPD
260 270 280 290 300
DVLQLVKSTN SLVMVNFYNQ FVSCSDSATL SQVADHLDHI KKVAGAGAVG
310 320 330 340 350
LGGDYDGVTN LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLAENLLRVF
360 370 380 390 400
SAVELVSNIM QVPEEETIPV EKLDGSCRTF YGHSRAPSIH LQIGALLASL
410
ASLVFSLHLL
Length:410
Mass (Da):45,522
Last modified:May 1, 2007 - v2
Checksum:i6DD618B44523862C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti409 – 4091L → P in AAA41093. (PubMed:1420313)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94056 mRNA. Translation: AAA41093.1.
L07315 mRNA. Translation: AAA41094.1.
L07316 mRNA. Translation: AAA41095.1.
BC072476 mRNA. Translation: AAH72476.1.
PIRiS27204.
RefSeqiNP_446043.1. NM_053591.2.
XP_006255845.1. XM_006255783.2.
UniGeneiRn.6051.

Genome annotation databases

EnsembliENSRNOT00000021397; ENSRNOP00000021397; ENSRNOG00000015880.
GeneIDi94199.
KEGGirno:94199.
UCSCiRGD:620324. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94056 mRNA. Translation: AAA41093.1 .
L07315 mRNA. Translation: AAA41094.1 .
L07316 mRNA. Translation: AAA41095.1 .
BC072476 mRNA. Translation: AAH72476.1 .
PIRi S27204.
RefSeqi NP_446043.1. NM_053591.2.
XP_006255845.1. XM_006255783.2.
UniGenei Rn.6051.

3D structure databases

ProteinModelPortali P31430.
SMRi P31430. Positions 17-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021397.

Protein family/group databases

MEROPSi M19.001.

PTM databases

PhosphoSitei P31430.

Proteomic databases

PaxDbi P31430.
PRIDEi P31430.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021397 ; ENSRNOP00000021397 ; ENSRNOG00000015880 .
GeneIDi 94199.
KEGGi rno:94199.
UCSCi RGD:620324. rat.

Organism-specific databases

CTDi 1800.
RGDi 620324. Dpep1.

Phylogenomic databases

eggNOGi COG2355.
GeneTreei ENSGT00390000017920.
HOGENOMi HOG000072016.
HOVERGENi HBG002339.
InParanoidi P31430.
KOi K01273.
OMAi GHYATAM.
OrthoDBi EOG7SJD4N.
PhylomeDBi P31430.
TreeFami TF324523.

Enzyme and pathway databases

Reactomei REACT_197237. Synthesis of Leukotrienes (LT) and Eoxins (EX).
SABIO-RK P31430.

Miscellaneous databases

NextBioi 617866.
PROi P31430.

Gene expression databases

Genevestigatori P31430.

Family and domain databases

InterProi IPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view ]
PANTHERi PTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
Pfami PF01244. Peptidase_M19. 1 hit.
[Graphical view ]
PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of rat renal dipeptidase and expression of its mRNA in rat tissues and COS-1 cells."
    Adachi H., Ishida N., Tsujimoto M.
    Biochim. Biophys. Acta 1132:311-314(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  2. "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: Lung.

Entry informationi

Entry nameiDPEP1_RAT
AccessioniPrimary (citable) accession number: P31430
Secondary accession number(s): Q6IN35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 1, 2007
Last modified: October 29, 2014
This is version 127 of the entry and version 2 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