Q9UHL4 (DPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dipeptidyl peptidase 2
EC=3.4.14.2

Alternative name(s):
Dipeptidyl aminopeptidase II
Dipeptidyl peptidase 7
Dipeptidyl peptidase II
Short name=DPP II
Quiescent cell proline dipeptidase

Gene names

Name:	DPP7
Synonyms:	DPP2, QPP

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	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in the degradation of some oligopeptides. Ref.8
Catalytic activity	Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides. Ref.8
Subunit structure	Homodimer. Ref.8
Subcellular location	Lysosome. Cytoplasmic vesicle. Secreted Ref.8.
Tissue specificity	Detected in seminal plasma (at protein level). Ref.8
Post-translational modification	N-glycosylated. Ref.8
Sequence similarities	Belongs to the peptidase S28 family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Lysosome Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: Compara serine-type peptidase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 25

4

Potential

PRO_0000027314

Chain

26 – 492

467

Dipeptidyl peptidase 2

PRO_0000027315

Sites

Active site

162

1

Charge relay system Potential

Active site

418

1

Charge relay system Potential

Active site

443

1

Charge relay system Potential

Amino acid modifications

Glycosylation

50

1

N-linked (GlcNAc...) Ref.6

Glycosylation

86

1

N-linked (GlcNAc...) Potential

Glycosylation

315

1

N-linked (GlcNAc...) Ref.6

Glycosylation

356

1

N-linked (GlcNAc...) Potential

Glycosylation

363

1

N-linked (GlcNAc...) Potential

Glycosylation

428

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

89

1

A → G. Ref.1 Ref.4
Corresponds to variant rs10747049 [ dbSNP | Ensembl ].

VAR_047087

Experimental info

Sequence conflict

71

1

I → T in AAF12747. Ref.1

Secondary structure

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492

Helix Strand Turn

Details...

Beta strand

32 – 40

9

Turn

47 – 50

4

Beta strand

52 – 60

9

Turn

66 – 68

3

Beta strand

71 – 75

5

Helix

81 – 87

7

Helix

89 – 98

10

Beta strand

101 – 105

5

Helix

117 – 121

5

Helix

131 – 148

18

Beta strand

156 – 161

6

Helix

163 – 174

12

Turn

176 – 178

3

Beta strand

180 – 185

6

Helix

191 – 193

3

Helix

200 – 210

11

Helix

214 – 233

20

Helix

236 – 243

8

Beta strand

245 – 247

3

Helix

252 – 271

20

Beta strand

278 – 284

7

Helix

288 – 297

10

Helix

302 – 314

13

Beta strand

316 – 318

3

Beta strand

321 – 323

3

Helix

325 – 328

4

Helix

342 – 351

10

Turn

352 – 354

3

Beta strand

363 – 368

6

Helix

375 – 386

12

Helix

394 – 399

6

Beta strand

409 – 415

7

Helix

421 – 423

3

Beta strand

430 – 438

9

Helix

445 – 447

3

Helix

456 – 476

21

Sequences

	Sequence		Length	Mass (Da)
	Q9UHL4 [UniParc]. Last modified November 4, 2008. Version 3. Checksum: 6C3EDECA90FA7583	FASTA	492	54,341
	10 20 30 40 50 60 MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN KTFPQRFLVS 70 80 90 100 110 120 DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA LLVFAEHRYY GKSLPFGAQS 130 140 150 160 170 180 TQRGHTELLT VEQALADFAE LLRALRRDLG AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA 190 200 210 220 230 240 GALAASAPVL AVAGLGDSNQ FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR 250 260 270 280 290 300 WEFGTCQPLS DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA 310 320 330 340 350 360 QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ ACTEINLTFA 370 380 390 400 410 420 SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW GGDLRAASNI IFSNGNLDPW 430 440 450 460 470 480 AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS HPEDPASVVE ARKLEATIIG EWVKAARREQ 490 QPALRGGPRL SL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase." Underwood R., Chiravuri M., Lee H., Schmitz T., Kabcenell A.K., Yardley Y., Huber B.T. J. Biol. Chem. 274:34053-34058(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-89.
[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]. Tissue: Synovial cell.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [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], VARIANT GLY-89. Tissue: Brain.
[5]	"Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase." Chiravuri M., Agarraberes F., Mathieu S.L., Lee H., Huber B.T. J. Immunol. 165:5695-5702(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-315, MASS SPECTROMETRY. Tissue: Liver.
[7]	"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].
[8]	"Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)." Maes M.B., Lambeir A.M., Gilany K., Senten K., Van der Veken P., Leiting B., Augustyns K., Scharpe S., De Meester I. Biochem. J. 386:315-324(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 28-492, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF154502 mRNA. Translation: AAF12747.1.
AK292112 mRNA. Translation: BAF84801.1.
AL929554 Genomic DNA. Translation: CAH72872.1.
BC011907 mRNA. Translation: AAH11907.1.
BC016961 mRNA. Translation: AAH16961.1.

IPI

IPI00296141.

PIR

S77568.

RefSeq

NP_037511.2. NM_013379.2.

UniGene

Hs.37916.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JYH	X-ray	2.19	A/B/C/D	28-492	[»]
3N0T	X-ray	2.45	A/B/C/D	28-492	[»]
4EBB	X-ray	2.00	A/B	27-492	[»]

ProteinModelPortal

Q9UHL4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHL4. 7 interactions.

STRING

9606.ENSP00000360635.

Protein family/group databases

MEROPS

S28.002.

PTM databases

PhosphoSite

Q9UHL4.

Polymorphism databases

DMDM

212276510.

Proteomic databases

PaxDb

Q9UHL4.

PRIDE

Q9UHL4.

Protocols and materials databases

DNASU

29952.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371579; ENSP00000360635; ENSG00000176978.

GeneID

29952.

KEGG

hsa:29952.

UCSC

uc004clh.3. human.

Organism-specific databases

CTD

29952.

GeneCards

GC09M140004.

H-InvDB

HIX0017204.
HIX0025819.

HGNC

HGNC:14892. DPP7.

HPA

CAB025541.
HPA021282.

MIM

610537. gene.

neXtProt

NX_Q9UHL4.

PharmGKB

PA27469.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290141.

HOGENOM

HOG000238311.

HOVERGEN

HBG005526.

InParanoid

Q9UHL4.

KO

K01276.

OMA

EWVKAAR.

OrthoDB

EOG4CJVH0.

PhylomeDB

Q9UHL4.

Gene expression databases

Bgee

Q9UHL4.

CleanEx

HS_DPP7.

Genevestigator

Q9UHL4.

GermOnline

ENSG00000176978. Homo sapiens.

Family and domain databases

InterPro

IPR008758. Peptidase_S28.
[Graphical view]

PANTHER

PTHR11010. PTHR11010. 1 hit.

Pfam

PF05577. Peptidase_S28. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9UHL4.

ChEMBL

CHEMBL3976.

EvolutionaryTrace

Q9UHL4.

GenomeRNAi

29952.

NextBio

52649.

SOURCE

Search...

Entry information

Entry name

DPP2_HUMAN

Accession

Primary (citable) accession number: Q9UHL4
Secondary accession number(s): A8K7U7, Q5VSF1, Q969X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 4, 2008
Last modified:	May 1, 2013
This is version 114 of the entry and version 3 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.