Reviewed, UniProtKB/Swiss-Prot P27487 (DPP4_HUMAN)

Names and origin

Protein names

Recommended name:
    Dipeptidyl peptidase 4
    EC=3.4.14.5
Alternative name(s):
    Dipeptidyl peptidase IV
      Short name=DPP IV
    T-cell activation antigen CD26
    TP103
    Adenosine deaminase complexing protein 2
    ADABP
    CD_antigen=CD26
Cleaved into the following 2 chains:
    1- Recommended name:
            Dipeptidyl peptidase 4 membrane form
        Alternative name(s):
            Dipeptidyl peptidase IV membrane form
    2- Recommended name:
            Dipeptidyl peptidase 4 soluble form
        Alternative name(s):
            Dipeptidyl peptidase IV soluble form

Gene names

Name:	DPP4
Synonyms:	ADCP2, CD26

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	766 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	Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation.
Catalytic activity	Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Subunit structure	Homodimer or heterodimer with Seprase (FAP). Ref.13 Ref.14 Ref.15 Ref.16
Subcellular location	Dipeptidyl peptidase 4 soluble form: Secreted. Cell membrane; Single-pass type II membrane protein.
Tissue specificity	Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon. Ref.9
Post-translational modification	The soluble form (SDPP) derives from the membrane form (MDPP) by proteolytic processing.
Sequence similarities	Belongs to the peptidase S9B family. DPPIV subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Domain	Signal-anchor Transmembrane
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	T cell activation Inferred from direct assay. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro regulation of cell-cell adhesion mediated by integrin Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 766

766

Dipeptidyl peptidase 4 membrane form

PRO_0000027213

Chain

39 – 766

728

Dipeptidyl peptidase 4 soluble form

PRO_0000027214

Regions

Topological domain

1 – 6

6

Cytoplasmic Potential

Transmembrane

7 – 28

22

Signal-anchor for type II membrane protein Potential

Topological domain

29 – 766

738

Extracellular Potential

Sites

Active site

630

1

Charge relay system By similarity

Active site

708

1

Charge relay system By similarity

Active site

740

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

85

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16

Glycosylation

92

1

N-linked (GlcNAc...)

Glycosylation

150

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

219

1

N-linked (GlcNAc...) Ref.14 Ref.15

Glycosylation

229

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16

Glycosylation

281

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16

Glycosylation

321

1

N-linked (GlcNAc...) Ref.14 Ref.15

Glycosylation

520

1

N-linked (GlcNAc...) Ref.15 Ref.11

Glycosylation

685

1

N-linked (GlcNAc...) Ref.11

Disulfide bond

328 ↔ 339

Ref.14 Ref.15 Ref.16

Disulfide bond

385 ↔ 394

Ref.14 Ref.15 Ref.16

Disulfide bond

444 ↔ 447

Ref.14 Ref.15 Ref.16

Disulfide bond

454 ↔ 472

Ref.14 Ref.15 Ref.16

Disulfide bond

649 ↔ 762

Ref.14 Ref.15 Ref.16

Experimental info

Sequence conflict

6

1

K → R in AAA52308. Ref.2

Sequence conflict

7

1

V → I in CAA43118. Ref.1

Sequence conflict

437

1

S → I in CAA43118. Ref.1

Sequence conflict

557

1

T → I in AAA52308. Ref.2

Sequence conflict

663

1

D → E in AAA52308. Ref.2

Secondary structure

1

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766

Helix Strand Turn

Details...

