P31429 (DPEP1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 1
EC=3.4.13.19

Alternative name(s):
43 kDa renal band 3-related protein
Microsomal dipeptidase

Gene names

Name:

DPEP1

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [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 › Lagomorpha › Leporidae › Oryctolagus

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 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 Direct protein sequencing 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	Ref.1
	Chain	17 – 384	368	Dipeptidase 1		PRO_0000018658
	Propeptide	385 – 410	26	Removed in mature form By similarity		PRO_0000018659
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
	Disulfide bond	87 ↔ 170		By similarity
	Disulfide bond	242 ↔ 274		By similarity
	Disulfide bond	377		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31429 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 2033F7BFBBF2CC72	FASTA	410	45,305
	10 20 30 40 50 60 MWTSWWLWPL VAVCTADSFL DQAVQILRVT PVIDGHNDLP WQLLNKFNNR LQDSRANLTV 70 80 90 100 110 120 LADTHTNIPK LRAGFVGGQF WSAYTPCDTQ NKDTVRRTLE QMDVVHRMCQ LYPETFLCVT 130 140 150 160 170 180 DSAGIQQAFR EGKVASLIGV EGGHSIDSSL GVLRALYRLG MRYLTLTHNC NTPWADNWLV 190 200 210 220 230 240 DRGDDEAQSG GLSVFGQRVV REMNRLGVMI DLAHVSVATM KAALQLSTAP VIFSHSSAFT 250 260 270 280 290 300 VCAHKRNVPD DVLQLVKETG SLVMVNFYND YVSCASEATL SQVADHLDYI KNVAGAAAVR 310 320 330 340 350 360 FGGDFDGVTR LPVGLEDVSK YPDLVAELLR RGWTEAEVRG ALAENLLRVF REVEQVSNQA 370 380 390 400 410 QVPEEEPISL EQLGGSCRTQ YGYSEAPSLH RRPGALLASL SLLLLSLGLL

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61503 mRNA. Translation: CAA43720.1.
PIR	S18442.
RefSeq	NP_001095167.1. NM_001101697.1.
UniGene	Ocu.3249.
3D structure databases
ProteinModelPortal	P31429.
SMR	P31429. Positions 17-384.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000008950.
Protein family/group databases
MEROPS	M19.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100009273.
Organism-specific databases
CTD	1800.
Phylogenomic databases
eggNOG	COG2355.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
OrthoDB	EOG4CVG74.
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
PMAP-CutDB	P31429.

Entry information

Entry name

DPEP1_RABIT

Accession

Primary (citable) accession number: P31429

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program