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Q9DA79 (DPEP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-anchorGPI-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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 462427Dipeptidase 3
PRO_0000231613
Propeptide463 – 49331Removed in mature form Potential
PRO_0000231614

Sites

Metal binding941Zinc 1; catalytic By similarity
Metal binding961Zinc 1; catalytic By similarity
Metal binding1931Zinc 1; catalytic By similarity
Metal binding1931Zinc 2; catalytic By similarity
Metal binding2661Zinc 2; catalytic By similarity
Metal binding2871Zinc 2; catalytic By similarity

Amino acid modifications

Lipidation4621GPI-anchor amidated serine Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond143 ↔ 222 By similarity
Disulfide bond294 ↔ 326 By similarity
Disulfide bond431Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DA79 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B9A0D39BB7CEB619

FASTA49354,247
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_082236.1. NM_027960.2.
UniGeneMm.173395.

3D structure databases

ProteinModelPortalQ9DA79.
SMRQ9DA79. Positions 77-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DA79. 1 interaction.
MINTMINT-8174108.

Protein family/group databases

MEROPSM19.011.

PTM databases

PhosphoSiteQ9DA79.

Proteomic databases

PaxDbQ9DA79.
PRIDEQ9DA79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034371; ENSMUSP00000034371; ENSMUSG00000031898.
GeneID71854.
KEGGmmu:71854.
UCSCuc009net.1. mouse.

Organism-specific databases

CTD64180.
MGIMGI:1919104. Dpep3.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidQ9DA79.
OMAKFRHHFY.
OrthoDBEOG7SJD4N.
PhylomeDBQ9DA79.
TreeFamTF324523.

Gene expression databases

BgeeQ9DA79.
CleanExMM_DPEP3.
MM_MBD3.
GenevestigatorQ9DA79.

Family and domain databases

InterProIPR028533. Dpep3.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF14. PTHR10443:SF14. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio334738.
PROQ9DA79.
SOURCESearch...

Entry information

Entry nameDPEP3_MOUSE
AccessionPrimary (citable) accession number: Q9DA79
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot