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Protein

Dipeptidyl peptidase 3

Gene

Dpp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves and degrades of the opioid peptide enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (By similarity).By similarity

Catalytic activityi

Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by spinorphin, an opioid peptide derived from hemoglobin.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi450 – 4501Zinc; catalyticBy similarity
Active sitei451 – 4511By similarity
Metal bindingi455 – 4551Zinc; catalyticBy similarity
Metal bindingi508 – 5081Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM49.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 3 (EC:3.4.14.4)
Alternative name(s):
Dipeptidyl aminopeptidase III
Dipeptidyl arylamidase III
Dipeptidyl peptidase III
Short name:
DPP III
Enkephalinase B
Gene namesi
Name:Dpp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1922471. Dpp3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 738737Dipeptidyl peptidase 3PRO_0000078239Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99KK7.
MaxQBiQ99KK7.
PaxDbiQ99KK7.
PRIDEiQ99KK7.

PTM databases

iPTMnetiQ99KK7.
PhosphoSiteiQ99KK7.

Expressioni

Gene expression databases

BgeeiQ99KK7.
CleanExiMM_DPP3.
GenevisibleiQ99KK7. MM.

Interactioni

Protein-protein interaction databases

IntActiQ99KK7. 2 interactions.
MINTiMINT-1869648.
STRINGi10090.ENSMUSP00000025851.

Structurei

3D structure databases

ProteinModelPortaliQ99KK7.
SMRiQ99KK7. Positions 3-726.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M49 family.Curated

Phylogenomic databases

eggNOGiKOG3675. Eukaryota.
ENOG410XRK4. LUCA.
GeneTreeiENSGT00390000007335.
HOGENOMiHOG000187784.
HOVERGENiHBG025680.
InParanoidiQ99KK7.
KOiK01277.
OMAiSETWDSK.
OrthoDBiEOG7WMCHW.
TreeFamiTF300598.

Family and domain databases

InterProiIPR005317. Dipeptidyl-peptase3.
[Graphical view]
PIRSFiPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99KK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAHHLSRA AWYGGLAVLL
60 70 80 90 100
QTSPEAPYIY ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY
110 120 130 140 150
SNMGNYKSFG DTKFVPNLPK DKLGRVILGS KAAQQRPEEV RDLWQTCGDL
160 170 180 190 200
MFSLEPRLRH LGLGKEGVTT YFSGDCTMED AKLAQDFLDS QNLSAYNTRL
210 220 230 240 250
FKVVGQEGKS HYEVRLASVL NTDPALDSEL TSKLKRYEFQ GNHFQVTRGD
260 270 280 290 300
YAPILQKVVE HLEKAKAYAA NSHQEQMLAQ YVESFTQGSI EAHKRGSRFW
310 320 330 340 350
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAMVNKAMS AKFERLVASA
360 370 380 390 400
EQLLKELPWP LAFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ
410 420 430 440 450
TEGFKNVSLG NVLAVAYAAK REKLTFLEEE DKDLYIRWKG PSFDVQVGLH
460 470 480 490 500
ELLGHGSGKL FVQDEKGAFN FDKETVINPE TGEQIQSWYR SGETWDSKFS
510 520 530 540 550
TIASSYEECR AESVGLYLCL NPQVLEIFGF EGADAEDVIY VNWLNMVRAG
560 570 580 590 600
LLALEFYTPE AANWRQAHMQ ARFVILRVLL EAGEGLVTVT PTTGSDGRPD
610 620 630 640 650
ARVRLDRSKI RSVGRPALER FLRRLQVLKS TGDVVAGRAL YEGYAAVTDA
660 670 680 690 700
PPECFLTLRD TVLLRKESRK LIVQPNTRLE GSEVQLVEYE ASAAGLIRSF
710 720 730
CERFPEDGPE LEEVLIQLAA ADARFWRNQA QEAPPGQA
Length:738
Mass (Da):82,898
Last modified:July 27, 2011 - v2
Checksum:iE2B6BD91AE9C81EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481A → V in AAH04600 (PubMed:15489334).Curated
Sequence conflicti361 – 3611L → P in AAH04600 (PubMed:15489334).Curated
Sequence conflicti728 – 7281N → D in AAH04600 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031020 mRNA. Translation: BAC27216.1.
AK166842 mRNA. Translation: BAE39063.1.
BC004600 mRNA. Translation: AAH04600.1.
CCDSiCCDS29443.1.
RefSeqiNP_598564.2. NM_133803.2.
XP_006531917.1. XM_006531854.2.
UniGeneiMm.234769.

Genome annotation databases

EnsembliENSMUST00000025851; ENSMUSP00000025851; ENSMUSG00000063904.
GeneIDi75221.
KEGGimmu:75221.
UCSCiuc008gbo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031020 mRNA. Translation: BAC27216.1.
AK166842 mRNA. Translation: BAE39063.1.
BC004600 mRNA. Translation: AAH04600.1.
CCDSiCCDS29443.1.
RefSeqiNP_598564.2. NM_133803.2.
XP_006531917.1. XM_006531854.2.
UniGeneiMm.234769.

3D structure databases

ProteinModelPortaliQ99KK7.
SMRiQ99KK7. Positions 3-726.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99KK7. 2 interactions.
MINTiMINT-1869648.
STRINGi10090.ENSMUSP00000025851.

Protein family/group databases

MEROPSiM49.001.

PTM databases

iPTMnetiQ99KK7.
PhosphoSiteiQ99KK7.

Proteomic databases

EPDiQ99KK7.
MaxQBiQ99KK7.
PaxDbiQ99KK7.
PRIDEiQ99KK7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025851; ENSMUSP00000025851; ENSMUSG00000063904.
GeneIDi75221.
KEGGimmu:75221.
UCSCiuc008gbo.2. mouse.

Organism-specific databases

CTDi10072.
MGIiMGI:1922471. Dpp3.

Phylogenomic databases

eggNOGiKOG3675. Eukaryota.
ENOG410XRK4. LUCA.
GeneTreeiENSGT00390000007335.
HOGENOMiHOG000187784.
HOVERGENiHBG025680.
InParanoidiQ99KK7.
KOiK01277.
OMAiSETWDSK.
OrthoDBiEOG7WMCHW.
TreeFamiTF300598.

Miscellaneous databases

ChiTaRSiDpp3. mouse.
NextBioi342490.
PROiQ99KK7.
SOURCEiSearch...

Gene expression databases

BgeeiQ99KK7.
CleanExiMM_DPP3.
GenevisibleiQ99KK7. MM.

Family and domain databases

InterProiIPR005317. Dipeptidyl-peptase3.
[Graphical view]
PIRSFiPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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: Thymus.
  2. "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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDPP3_MOUSE
AccessioniPrimary (citable) accession number: Q99KK7
Secondary accession number(s): Q8C0I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.