Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8C255 (DPEP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidase 2

EC=3.4.13.19
Alternative name(s):
Membrane-bound dipeptidase 2
Short name=MBD-2
Gene names
Name:Dpep2
Synonyms:Mbd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length478 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 leukotriene D4 (LTD4) into leukotriene E4 (LTE4).

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 heart, lung, testis, spleen and skeletal muscle. Ref.1

Sequence similarities

Belongs to the peptidase M19 family.

Biophysicochemical properties

Kinetic parameters:

KM=5 µM for LTD4 Ref.1

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8C255-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8C255-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAWHGETYCL...VPACSALSKM
     176-179: ALNS → VKWIYSG
     334-340: DHFDHIR → EKGQQKHQFTPPRDTHFV
Isoform 3 (identifier: Q8C255-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 459428Dipeptidase 2
PRO_0000231605
Propeptide460 – 47819Removed in mature form Potential
PRO_0000231606

Sites

Metal binding911Zinc 1; catalytic By similarity
Metal binding931Zinc 1; catalytic By similarity
Metal binding1901Zinc 1; catalytic By similarity
Metal binding1901Zinc 2; catalytic By similarity
Metal binding2631Zinc 2; catalytic By similarity
Metal binding2841Zinc 2; catalytic By similarity
Binding site2171Substrate By similarity
Binding site2951Substrate By similarity
Binding site3531Substrate By similarity

Amino acid modifications

Lipidation4591GPI-anchor amidated serine Potential
Glycosylation1131N-linked (GlcNAc...) By similarity
Glycosylation1781N-linked (GlcNAc...) Potential
Disulfide bond140 ↔ 219 By similarity
Disulfide bond291 ↔ 323 By similarity
Disulfide bond428Interchain By similarity

Natural variations

Alternative sequence1 – 9393Missing in isoform 3.
VSP_017852
Alternative sequence11M → MAWHGETYCLIGGYRVYGDA PLPTPAKAEQEEKPVPRRAP KRQRVQEESDQDLGCPGAKV PRLKLKHGGKGLSRPSSVPA CSALSKM in isoform 2.
VSP_017853
Alternative sequence176 – 1794ALNS → VKWIYSG in isoform 2.
VSP_017854
Alternative sequence334 – 3407DHFDHIR → EKGQQKHQFTPPRDTHFV in isoform 2.
VSP_017855

Experimental info

Sequence conflict781A → T in BAE42354. Ref.2
Sequence conflict891D → G in BAE42559. Ref.2
Sequence conflict991R → G in BAE42559. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0790B97009F5D41F

FASTA47852,664
        10         20         30         40         50         60 
MSLTGLKGHW VLGHGLSVFL LVLLLLGPSQ PLIWTQTKPG FSGASTTSSI PRALTKPDIS 

        70         80         90        100        110        120 
SIPTTPGNPN FPDLRDRARA LMQEFPLIDG HNDMPLVLRQ FYQNGLQDAN LRNFTHGQTS 

       130        140        150        160        170        180 
LDRLKDGLVG AQFWSAYVPC QTQDRDALRL TLEQIDLIRR ICASYSELEL VTSVKALNST 

       190        200        210        220        230        240 
QKLACLIGVE GGHSLDNSLA VLRSFYLLGV RYLTLTHTCN TPWAETSSKG VHAFYSSVTG 

       250        260        270        280        290        300 
LTSFGEKVVA EMNRLGMMVD LSHVSDAAAR RALEVSQAPV IFSHSAARAV CPNARNLPDD 

       310        320        330        340        350        360 
LLQLLKKNGG IVMVTFSVGV LPCNPLANVS TVADHFDHIR SVIGSEFIGI GGDYDGTKQF 

       370        380        390        400        410        420 
PQGLEDVSTY PVLIEELLRR GWNEQELQGI LRGNLLRVFR QVEQVRDKSK WQSPLEDMIP 

       430        440        450        460        470 
EEQLDSACHS ALRPQKQHPE KNQPETPEYH ILKFSHSKSS PHIVPSLAIV ATLLGLIV 

« Hide

Isoform 2 [UniParc].

Checksum: 253DC762000875A4
Show »

FASTA57863,675
Isoform 3 [UniParc].

Checksum: D28E45A1A5169543
Show »

FASTA38542,667

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] (ISOFORM 2), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.
Strain: C57BL/6.
Tissue: Heart, Lung and Spleen.
[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] (ISOFORMS 1 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Dendritic cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF488552 mRNA. Translation: AAP84986.1.
AK089244 mRNA. Translation: BAC40810.1.
AK155417 mRNA. Translation: BAE33255.1.
AK170094 mRNA. Translation: BAE41559.1.
AK170970 mRNA. Translation: BAE42149.1.
AK171044 mRNA. Translation: BAE42209.1.
AK171122 mRNA. Translation: BAE42264.1.
AK171155 mRNA. Translation: BAE42280.1.
AK171196 mRNA. Translation: BAE42306.1.
AK171268 mRNA. Translation: BAE42354.1.
AK171503 mRNA. Translation: BAE42494.1.
AK171606 mRNA. Translation: BAE42559.1.
RefSeqNP_795887.2. NM_176913.3.
XP_006531142.1. XM_006531079.1.
XP_006531143.1. XM_006531080.1.
UniGeneMm.248357.

3D structure databases

ProteinModelPortalQ8C255.
SMRQ8C255. Positions 74-430.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM19.004.

Proteomic databases

PaxDbQ8C255.
PRIDEQ8C255.

Protocols and materials databases

DNASU319446.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034373; ENSMUSP00000034373; ENSMUSG00000053687. [Q8C255-1]
ENSMUST00000081998; ENSMUSP00000080659; ENSMUSG00000053687. [Q8C255-2]
ENSMUST00000117555; ENSMUSP00000113877; ENSMUSG00000053687. [Q8C255-3]
GeneID319446.
KEGGmmu:319446.
UCSCuc009nev.1. mouse. [Q8C255-3]
uc009ney.1. mouse. [Q8C255-2]

Organism-specific databases

CTD64174.
MGIMGI:2442042. Dpep2.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
OMAIEATHRQ.
OrthoDBEOG7SJD4N.
PhylomeDBQ8C255.
TreeFamTF324523.

Gene expression databases

BgeeQ8C255.
CleanExMM_DPEP2.
MM_MBD2.
GenevestigatorQ8C255.

Family and domain databases

InterProIPR028531. Dpep2.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF15. PTHR10443:SF15. 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

NextBio394746.
PROQ8C255.
SOURCESearch...

Entry information

Entry nameDPEP2_MOUSE
AccessionPrimary (citable) accession number: Q8C255
Secondary accession number(s): Q3TAV9 expand/collapse secondary AC list , Q3TBF7, Q3TBK3, Q3TBM9, Q7TQ53
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 84 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