Helix

45 – 50

6

Beta strand

64 – 72

9

Beta strand

75 – 80

6

Turn

81 – 83

3

Beta strand

86 – 90

5

Turn

92 – 95

4

Helix

96 – 98

3

Beta strand

102 – 107

6

Beta strand

111 – 122

12

Beta strand

124 – 126

3

Beta strand

128 – 136

9

Turn

137 – 140

4

Beta strand

154 – 157

4

Beta strand

159 – 162

4

Beta strand

164 – 168

5

Beta strand

171 – 177

7

Turn

191 – 193

3

Beta strand

194 – 198

5

Helix

201 – 205

5

Beta strand

208 – 212

5

Beta strand

214 – 216

3

Beta strand

220 – 229

10

Beta strand

235 – 240

6

Beta strand

250 – 255

6

Beta strand

265 – 272

8

Beta strand

278 – 280

3

Beta strand

284 – 287

4

Helix

291 – 294

4

Beta strand

298 – 307

10

Beta strand

310 – 319

10

Beta strand

322 – 330

9

Turn

332 – 334

3

Beta strand

337 – 339

3

Turn

341 – 343

3

Beta strand

345 – 348

4

Beta strand

350 – 352

3

Beta strand

354 – 358

5

Beta strand

368 – 376

9

Beta strand

382 – 388

7

Beta strand

391 – 393

3

Beta strand

395 – 397

3

Beta strand

400 – 402

3

Beta strand

404 – 410

7

Beta strand

412 – 420

9

Helix

422 – 424

3

Beta strand

429 – 435

7

Beta strand

442 – 446

5

Turn

451 – 453

3

Beta strand

456 – 461

6

Helix

463 – 465

3

Beta strand

466 – 472

7

Beta strand

475 – 477

3

Beta strand

479 – 484

6

Turn

485 – 488

4

Beta strand

489 – 495

7

Helix

498 – 505

8

Beta strand

511 – 530

20

Beta strand

540 – 546

7

Helix

563 – 569

7

Beta strand

574 – 578

5

Beta strand

584 – 586

3

Helix

588 – 591

4

Helix

592 – 594

3

Helix

601 – 615

15

Beta strand

619 – 629

11

Helix

631 – 640

10

Turn

641 – 643

3

Beta strand

648 – 654

7

Helix

659 – 661

3

Helix

664 – 671

8

Turn

676 – 679

4

Helix

680 – 685

6

Helix

689 – 697

9

Beta strand

698 – 705

8

Beta strand

709 – 711

3

Helix

713 – 725

13

Beta strand

731 – 735

5

Helix

745 – 762

18

Sequences

	Sequence		Length	Mass (Da)
	P27487-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 5FB4A2C6662D6117	FASTA	766	88,279
	10 20 30 40 50 60 MKTPWKVLLG LLGAAALVTI ITVPVVLLNK GTDDATADSR KTYTLTDYLK NTYRLKLYSL 70 80 90 100 110 120 RWISDHEYLY KQENNILVFN AEYGNSSVFL ENSTFDEFGH SINDYSISPD GQFILLEYNY 130 140 150 160 170 180 VKQWRHSYTA SYDIYDLNKR QLITEERIPN NTQWVTWSPV GHKLAYVWNN DIYVKIEPNL 190 200 210 220 230 240 PSYRITWTGK EDIIYNGITD WVYEEEVFSA YSALWWSPNG TFLAYAQFND TEVPLIEYSF 250 260 270 280 290 300 YSDESLQYPK TVRVPYPKAG AVNPTVKFFV VNTDSLSSVT NATSIQITAP ASMLIGDHYL 310 320 330 340 350 360 CDVTWATQER ISLQWLRRIQ NYSVMDICDY DESSGRWNCL VARQHIEMST TGWVGRFRPS 370 380 390 400 410 420 EPHFTLDGNS FYKIISNEEG YRHICYFQID KKDCTFITKG TWEVIGIEAL TSDYLYYISN 430 440 450 460 470 480 EYKGMPGGRN LYKIQLSDYT KVTCLSCELN PERCQYYSVS FSKEAKYYQL RCSGPGLPLY 490 500 510 520 530 540 TLHSSVNDKG LRVLEDNSAL DKMLQNVQMP SKKLDFIILN ETKFWYQMIL PPHFDKSKKY 550 560 570 580 590 600 PLLLDVYAGP CSQKADTVFR LNWATYLAST ENIIVASFDG RGSGYQGDKI MHAINRRLGT 610 620 630 640 650 660 FEVEDQIEAA RQFSKMGFVD NKRIAIWGWS YGGYVTSMVL GSGSGVFKCG IAVAPVSRWE 670 680 690 700 710 720 YYDSVYTERY MGLPTPEDNL DHYRNSTVMS RAENFKQVEY LLIHGTADDN VHFQQSAQIS 730 740 750 760 KALVDVGVDF QAMWYTDEDH GIASSTAHQH IYTHMSHFIK QCFSLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface." Misumi Y., Hayashi Y., Arakawa F., Ikehara Y. Biochim. Biophys. Acta 1131:333-336(1992) [PubMed: 1352704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Dipeptidyl peptidase IV (CD 26) gene expression in enterocyte-like colon cancer cell lines HT-29 and Caco-2. Cloning of the complete human coding sequence and changes of dipeptidyl peptidase IV mRNA levels during cell differentiation." Darmoul D., Lacasa M., Baricault L., Marguet D., Sapin C., Trotot P., Barbat A. J. Biol. Chem. 267:4824-4833(1992) [PubMed: 1347043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Colon.
