Reviewed, UniProtKB/Swiss-Prot P28843 (DPP4_MOUSE)

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
    Thymocyte-activating molecule
      Short name=THAM
    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:	Cd26

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	760 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.
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.
Subcellular location	Cell membrane; Single-pass type II membrane protein. Dipeptidyl peptidase 4 soluble form: Secreted.
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	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell intercellular canaliculus Inferred from direct assay. Source: MGI
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW 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 – 760	760	Dipeptidyl peptidase 4 membrane form		PRO_0000027215
	Chain	37 – 760	724	Dipeptidyl peptidase 4 soluble form By similarity		PRO_0000027216
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 28	22	Signal-anchor for type II membrane protein Potential
	Topological domain	29 – 760	732	Extracellular Potential
	Compositional bias	295 – 466	172	Cys-rich
Sites
	Active site	624	1	Charge relay system By similarity
	Active site	702	1	Charge relay system By similarity
	Active site	734	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	83	1	N-linked (GlcNAc...) By similarity
	Glycosylation	90	1	N-linked (GlcNAc...) By similarity
	Glycosylation	145	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Glycosylation	223	1	N-linked (GlcNAc...) By similarity
	Glycosylation	315	1	N-linked (GlcNAc...) By similarity
	Glycosylation	328	1	N-linked (GlcNAc...) Potential
	Glycosylation	514	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	679	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	379 ↔ 388		By similarity
	Disulfide bond	438 ↔ 441		By similarity
	Disulfide bond	448 ↔ 466		By similarity
	Disulfide bond	643 ↔ 756		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P28843-1 [UniParc]. Last modified February 1, 1996. Version 3. Checksum: A5F644B46E4A3DF8	FASTA	760	87,437
	10 20 30 40 50 60 MKTPWKVLLG LLGVAALVTI ITVPIVLLSK DEAAADSRRT YSLADYLKST FRVKSYSLWW 70 80 90 100 110 120 VSDFEYLYKQ ENNILLLNAE HGNSSIFLEN STFESFGYHS VSPDRLFVLL EYNYVKQWRH 130 140 150 160 170 180 SYTASYNIYD VNKRQLITEE KIPNNTQWIT WSPEGHKLAY VWKNDIYVKV EPHLPSHRIT 190 200 210 220 230 240 STGEENVIYN GITDWVYEEE VFGAYSALWW SPNNTFLAYA QFNDTGVPLI EYSFYSDESL 250 260 270 280 290 300 QYPKTVWIPY PKAGAVNPTV KFFIVNIDSL SSSSSAAPIQ IPAPASVARG DHYLCDVVWA 310 320 330 340 350 360 TEERISLQWL RRIQNYSVMA ICDYDKINLT WNCPSEQQHV EMSTTGWVGR FRPAEPHFTS 370 380 390 400 410 420 DGSSFYKIIS DKDGYKHICH FPKDKKDCTF ITKGAWEVIS IEALTSDYLY YISNQYKEMP 430 440 450 460 470 480 GGRNLYKIQL TDHTNVKCLS CDLNPERCQY YAVSFSKEAK YYQLGCWGPG LPLYTLHRST 490 500 510 520 530 540 DHKELRVLED NSALDRMLQD VQMPSKKLDF IVLNETRFWY QMILPPHFDK SKKYPLLLDV 550 560 570 580 590 600 YAGPCSQKAD ASFRLNWATY LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTLEVEDQ 610 620 630 640 650 660 IEAARQFVKM GFVDSKRVAI WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV SRWEYYDSVY 670 680 690 700 710 720 TERYMGLPIP EDNLDHYRNS TVMSRAEHFK QVEYLLIHGT ADDNVHFQQS AQISKALVDA 730 740 750 760 GVDFQAMWYT DEDHGIASST AHQHIYSHMS HFLQQCFSLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases." Marguet D.A., Bernard A.-M., Vivier I., Darmoul D., Naquet P., Pierres M. J. Biol. Chem. 267:2200-2208(1992) [PubMed: 1370813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss. Tissue: Thymus.
[2]	Marguet D.A. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Structure of the mouse dipeptidyl peptidase IV (CD26) gene." Bernard A.-M., Mattei M.-G., Pierres M., Marguet D. Biochemistry 33:15204-15214(1994) [PubMed: 7999781] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B10.A. Tissue: Liver.
[4]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Kidney and Thymus.
[5]	"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].
[6]	"Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV)." Vivier I., Marguet D.A., Naquet P., Bonicel J., Black D., Li C.X.-Y., Bernard A.-M., Gorvel J.-P., Pierres M. J. Immunol. 147:447-454(1991) [PubMed: 1712807] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20.
[7]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-514, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58384 mRNA. Translation: CAA41274.1. U12620 , U12599, U12600, U12601, U12602, U12603, U12604, U12605, U12606, U12607, U12608, U12609, U12610, U12611, U12612, U12613, U12614, U12615, U12616, U12617, U12618, U12619 Genomic DNA. Translation: AAA82213.1. AK085370 mRNA. Translation: BAC39434.1. AK153939 mRNA. Translation: BAE32266.1. BC022183 mRNA. Translation: AAH22183.1.
IPI	IPI00125813.
PIR	S23752.
RefSeq	NP_001153015.1. NP_034204.1.
UniGene	Mm.1151
3D structure databases
HSSP	HSSP built from PDB template 1PFQ based on UniProtKB P27487.
SMR	P28843. Positions 37-759.
ModBase	Search...
Protein-protein interaction databases
STRING	P28843.
Protein family/group databases
MEROPS	S09.003.
PTM databases
PhosphoSite	P28843.
Proteomic databases
PRIDE	P28843.
Genome annotation databases
Ensembl	ENSMUST00000047812; ENSMUSP00000044050; ENSMUSG00000035000; Mus musculus. [Genome view]
GeneID	13482.
KEGG	mmu:13482.
UCSC	uc008jvg.1. mouse.
Organism-specific databases
CTD	13482.
MGI	MGI:94919. Dpp4.
Phylogenomic databases
HOGENOM	P28843.
HOVERGEN	P28843.
OMA	YLASTEN.
Enzyme and pathway databases
BRENDA	3.4.14.5. 244.
Gene expression databases
ArrayExpress	P28843.
Bgee	P28843.
CleanEx	MM_DPP4.
Genevestigator	P28843.
GermOnline	ENSMUSG00000035000. Mus musculus.
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
NextBio	283979.
SOURCE	Search...

Entry information

Entry name

DPP4_MOUSE

Accession

Primary (citable) accession number: P28843
Secondary accession number(s): Q3U514

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1996
Last modified:	November 3, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)