Q9DA79 (DPEP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidase 3
EC=3.4.13.19

Alternative name(s):
Membrane-bound dipeptidase 3
Short name=MBD-3
Protein expressed in male leptotene and zygotene spermatocytes 136
Short name=MLZ-136

Gene names

Name:	Dpep3
Synonyms:	Mbd3

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	493 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	Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis. Ref.4
Catalytic activity	Hydrolysis of dipeptides.
Cofactor	Zinc By similarity.
Enzyme regulation	Inhibited by L-penicillamine. Ref.1
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Membrane; Lipid-anchor › GPI-anchor Ref.1.
Tissue specificity	Expressed in testis but not ovary. Ref.1 Ref.4
Developmental stage	expressed in ovary and testis at E15.5. Ref.4
Sequence similarities	Belongs to the peptidase M19 family.
Biophysicochemical properties	Kinetic parameters: KM=2.5 mM for cystinyl-bis-glycine Ref.1

Ontologies

Keywords
Biological process	Meiosis
Cellular component	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	male meiosis Inferred from expression pattern Ref.4. Source: UniProtKB proteolysis Inferred from direct assay Ref.1. Source: MGI
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay Ref.1. Source: MGI
Molecular_function	dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro peptidase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 462	427	Dipeptidase 3		PRO_0000231613
	Propeptide	463 – 493	31	Removed in mature form Potential		PRO_0000231614
Sites
	Metal binding	94	1	Zinc 1; catalytic By similarity
	Metal binding	96	1	Zinc 1; catalytic By similarity
	Metal binding	193	1	Zinc 1; catalytic By similarity
	Metal binding	193	1	Zinc 2; catalytic By similarity
	Metal binding	266	1	Zinc 2; catalytic By similarity
	Metal binding	287	1	Zinc 2; catalytic By similarity
Amino acid modifications
	Lipidation	462	1	GPI-anchor amidated serine Potential
	Glycosylation	331	1	N-linked (GlcNAc...) Potential
	Disulfide bond	143 ↔ 222		By similarity
	Disulfide bond	294 ↔ 326		By similarity
	Disulfide bond	431		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9DA79 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B9A0D39BB7CEB619	FASTA	493	54,247
	10 20 30 40 50 60 MQPAGLEGPR ALGLRPLGHR LSLLGVLLLV PSLWVTCTLT TPSPSSAPTT PEASNATTAP 70 80 90 100 110 120 GIPNDTATSG VTSDPRLREQ ALALMRDFPL VDGHNDLPLL LRELFQNQLQ DVNLRNFTRG 130 140 150 160 170 180 QTNLDRLRDG LVGAQFWSAY IPCQTQDRDA VRLALEQIDL IRRMCSAYPE LELVTSADGL 190 200 210 220 230 240 NNTQKLACLI GVEGGHSLDT SLAVLRSFYE LGVRYLTLTF TCSTPWAESA TKFRHHFYTN 250 260 270 280 290 300 ISGLTSFGEK VVEEMNRLGM MIDLSHASDT LVKQTLEVSQ APVIFSHSAA RSVCDNLLNI 310 320 330 340 350 360 PDDILQLLKK NGGIVMVTLS MGVLQCSLFA NVSTVADHFD HIRTVIGSEF IGIGGSYDGS 370 380 390 400 410 420 GRFPQGLEDV STYPVLIEEL LSRGWDEREL QGVLRGNLLR VFRQVEQVRE KSLGQSPVEV 430 440 450 460 470 480 KFPERQQSNT CHSHLLPQPQ EDQHQDTHLK VTKLPNILQR ASKAPPHPLP GLMATLTSLA 490 LILWLCCSGH RAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION. Strain: L129. Tissue: Spleen and Testis.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[3]	"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: Testis.
[4]	"Screening of genes involved in chromosome segregation during meiosis I: toward the identification of genes responsible for infertility in humans." Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T., Inagaki H., Taniguchi M., Toda T., Kurahashi H. J. Hum. Genet. 55:293-299(2010) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, FUNCTION, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF488553 mRNA. Translation: AAP84987.1. AK006085 mRNA. Translation: BAB24402.1. BC051148 mRNA. Translation: AAH51148.1.
IPI	IPI00118037.
RefSeq	NP_082236.1. NM_027960.2.
UniGene	Mm.173395.
3D structure databases
ProteinModelPortal	Q9DA79.
SMR	Q9DA79. Positions 77-434.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-8174108.
Protein family/group databases
MEROPS	M19.011.
PTM databases
PhosphoSite	Q9DA79.
Proteomic databases
PaxDb	Q9DA79.
PRIDE	Q9DA79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034371; ENSMUSP00000034371; ENSMUSG00000031898.
GeneID	71854.
KEGG	mmu:71854.
UCSC	uc009net.1. mouse.
Organism-specific databases
CTD	64180.
MGI	MGI:1919104. Dpep3.
Phylogenomic databases
eggNOG	COG2355.
GeneTree	ENSGT00390000017920.
HOGENOM	HOG000072016.
HOVERGEN	HBG002339.
InParanoid	Q9DA79.
OMA	HIDYLIN.
OrthoDB	EOG4X97J0.
Gene expression databases
Bgee	Q9DA79.
CleanEx	MM_DPEP3. MM_MBD3.
Genevestigator	Q9DA79.
GermOnline	ENSMUSG00000031898. 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	334738.
SOURCE	Search...

Entry information

Entry name

DPEP3_MOUSE

Accession

Primary (citable) accession number: Q9DA79

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program