P31428 (DPEP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 1
EC=3.4.13.19

Alternative name(s):
Membrane-bound dipeptidase 1
Short name=MBD-1
Microsomal dipeptidase
Renal dipeptidase

Gene names

Name:	Dpep1
Synonyms:	Mbd1, Rdp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	Hydrolysis of dipeptides.
Cofactor	Zinc.
Enzyme regulation	Inhibited by L-penicillamine. Ref.4
Subunit structure	Homodimer; disulfide-linked.
Subcellular location	Apical cell membrane; Lipid-anchor › GPI-anchor. Cell projection › microvillus membrane; Lipid-anchor › GPI-anchor. Note: Brush border membrane.
Sequence similarities	Belongs to the peptidase M19 family.
Biophysicochemical properties	Kinetic parameters: KM=10 µM for leukotriene D4 Ref.4 KM=0.45 mM for cystinyl-bis-glycine KM=111 µM for beta-lactam

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Membrane
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Dipeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antibiotic 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to 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_function	GPI 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	By similarity
	Chain	17 – 384	368	Dipeptidase 1		PRO_0000018654
	Propeptide	385 – 410	26	Removed in mature form By similarity		PRO_0000018655
Sites
	Metal binding	36	1	Zinc 1; catalytic By similarity
	Metal binding	38	1	Zinc 1; catalytic By similarity
	Metal binding	141	1	Zinc 1; catalytic By similarity
	Metal binding	141	1	Zinc 2; catalytic By similarity
	Metal binding	214	1	Zinc 2; catalytic By similarity
	Metal binding	235	1	Zinc 2; catalytic By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	246	1	Substrate By similarity
	Binding site	304	1	Substrate By similarity
Amino acid modifications
	Lipidation	384	1	GPI-anchor amidated serine By similarity
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Glycosylation	258	1	N-linked (GlcNAc...) Potential
	Glycosylation	332	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	87 ↔ 170		By similarity
	Disulfide bond	242 ↔ 274		By similarity
	Disulfide bond	377		Interchain By similarity
Experimental info
	Sequence conflict	204	1	N → T in BAA02432. Ref.1
	Sequence conflict	358	1	N → S in BAA02432. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31428 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 46A454B51CA57BB5	FASTA	410	45,722
	10 20 30 40 50 60 MVIIWWFWSL LAICASDSFR DQAVAIMRTT PVIDGHNDLP WQLLNLFNNQ LLRPDADLNK 70 80 90 100 110 120 LAQTHTNIPK LKAGFVGGQF WSAYMPCDTQ NKDAVKRILE QMDVIHRMCQ LYPETFMCVT 130 140 150 160 170 180 NSSDILQAFR RGKVASLIGV EGGHLIDSSL GVLRTLYHLG MRYLTLTHNC NTPWADNWLV 190 200 210 220 230 240 DRGDDEAESH GLSPFGKRLL NEMNRLGVMI DLSHVSVATM KDALQISRAP VIFSHSSAYS 250 260 270 280 290 300 LCPHRRNVPD DVLQLVKNTS SLVMVNFFSN FVSCSDSATL PQVADHLDHI KKVAGAGAVG 310 320 330 340 350 360 LGGDYDGVTM LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLADNLIRVF SEVELVSNNM 370 380 390 400 410 QSPEEVPITL KELDGSCRTY YGYSQAHSIH LQTGALVASL ASLLFRLHLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and molecular cloning of mouse renal dipeptidase." Satoh S., Keida Y., Konta Y., Maeda M., Matsumoto Y., Niwa M., Kohsaka M. Biochim. Biophys. Acta 1163:234-242(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Identification of two additional members of the membrane-bound dipeptidase family." Habib G.M., Shi Z.-Z., Cuevas A.A., Lieberman M.W. FASEB J. 17:1313-1315(2003) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13139 mRNA. Translation: BAA02432.1. AC163617 Genomic DNA. No translation available. CH466525 Genomic DNA. Translation: EDL11712.1.
IPI	IPI00134390.
PIR	S33757.
RefSeq	NP_031902.2. NM_007876.2.
UniGene	Mm.20388.
3D structure databases
ProteinModelPortal	P31428.
SMR	P31428. Positions 17-384.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000019422.
Protein family/group databases
MEROPS	M19.001.
PTM databases
PhosphoSite	P31428.
Proteomic databases
PaxDb	P31428.
PRIDE	P31428.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019422; ENSMUSP00000019422; ENSMUSG00000019278.
GeneID	13479.
KEGG	mmu:13479.
UCSC	uc009nui.2. mouse.
Organism-specific databases
CTD	1800.
MGI	MGI:94917. Dpep1.
Phylogenomic databases
eggNOG	COG2355.
GeneTree	ENSGT00390000017920.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
InParanoid	P31428.
KO	K01273.
OMA	CETQNKD.
OrthoDB	EOG4CVG74.
Gene expression databases
CleanEx	MM_DPEP1. MM_MBD1.
Genevestigator	P31428.
GermOnline	ENSMUSG00000019278. Mus musculus.
Family and domain databases
InterPro	IPR000180. Pept_M19_AS. IPR008257. Peptidase_M19. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit.
Pfam	PF01244. Peptidase_M19. 1 hit. [Graphical view]
PROSITE	PS00869. RENAL_DIPEPTIDASE_1. 1 hit. PS51365. RENAL_DIPEPTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	283967.
SOURCE	Search...

Entry information

Entry name

DPEP1_MOUSE

Accession

Primary (citable) accession number: P31428
Secondary accession number(s): G5E824

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program