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UniProtKB/Swiss-Prot entry P28843


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DPP4_MOUSE
Primary accession number P28843
Secondary accession number Q3U514
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on February 1, 1996 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 83)
Name and origin of the protein
Protein name Dipeptidyl peptidase 4
Synonyms EC 3.4.14.5
Dipeptidyl peptidase IV
DPP IV
T-cell activation antigen CD26
Thymocyte-activating molecule
THAM
CD26 antigen
Contains Dipeptidyl peptidase 4 membrane form
     (Dipeptidyl peptidase IV membrane form)
Dipeptidyl peptidase 4 soluble form
     (Dipeptidyl peptidase IV soluble form)
Gene name
Name: Dpp4
Synonyms: Cd26
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Swiss;
TISSUE=Thymus;
PubMed=1370813 [NCBI, ExPASy, EBI, Israel, Japan]
Marguet D.A., Bernard A.-M., Vivier I., Darmoul D., Naquet P., Pierres M.;
"cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases.";
J. Biol. Chem. 267:2200-2208(1992).
[2]
SEQUENCE REVISION.
Marguet D.A.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B10.A;
TISSUE=Liver;
DOI=10.1021/bi00254a032; PubMed=7999781 [NCBI, ExPASy, EBI, Israel, Japan]
Bernard A.-M., Mattei M.-G., Pierres M., Marguet D.;
"Structure of the mouse dipeptidyl peptidase IV (CD26) gene.";
Biochemistry 33:15204-15214(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Kidney, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-20.
PubMed=1712807 [NCBI, ExPASy, EBI, Israel, Japan]
Vivier I., Marguet D.A., Naquet P., Bonicel J., Black D., Li C.X.-Y., Bernard A.-M., Gorvel J.-P., Pierres M.;
"Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV).";
J. Immunol. 147:447-454(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X58384; CAA41274.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12620; AAA82213.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12599; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12600; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12601; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12602; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12603; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12604; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12605; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12606; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12607; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12608; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12609; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12610; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12611; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12612; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12613; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12614; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12615; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12616; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12617; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12618; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12619; AAA82213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK085370; BAC39434.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK153939; BAE32266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022183; AAH22183.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S23752; S23752.
RefSeq NP_034204.1; -.
UniGene Mm.1151
3D structure databases
HSSP P27487; 1PFQ. [HSSP ENTRY / PDB]
SMR P28843; 37-759.
ModBase P28843.
Protein family/group databases
MEROPS S09.003; -.
PTM databases
PhosphoSite P28843; -.
Organism-specific databases
MGI MGI:94919; Dpp4.
Gene expression databases
ArrayExpress P28843; -.
CleanEx MM_DPP4; -.
GermOnline ENSMUSG00000035000; Mus musculus.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0046581; Cellular component: intercellular canaliculus (inferred from direct assay from MGI).
GO:0004177; Molecular function: aminopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002471; Pept_S9_AS.
IPR001375; Peptidase_S9.
IPR002469; Peptidase_S9B.
Graphical view of domain structure.
Pfam PF00930; DPPIV_N; 1.
PF00326; Peptidase_S9; 1.
Pfam graphical view of domain structure.
PROSITE PS00708; PRO_ENDOPEP_SER; 1.
BLOCKS P28843.
ProtoNet P28843.
Genome annotation databases
Ensembl ENSMUSG00000035000; Mus musculus. [Contig view]
GeneID 13482; -.
KEGG mmu:13482; -.
Phylogenomic databases
HOGENOM P28843; -.
HOVERGEN P28843; -.
Other
NextBio 283979; -.
SOURCE Dpp4; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminopeptidase; Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Protease; Secreted; Serine protease; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   760  760     Dipeptidyl peptidase 4 membrane form. PRO_0000027215
CHAIN   37   760  724     Dipeptidyl peptidase 4 soluble form (By similarity). PRO_0000027216
TOPO_DOM   1     6  6     Cytoplasmic (Potential). 
TRANSMEM   7    28  22     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   29   760  732     Extracellular (Potential). 
COMPBIAS   295   466  172     Cys-rich. 
ACT_SITE   624   624        Charge relay system (By similarity). 
ACT_SITE   702   702        Charge relay system (By similarity). 
ACT_SITE   734   734        Charge relay system (By similarity). 
CARBOHYD   83    83        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   90    90        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   213   213        N-linked (GlcNAc...) (Potential). 
CARBOHYD   223   223        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   315   315        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   328   328        N-linked (GlcNAc...) (Potential). 
CARBOHYD   514   514        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   679   679        N-linked (GlcNAc...) (By similarity). 
DISULFID   379   388        By similarity. 
DISULFID   438   441        By similarity. 
DISULFID   448   466        By similarity. 
DISULFID   643   756        By similarity. 
Sequence information
Length: 760 AA [This is the length of the unprocessed precursor] Molecular weight: 87437 Da [This is the MW of the unprocessed precursor] CRC64: A5F644B46E4A3DF8 [This is a checksum on the sequence]
        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 

P28843 in FASTA format

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View entry in raw text format (no links)
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