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

Q9NY33 (DPP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DPP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves and degrades of the opioid peptide enkephalin. Also cleaves Arg-Arg-beta-naphthylamide. Ref.11

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Ref.11

Enzyme regulation

Inhibited by spinorphin, an opioid peptide derived from hemoglobin. Ref.11

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the peptidase M49 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.8.

Mass spectrometry

Isoform 1: Molecular mass is 82500±60 Da from positions 1 - 737. Determined by MALDI. Ref.6

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KEAP1Q141452EBI-718333,EBI-751001

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NY33-1)

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: Q9NY33-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-601: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Isoform 3 (identifier: Q8NFJ9-2)

Also known as: DPP3-BBS1;

The sequence of this isoform can be found in the external entry Q8NFJ9.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Based on a readthrough transcript which may produce a DPP3-BBS1 fusion protein. No experimental confirmation available.
Isoform 4 (identifier: Q9NY33-4)

The sequence of this isoform differs from the canonical sequence as follows:
     91-120: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 737736Dipeptidyl peptidase 3
PRO_0000078238

Sites

Active site4511 By similarity
Metal binding4501Zinc; catalytic
Metal binding4551Zinc; catalytic
Metal binding5081Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.10

Natural variations

Alternative sequence91 – 12030Missing in isoform 4.
VSP_044696
Alternative sequence182 – 601420Missing in isoform 2.
VSP_005510
Natural variant761R → H. Ref.4
Corresponds to variant rs11826683 [ dbSNP | Ensembl ].
VAR_033494
Natural variant1451Q → H. Ref.1
Corresponds to variant rs11550299 [ dbSNP | Ensembl ].
VAR_033495
Natural variant6781R → H. Ref.1 Ref.5
Corresponds to variant rs2305535 [ dbSNP | Ensembl ].
VAR_021850
Natural variant6901E → K.
Corresponds to variant rs12421620 [ dbSNP | Ensembl ].
VAR_051597

Experimental info

Sequence conflict2241P → S in BAG59686. Ref.2
Sequence conflict417 – 4193YAT → TA in BAA75785. Ref.5
Sequence conflict6971I → Y in BAA75785. Ref.5

Secondary structure

........................................................................................................................................ 737
Helix Strand Turn

Details...

Sequences

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

Last modified May 10, 2002. Version 2.
Checksum: E2BB1923C9CAFDEC

FASTA73782,589
        10         20         30         40         50         60 
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL QTSPEAPYIY 

        70         80         90        100        110        120 
ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK 

       130        140        150        160        170        180 
EKLERVILGS EAAQQHPEEV RGLWQTCGEL MFSLEPRLRH LGLGKEGITT YFSGNCTMED 

       190        200        210        220        230        240 
AKLAQDFLDS QNLSAYNTRL FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR 

       250        260        270        280        290        300 
GSPFQVTRGD YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW 

       310        320        330        340        350        360 
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA EQLLKELPWP 

       370        380        390        400        410        420 
PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYATQ 

       430        440        450        460        470        480 
REKLTFLEED DKDLYILWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDQETVINPE 

       490        500        510        520        530        540 
TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY 

       550        560        570        580        590        600 
VNWLNMVRAG LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD 

       610        620        630        640        650        660 
ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA PPECFLTLRD 

       670        680        690        700        710        720 
TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF SERFPEDGPE LEEILTQLAT 

       730 
ADARFWKGPS EAPSGQA 

« Hide

Isoform 2 [UniParc].

Checksum: A172153E757C72E5
Show »

FASTA31735,489
Isoform 3 (DPP3-BBS1) [UniParc].

See Q8NFJ9.

Isoform 4 [UniParc].

