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P31429

- DPEP1_RABIT

UniProt

P31429 - DPEP1_RABIT

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Protein

Dipeptidase 1

Gene
DPEP1
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by L-penicillamine By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc 1; catalytic By similarity
Metal bindingi38 – 381Zinc 1; catalytic By similarity
Metal bindingi141 – 1411Zinc 1; catalytic By similarity
Metal bindingi141 – 1411Zinc 2; catalytic By similarity
Binding sitei168 – 1681Substrate By similarity
Metal bindingi214 – 2141Zinc 2; catalytic By similarity
Metal bindingi235 – 2351Zinc 2; catalytic By similarity
Binding sitei246 – 2461Substrate By similarity
Binding sitei304 – 3041Substrate By similarity

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):
43 kDa renal band 3-related protein
Microsomal dipeptidase
Gene namesi
Name:DPEP1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: 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 – 16161 PublicationAdd
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018658Add
BLAST
Propeptidei385 – 41026Removed in mature form By similarityPRO_0000018659Add
BLAST

Amino acid modifications

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

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
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.

P31429-1 [UniParc]FASTAAdd to Basket

« Hide

MWTSWWLWPL VAVCTADSFL DQAVQILRVT PVIDGHNDLP WQLLNKFNNR    50
LQDSRANLTV LADTHTNIPK LRAGFVGGQF WSAYTPCDTQ NKDTVRRTLE 100
QMDVVHRMCQ LYPETFLCVT DSAGIQQAFR EGKVASLIGV EGGHSIDSSL 150
GVLRALYRLG MRYLTLTHNC NTPWADNWLV DRGDDEAQSG GLSVFGQRVV 200
REMNRLGVMI DLAHVSVATM KAALQLSTAP VIFSHSSAFT VCAHKRNVPD 250
DVLQLVKETG SLVMVNFYND YVSCASEATL SQVADHLDYI KNVAGAAAVR 300
FGGDFDGVTR LPVGLEDVSK YPDLVAELLR RGWTEAEVRG ALAENLLRVF 350
REVEQVSNQA QVPEEEPISL EQLGGSCRTQ YGYSEAPSLH RRPGALLASL 400
SLLLLSLGLL 410
Length:410
Mass (Da):45,305
Last modified:July 1, 1993 - v1
Checksum:i2033F7BFBBF2CC72
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61503 mRNA. Translation: CAA43720.1.
PIRiS18442.
RefSeqiNP_001095167.1. NM_001101697.1.
UniGeneiOcu.3249.

Genome annotation databases

GeneIDi100009273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61503 mRNA. Translation: CAA43720.1 .
PIRi S18442.
RefSeqi NP_001095167.1. NM_001101697.1.
UniGenei Ocu.3249.

3D structure databases

ProteinModelPortali P31429.
SMRi P31429. Positions 17-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000008950.

Protein family/group databases

MEROPSi M19.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009273.

Organism-specific databases

CTDi 1800.

Phylogenomic databases

eggNOGi COG2355.
HOGENOMi HOG000072016.
HOVERGENi HBG002339.

Miscellaneous databases

PMAP-CutDB P31429.

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

  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: September 3, 2014
This is version 109 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

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