Q9NY33 (DPP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

DPP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves Arg-Arg-beta-naphthylamide.
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 By similarity.
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

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Traceable author statement PubMed 10387075. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Traceable author statement PubMed 10387075. Source: ProtInc metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 737

737

Dipeptidyl peptidase 3

PRO_0000078238

Sites

Active site

451

1

By similarity

Metal binding

450

1

Zinc; catalytic By similarity

Metal binding

455

1

Zinc; catalytic By similarity

Natural variations

Alternative sequence

91 – 120

30

Missing in isoform 4.

VSP_044696

Alternative sequence

182 – 601

420

Missing in isoform 2.

VSP_005510

Natural variant

76

1

R → H. Ref.4
Corresponds to variant rs11826683 [ dbSNP | Ensembl ].

VAR_033494

Natural variant

145

1

Q → H. Ref.1
Corresponds to variant rs11550299 [ dbSNP | Ensembl ].

VAR_033495

Natural variant

678

1

R → H. Ref.1 Ref.5
Corresponds to variant rs2305535 [ dbSNP | Ensembl ].

VAR_021850

Natural variant

690

1

E → K.
Corresponds to variant rs12421620 [ dbSNP | Ensembl ].

VAR_051597

Experimental info

Sequence conflict

224

1

P → S in BAG59686. Ref.2

Sequence conflict

417 – 419

3

YAT → TA in BAA75785. Ref.5

Sequence conflict

697

1

I → Y in BAA75785. Ref.5

Secondary structure

1

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737

Helix Strand Turn

Details...

Helix

4 – 6

3

Beta strand

14 – 16

3

Helix

20 – 24

5

Helix

28 – 45

18

Helix

47 – 50

4

Helix

56 – 69

14

Helix

72 – 81

10

Helix

86 – 102

17

Beta strand

104 – 106

3

Turn

108 – 110

3

Helix

120 – 129

10

Helix

131 – 135

5

Helix

137 – 152

16

Helix

156 – 158

3

Beta strand

159 – 161

3

Helix

164 – 166

3

Beta strand

170 – 172

3

Helix

178 – 190

13

Beta strand

198 – 204

7

Beta strand

206 – 208

3

Beta strand

210 – 217

8

Beta strand

222 – 224

3

Helix

231 – 233

3

Beta strand

235 – 239

5

Beta strand

242 – 250

9

Helix

252 – 266

15

Helix

272 – 287

16

Helix

290 – 302

13

Beta strand

307 – 316

10

Beta strand

318 – 320

3

Beta strand

321 – 323

3

Beta strand

327 – 334

8

Helix

337 – 348

12

Helix

350 – 355

6

Beta strand

357 – 359

3

Helix

361 – 363

3

Beta strand

375 – 384

10

Beta strand

388 – 392

5

Helix

396 – 401

6

Beta strand

405 – 409

5

Helix

410 – 413

4

Helix

421 – 423

3

Helix

429 – 452

24

Turn

453 – 456

4

Beta strand

465 – 467

3

Beta strand

469 – 471

3

Turn

473 – 475

3

Turn

479 – 481

3

Beta strand

482 – 484

3

Helix

495 – 498

4

Turn

500 – 502

3

Helix

503 – 518

16

Helix

522 – 528

7

Helix

532 – 552

21

Helix

553 – 556

4

Helix

559 – 561

3

Beta strand

563 – 565

3

Helix

567 – 581

15

Beta strand

586 – 593

8

Beta strand

597 – 605

9

Helix

607 – 609

3

Turn

610 – 613

4

Helix

614 – 630

17

Helix

634 – 644

11

Turn

651 – 653

3

Helix

655 – 664

10

Beta strand

671 – 673

3

Beta strand

676 – 680

5

Beta strand

683 – 687

5

Helix

693 – 701

9

Turn

705 – 707

3

Helix

708 – 722

15

Helix

723 – 725

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: E2BB1923C9CAFDEC	FASTA	737	82,589
	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
	Isoform 2 [UniParc]. Checksum: A172153E757C72E5	FASTA	317	35,489
	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 ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA PPECFLTLRD 250 260 270 280 290 300 TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF SERFPEDGPE LEEILTQLAT 310 ADARFWKGPS EAPSGQA
	Isoform 3 (DPP3-BBS1) [UniParc]. See Q8NFJ9.		–	–
	Isoform 4 [UniParc]. Checksum: 52EAAAFC59AB9AFA	FASTA	707	79,307
	10 20 30 40 50 60 MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL QTSPEAPYIY 70 80 90 100 110 120 ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ EKLERVILGS EAAQQHPEEV RGLWQTCGEL 130 140 150 160 170 180 MFSLEPRLRH LGLGKEGITT YFSGNCTMED AKLAQDFLDS QNLSAYNTRL FKEVDGEGKP 190 200 210 220 230 240 YYEVRLASVL GSEPSLDSEV TSKLKSYEFR GSPFQVTRGD YAPILQKVVE QLEKAKAYAA 250 260 270 280 290 300 NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW IQDKGPIVES YIGFIESYRD PFGSRGEFEG 310 320 330 340 350 360 FVAVVNKAMS AKFERLVASA EQLLKELPWP PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI 370 380 390 400 410 420 NIPNYDDLRQ TEGFKNVSLG NVLAVAYATQ REKLTFLEED DKDLYILWKG PSFDVQVGLH 430 440 450 460 470 480 ELLGHGSGKL FVQDEKGAFN FDQETVINPE TGEQIQSWYR SGETWDSKFS TIASSYEECR 490 500 510 520 530 540 AESVGLYLCL HPQVLEIFGF EGADAEDVIY VNWLNMVRAG LLALEFYTPE AFNWRQAHMQ 550 560 570 580 590 600 ARFVILRVLL EAGEGLVTIT PTTGSDGRPD ARVRLDRSKI RSVGKPALER FLRRLQVLKS 610 620 630 640 650 660 TGDVAGGRAL YEGYATVTDA PPECFLTLRD TVLLRKESRK LIVQPNTRLE GSDVQLLEYE 670 680 690 700 ASAAGLIRSF SERFPEDGPE LEEILTQLAT ADARFWKGPS EAPSGQA

References

	« Hide 'large scale' referencesShow '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. , 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. , 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].
+	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.

IPI

IPI00020672.
IPI00645171.
IPI00979514.

RefSeq

NP_001243599.1. NM_001256670.1.
NP_005691.2. NM_005700.4.
NP_569710.2. NM_130443.3.

UniGene

Hs.502914.
Hs.740670.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FVY	X-ray	1.90	A	1-726	[»]
3T6B	X-ray	2.40	A/B	1-726	[»]
3T6J	X-ray	2.98	A	1-726	[»]

ProteinModelPortal

Q9NY33.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NY33. 4 interactions.

Protein family/group databases

MEROPS

M49.001.

PTM databases

PhosphoSite

Q9NY33.

Polymorphism databases

DMDM

20532389.

Proteomic databases

PeptideAtlas

Q9NY33.

PRIDE

Q9NY33.

Protocols and materials databases

DNASU

10072.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360510; ENSP00000353701; ENSG00000254986.
ENST00000453114; ENSP00000389943; ENSG00000254986.
ENST00000530165; ENSP00000436941; ENSG00000254986.
ENST00000541961; ENSP00000440502; ENSG00000254986.

GeneID

10072.

KEGG

hsa:10072.

UCSC

uc001oif.1. human.

Organism-specific databases

CTD

10072.

GeneCards

GC11P066249.

HGNC

HGNC:3008. DPP3.

HPA

HPA035781.

MIM

606818. gene.

neXtProt

NX_Q9NY33.

PharmGKB

PA27466.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000187784.

HOVERGEN

HBG025680.

InParanoid

Q9NY33.

KO

K01277.

OrthoDB

EOG49W2DT.

Gene expression databases

ArrayExpress

Q9NY33.

Bgee

Q9NY33.

CleanEx

HS_DPP3.

Genevestigator

Q9NY33.

GermOnline

ENSG00000174483. Homo sapiens.

Family and domain databases

InterPro

IPR005317. Dipeptidyl-peptase3.
[Graphical view]

PANTHER

PTHR23422:SF3. PTHR23422:SF3. 1 hit.

PIRSF

PIRSF007828. Dipeptidyl-peptidase_III. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q9NY33.

ChEMBL

CHEMBL4520.

ChiTaRS

DPP3. human.

EvolutionaryTrace

Q9NY33.

GenomeRNAi

10072.

NextBio

38071.

SOURCE

Search...

Entry information

Entry name

DPP3_HUMAN

Accession

Primary (citable) accession number: Q9NY33
Secondary accession number(s): B2RDB5 , B4DLX4, F5H8L6, O95748, Q969H2, Q9BV67, Q9HAL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 10, 2002
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.