[3]	"Cloning and functional expression of the T cell activation antigen CD26." Tanaka T., Camerini D., Seed B., Torimoto Y., Dang N.H., Kameoka J., Dahlberg H.N., Schlossman S.F., Morimoto C. J. Immunol. 149:481-486(1992) [PubMed: 1352530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Peripheral blood.
[4]	Erratum Tanaka T. J. Immunol. 150:2090-2090(1993) [PubMed: 8094732] [Abstract]
[5]	"Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene." Abbott C.A., Baker E., Sutherland G.R., McCaughan G.W. Immunogenetics 40:331-338(1994) [PubMed: 7927537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate and Uterus.
[7]	"Isolation of a cDNA probe for the human intestinal dipeptidylpeptidase IV and assignment of the gene locus DPP4 to chromosome 2." Darmoul D., Lacasa M., Chantret I., Swallow D., Trugnan G. Ann. Hum. Genet. 54:191-197(1990) [PubMed: 1977364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 545-766. Tissue: Colon.
[8]	"Human dipeptidyl peptidase IV gene promoter: tissue-specific regulation from a TATA-less GC-rich sequence characteristic of a housekeeping gene promoter." Boehm S.K., Gum J.R. Jr., Erickson R.H., Hicks J.W., Kim Y.S. Biochem. J. 311:835-843(1995) [PubMed: 7487939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
[9]	"Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon." Gorvel J.P., Ferrero A., Chambraud L., Rigal A., Bonicel J., Maroux S. Gastroenterology 101:618-625(1991) [PubMed: 1677636] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-22, TISSUE SPECIFICITY.
[10]	"A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase." Morrison M.E., Vijayasaradhi S., Engelstein D., Albino A.P., Houghton A.N. J. Exp. Med. 177:1135-1143(1993) [PubMed: 8096237] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Kidney.
[11]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-520 AND ASN-685, MASS SPECTROMETRY. Tissue: Plasma.
[12]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-92; ASN-150; ASN-520 AND ASN-685, MASS SPECTROMETRY. Tissue: Liver.
[13]	"High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine." Oefner C., D'Arcy A., Mac Sweeney A., Pierau S., Gardiner R., Dale G.E. Acta Crystallogr. D 59:1206-1212(2003) [PubMed: 12832764] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-766 IN COMPLEX WITH INHIBITOR, HOMODIMERIZATION.
[14]	"The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold." Hiramatsu H., Kyono K., Higashiyama Y., Fukushima C., Shima H., Sugiyama S., Inaka K., Yamamoto A., Shimizu R. Biochem. Biophys. Res. Commun. 302:849-854(2003) [PubMed: 12646248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-771, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-219; ASN-229; ASN-281 AND ASN-321, DISULFIDE BONDS.
[15]	"Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog." Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N. Nat. Struct. Biol. 10:19-25(2003) [PubMed: 12483204] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-219; ASN-229; ASN-281; ASN-321 AND ASN-520, DISULFIDE BONDS.
[16]	"Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV." Thoma R., Loeffler B., Stihle M., Huber W., Ruf A., Hennig M. Structure 11:947-959(2003) [PubMed: 12906826] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-766, HOMODIMERIZATION, GLYCOSYLATION AT ASN-85; ASN-150; ASN-229 AND ASN-281, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Wikipedia

Dipeptidyl peptidase-4 entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

X60708 mRNA. Translation: CAA43118.1.
M80536 mRNA. Translation: AAA52308.1.
M74777 mRNA. Translation: AAA51943.1.
U13735 , U13710, U13711, U13712, U13713, U13714, U13715, U13716, U13717, U13718, U13719, U13720, U13721, U13722, U13723, U13724, U13725, U13726, U13727, U13728, U13729, U13730, U13731, U13732, U13733, U13734 Genomic DNA. Translation: AAB60646.1.
BC013329 mRNA. Translation: AAH13329.2.
BC065265 mRNA. Translation: AAH65265.1.
S79876 Genomic DNA. Translation: AAB35614.1.

IPI

IPI00018953.

PIR

CDHU26. S24313.

RefSeq

NP_001926.2.

