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P43477 (DPEP1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidase 1

EC=3.4.13.19
Alternative name(s):
Microsomal dipeptidase
Gene names
Name:DPEP1
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc.

Enzyme regulation

Inhibited by L-penicillamine By similarity.

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Apical cell membrane; Lipid-anchorGPI-anchor. Cell projectionmicrovillus membrane; Lipid-anchorGPI-anchor. Note: Brush border membrane.

Tissue specificity

Expressed in lung, kidney and intestinal tissues. Ref.1

Sequence similarities

Belongs to the peptidase M19 family.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionDipeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantibiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nitric oxide

Inferred from sequence or structural similarity. Source: UniProtKB

homocysteine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

apical part of cell

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGPI anchor binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

dipeptidyl-peptidase activity

Inferred from electronic annotation. Source: InterPro

metallodipeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

modified amino acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 By similarity
Chain17 – 384368Dipeptidase 1
PRO_0000018662
Propeptide385 – 41026Removed in mature form By similarity
PRO_0000018663

Sites

Metal binding361Zinc 1; catalytic By similarity
Metal binding381Zinc 1; catalytic By similarity
Metal binding1411Zinc 1; catalytic By similarity
Metal binding1411Zinc 2; catalytic By similarity
Metal binding2141Zinc 2; catalytic By similarity
Metal binding2351Zinc 2; catalytic By similarity
Binding site1681Substrate By similarity
Binding site2461Substrate By similarity
Binding site3041Substrate By similarity

Amino acid modifications

Lipidation3841GPI-anchor amidated serine By similarity
Glycosylation571N-linked (GlcNAc...) By similarity
Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 170 By similarity
Disulfide bond242 ↔ 274 By similarity
Disulfide bond377Interchain By similarity

Experimental info

Sequence conflict421A → Q AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P43477 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: AA818C8B8BB91F31

FASTA41045,096
        10         20         30         40         50         60 
MWTGWWLWPL VAVCTADQFR DNAVRLMQST PVIDGHNDLP WALLKKFNNQ LQDPRANLTS 

        70         80         90        100        110        120 
LNSTHTNIPK LKAGFVGAQF WSAYTPCDTQ NKDSVKRTVE QIDVIQRMCQ LYPETFLCVT 

       130        140        150        160        170        180 
DSAGIQQAFQ EGKVASLVGV EGGHSIDSSL GVLRALYHLG MRYLTLTHSC NTPWADNWLV 

       190        200        210        220        230        240 
DTGEDKAQSQ GLSSFGQSVV KEMNRLGIII DLAHVSVATM EAALQLSKAP VIFSHSSAYS 

       250        260        270        280        290        300 
LCHHRRNVPD HVLQLVKQTG SLVMVNFYND YVSCKAEANL SQVADHLDYI KKVAGAGAVG 

       310        320        330        340        350        360 
FGGDYDGVSR LPSGLEDVSK YPDLVAELLR RQWTEEEVRG ALAENLLRVF KAVEQASDHK 

       370        380        390        400        410 
QAPGEEPIPL GQLEASCRTK YGYSGTPSLH LQPGSLLASL VTLLLSLCLL 

« Hide

References

[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(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-56, FUNCTION, TISSUE SPECIFICITY.
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27113 mRNA. Translation: AAA21725.1.

3D structure databases

ProteinModelPortalP43477.
SMRP43477. Positions 17-384.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM19.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002339.

Family and domain databases

InterProIPR028536. Dpep1.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPEP1_SHEEP
AccessionPrimary (citable) accession number: P43477
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries