P31430 (DPEP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 1
EC=3.4.13.19

Alternative name(s):
Microsomal dipeptidase
Renal dipeptidase

Gene names

Name:	Dpep1
Synonyms:	Rdp

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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 transcript 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 By similarity.
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.

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
	Chain	17 – 384	368	Dipeptidase 1		PRO_0000018660
	Propeptide	385 – 410	26	Removed in mature form By similarity		PRO_0000018661
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	57	1	N-linked (GlcNAc...) By similarity
	Glycosylation	121	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	409	1	L → P in AAA41093. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31430 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 6DD618B44523862C	FASTA	410	45,522
	10 20 30 40 50 60 MLIIWWFWSL LAICASDSFR NQAENIMRTT PVIDGHNDLP WQMLTLFNNQ LRKSEANLSA 70 80 90 100 110 120 LAETHTNIPK LRAGFVGGQF WSAYMPCDTQ NKDAVKRILE QIDVIHRMCQ LYPETFECVT 130 140 150 160 170 180 NSSDILQAFR RGKVASLIGV EGGHLIDSSL GVLRTLYHLG MRYLTLTHNC NTPWADNWLV 190 200 210 220 230 240 DKGDDEAESQ GLSPFGKLVL NEMNRLGVMI DLSHVSVATM KDALQLSKAP VIFSHSSAYS 250 260 270 280 290 300 VCPHRRNVPD DVLQLVKSTN SLVMVNFYNQ FVSCSDSATL SQVADHLDHI KKVAGAGAVG 310 320 330 340 350 360 LGGDYDGVTN LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLAENLLRVF SAVELVSNIM 370 380 390 400 410 QVPEEETIPV EKLDGSCRTF YGHSRAPSIH LQIGALLASL ASLVFSLHLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M94056 mRNA. Translation: AAA41093.1. L07315 mRNA. Translation: AAA41094.1. L07316 mRNA. Translation: AAA41095.1. BC072476 mRNA. Translation: AAH72476.1.
IPI	IPI00327697.
PIR	S27204.
RefSeq	NP_446043.1. NM_053591.2.
UniGene	Rn.6051.
3D structure databases
ProteinModelPortal	P31430.
SMR	P31430. Positions 17-384.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000021397.
Protein family/group databases
MEROPS	M19.001.
PTM databases
PhosphoSite	P31430.
Proteomic databases
PaxDb	P31430.
PRIDE	P31430.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000021397; ENSRNOP00000021397; ENSRNOG00000015880.
GeneID	94199.
KEGG	rno:94199.
UCSC	RGD:620324. rat.
Organism-specific databases
CTD	1800.
RGD	620324. Dpep1.
Phylogenomic databases
eggNOG	COG2355.
GeneTree	ENSGT00390000017920.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
InParanoid	P31430.
KO	K01273.
OMA	YITLAHS.
OrthoDB	EOG4CVG74.
Enzyme and pathway databases
SABIO-RK	P31430.
Gene expression databases
Genevestigator	P31430.
GermOnline	ENSRNOG00000015880. Rattus norvegicus.
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	617866.

Entry information

Entry name

DPEP1_RAT

Accession

Primary (citable) accession number: P31430
Secondary accession number(s): Q6IN35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program