UniGene

Hs.368912

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2E	X-ray	2.60	A/B	33-766	[»]
1N1M	X-ray	2.50	A/B	39-766	[»]
1NU6	X-ray	2.10	A/B	39-766	[»]
1NU8	X-ray	2.50	A/B	39-766	[»]
1PFQ	X-ray	1.90	A/B	36-766	[»]
1R9M	X-ray	2.10	A/B/C/D	39-766	[»]
1R9N	X-ray	2.30	A/B/C/D	39-766	[»]
1RWQ	X-ray	2.20	A/B	39-766	[»]
1TK3	X-ray	2.00	A/B	39-766	[»]
1TKR	X-ray	2.70	A/B	39-766	[»]
1U8E	X-ray	2.20	A/B	39-766	[»]
1W1I	X-ray	3.03	A/B/C/D	39-766	[»]
1WCY	X-ray	2.20	A/B	33-766	[»]
1X70	X-ray	2.10	A/B	40-766	[»]
2AJL	X-ray	2.50	I/J	39-766	[»]
2BGN	X-ray	3.15	A/B/C/D	39-766	[»]
2BGR	X-ray	2.00	A/B	29-766	[»]
2BUB	X-ray	2.66	A/B	39-766	[»]
2FJP	X-ray	2.40	A/B	40-766	[»]
2G5P	X-ray	2.40	A/B	39-764	[»]
2G5T	X-ray	2.30	A/B	39-764	[»]
2G63	X-ray	2.00	A/B/C/D	39-764	[»]
2HHA	X-ray	2.35	A/B	39-766	[»]
2I03	X-ray	2.40	A/B/C/D	39-764	[»]
2I78	X-ray	2.50	A/B/C/D	39-764	[»]
2IIT	X-ray	2.35	A/B	40-766	[»]
2IIV	X-ray	2.15	A/B	40-766	[»]
2JID	X-ray	2.80	A/B	31-766	[»]
2OAG	X-ray	2.30	A/B/C/D	39-764	[»]
2OGZ	X-ray	2.10	A/B	39-766	[»]
2OLE	X-ray	2.40	A/B	39-766	[»]
2ONC	X-ray	2.55	A/B/C/D	41-766	[»]
2OPH	X-ray	2.40	A/B	40-766	[»]
2OQI	X-ray	2.80	A/B/C/D	39-766	[»]
2OQV	X-ray	2.80	A/B	39-764	[»]
2P8S	X-ray	2.20	A/B	40-766	[»]
2QJR	X-ray	2.20	A/B	31-766	[»]
2QKY	X-ray	3.10	A/B/C/D	40-766	[»]
2QOE	X-ray	2.30	A/B	40-766	[»]
2QT9	X-ray	2.10	A/B	1-766	[»]
2QTB	X-ray	2.25	A/B	1-766	[»]
2RGU	X-ray	2.60	A/B	39-766	[»]
2RIP	X-ray	2.90	A	38-766	[»]
3BJM	X-ray	2.35	A/B	39-766	[»]
3C43	X-ray	2.30	A/B	40-766	[»]
3C45	X-ray	2.05	A/B	40-766	[»]
3CCB	X-ray	2.49	A/B/C/D	39-766	[»]
3CCC	X-ray	2.71	A/B/C/D	39-766	[»]
3D4L	X-ray	2.00	A/B	40-766	[»]
3EIO	X-ray	2.00	A/B	39-766	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:351N.

Protein family/group databases

MEROPS

S09.003.

PTM databases

PhosphoSite

P27487.

Proteomic databases

PeptideAtlas

P27487.

PRIDE

P27487.

Genome annotation databases

Ensembl

ENSG00000197635. Homo sapiens. [Contig view]

GeneID

1803.

KEGG

hsa:1803.

UCSC

uc002ubz.1. human.

Organism-specific databases

GeneCards

GC02M162557.

H-InvDB

HIX0002546.

HGNC

HGNC:3009. DPP4.

MIM

102720. gene.

PharmGKB

PA27467.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P27487.

HOVERGEN

P27487.

OMA

P27487. YLASTEN.

Enzyme and pathway databases

BRENDA

3.4.14.5. 247.

Gene expression databases

ArrayExpress

P27487.

Bgee

P27487.

CleanEx

HS_DPP4.

GermOnline

ENSG00000197635. Homo sapiens.

Family and domain databases

InterPro

IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]

Pfam

PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]

PROSITE

PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01261. Sitagliptin.

NextBio

7345.

SOURCE

Search...

Entry information

Entry name

DPP4_HUMAN

Accession

Primary (citable) accession number: P27487

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1996
Last modified:	July 7, 2009
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)