Checksum: 52EAAAFC59AB9AFA
Show »

FASTA70779,307

References

« Hide 'large scale' references
[1]"Cloning and sequencing of human dipeptidyl-peptidase III."
Chen J.M., Fortunato M., Barrett A.J.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS HIS-145 AND HIS-678.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Tissue: Brain and Embryo.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1), VARIANT HIS-76.
Tissue: Colon, Kidney and Placenta.
[5]"Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression."
Fukasawa K., Fukusawa K.M., Kanai M., Fujii S., Hirose J., Harada M.
Biochem. J. 329:275-282(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-723 (ISOFORM 1), CHARACTERIZATION, VARIANT HIS-678.
[6]"Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences."
Abramic M., Schleuder D., Dolovcak L., Schroeder W., Strupat K., Sagi D., Peter-Katalini J., Vitale L.
Biol. Chem. 381:1233-1243(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
Tissue: Erythrocyte.
[7]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III."
Bezerra G.A., Dobrovetsky E., Viertlmayr R., Dong A., Binter A., Abramic M., Macheroux P., Dhe-Paganon S., Gruber K.
Proc. Natl. Acad. Sci. U.S.A. 109:6525-6530(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-726 IN COMPLEX WITH OPIOID PEPTIDE, FUNCTION, ENZYME REGULATION, COFACTOR, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271216 mRNA. Translation: CAB72433.1.
AK021449 mRNA. Translation: BAB13828.1.
AK297199 mRNA. Translation: BAG59686.1.
AK315478 mRNA. Translation: BAG37862.1.
AP002748 Genomic DNA. No translation available.
BC001446 mRNA. Translation: AAH01446.1.
BC007221 mRNA. Translation: AAH07221.1.
BC014038 mRNA. Translation: AAH14038.1.
BC024271 mRNA. Translation: AAH24271.1.
AB017970 mRNA. Translation: BAA75785.1.
RefSeqNP_001243599.1. NM_001256670.1.
NP_005691.2. NM_005700.4.
NP_569710.2. NM_130443.3.
UniGeneHs.502914.
Hs.740670.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FVYX-ray1.90A1-726[»]
3T6BX-ray2.40A/B1-726[»]
3T6JX-ray2.98A1-726[»]
ProteinModelPortalQ9NY33.
SMRQ9NY33. Positions 3-726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115383. 20 interactions.
DIPDIP-53793N.
IntActQ9NY33. 4 interactions.

Chemistry

BindingDBQ9NY33.
ChEMBLCHEMBL4520.

Protein family/group databases

MEROPSM49.001.

PTM databases

PhosphoSiteQ9NY33.

Polymorphism databases

DMDM20532389.

Proteomic databases

PeptideAtlasQ9NY33.
PRIDEQ9NY33.

Protocols and materials databases

DNASU10072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360510; ENSP00000353701; ENSG00000254986. [Q9NY33-1]
ENST00000453114; ENSP00000389943; ENSG00000254986. [Q9NY33-1]
ENST00000530165; ENSP00000436941; ENSG00000254986. [Q9NY33-4]
ENST00000541961; ENSP00000440502; ENSG00000254986. [Q9NY33-1]
GeneID10072.
KEGGhsa:10072.
UCSCuc001oif.2. human. [Q9NY33-1]

Organism-specific databases

CTD10072.
GeneCardsGC11P066249.
HGNCHGNC:3008. DPP3.
HPAHPA035780.
HPA035781.
MIM606818. gene.
neXtProtNX_Q9NY33.
PharmGKBPA27466.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000187784.
HOVERGENHBG025680.
InParanoidQ9NY33.
KOK01277.
PhylomeDBQ9NY33.
TreeFamTF300598.

Gene expression databases

ArrayExpressQ9NY33.
BgeeQ9NY33.
CleanExHS_DPP3.
GenevestigatorQ9NY33.

Family and domain databases

InterProIPR005317. Dipeptidyl-peptase3.
[Graphical view]
PANTHERPTHR23422:SF3. PTHR23422:SF3. 1 hit.
PIRSFPIRSF007828. Dipeptidyl-peptidase_III. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDPP3. human.
EvolutionaryTraceQ9NY33.
GeneWikiDPP3.
GenomeRNAi10072.
NextBio38071.
PROQ9NY33.
SOURCESearch...

Entry information

Entry nameDPP3_HUMAN
AccessionPrimary (citable) accession number: Q9NY33
Secondary accession number(s): B2RDB5 expand/collapse secondary AC list , B4DLX4, F5H8L6, O95748, Q969H2, Q9BV67, Q9HAL6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 10, 2002
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM