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Protein

Dipeptidase 1

Gene

DPEP1

Organism
Ovis aries (Sheep)
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. In lung tissue, it may terminate or significantly reduce the leukotriene induced signal for bronchospasm.1 Publication

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

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

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Microsomal dipeptidase
Gene namesi
Name:DPEP1
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. apical part of cell Source: UniProtKB
  3. apical plasma membrane Source: UniProtKB-SubCell
  4. extracellular space Source: UniProtKB
  5. microvillus membrane Source: UniProtKB-SubCell
  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 – 1616By similarityAdd
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018662Add
BLAST
Propeptidei385 – 41026Removed in mature formBy similarityPRO_0000018663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)By similarity
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi377 – 377InterchainPROSITE-ProRule annotation
Lipidationi384 – 3841GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

Expressed in lung, kidney and intestinal tissues.1 Publication

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Structurei

3D structure databases

ProteinModelPortaliP43477.
SMRiP43477. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG002339.

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.

P43477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTGWWLWPL VAVCTADQFR DNAVRLMQST PVIDGHNDLP WALLKKFNNQ
60 70 80 90 100
LQDPRANLTS LNSTHTNIPK LKAGFVGAQF WSAYTPCDTQ NKDSVKRTVE
110 120 130 140 150
QIDVIQRMCQ LYPETFLCVT DSAGIQQAFQ EGKVASLVGV EGGHSIDSSL
160 170 180 190 200
GVLRALYHLG MRYLTLTHSC NTPWADNWLV DTGEDKAQSQ GLSSFGQSVV
210 220 230 240 250
KEMNRLGIII DLAHVSVATM EAALQLSKAP VIFSHSSAYS LCHHRRNVPD
260 270 280 290 300
HVLQLVKQTG SLVMVNFYND YVSCKAEANL SQVADHLDYI KKVAGAGAVG
310 320 330 340 350
FGGDYDGVSR LPSGLEDVSK YPDLVAELLR RQWTEEEVRG ALAENLLRVF
360 370 380 390 400
KAVEQASDHK QAPGEEPIPL GQLEASCRTK YGYSGTPSLH LQPGSLLASL
410
VTLLLSLCLL
Length:410
Mass (Da):45,096
Last modified:November 1, 1995 - v1
Checksum:iAA818C8B8BB91F31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421A → Q AA sequence (PubMed:8054366).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27113 mRNA. Translation: AAA21725.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27113 mRNA. Translation: AAA21725.1.

3D structure databases

ProteinModelPortaliP43477.
SMRiP43477. Positions 17-384.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM19.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG002339.

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. "Molecular cloning of sheep lung dipeptidase: a glycosyl phosphatidylinositol-anchored ectoenzyme that converts leukotriene D4 to leukotriene E4."
    An S., Schmidt F.J., Campbell B.J.
    Biochim. Biophys. Acta 1226:337-340(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-56, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Lung.

Entry informationi

Entry nameiDPEP1_SHEEP
AccessioniPrimary (citable) accession number: P43477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 98 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.