P43477 (DPEP1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 1
EC=3.4.13.19

Alternative name(s):
Microsomal dipeptidase

Gene names

Name:

DPEP1

Organism

Ovis aries (Sheep)

Taxonomic identifier

9940 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis

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. 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-anchor › GPI-anchor. Cell projection › microvillus membrane; Lipid-anchor › GPI-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 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	Direct protein sequencing
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_0000018662
	Propeptide	385 – 410	26	Removed in mature form By similarity		PRO_0000018663
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	62	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Disulfide bond	87 ↔ 170		By similarity
	Disulfide bond	242 ↔ 274		By similarity
	Disulfide bond	377		Interchain By similarity
Experimental info
	Sequence conflict	42	1	A → Q AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P43477 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: AA818C8B8BB91F31	FASTA	410	45,096
	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

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
ProteinModelPortal	P43477.
SMR	P43477. Positions 17-384.
ModBase	Search...
Protein family/group databases
MEROPS	M19.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG002339.
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...

Entry information

Entry name

DPEP1_SHEEP

Accession

Primary (citable) accession number: P43477

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program