Dipeptidyl peptidase 4 - Bos taurus (Bovine)

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Reviewed, UniProtKB/Swiss-Prot P81425 (DPP4_BOVIN)

Last modified October 13, 2009. Version 72. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
    Adenosine deaminase complexing protein
      Short name=ADCP-I
    Activation molecule 3
      Short name=ACT3
    WC10
    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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	765 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Binds and regulates the activity of ADA.
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 By similarity. Dipeptidyl peptidase 4 soluble form: Secreted By similarity.
Tissue specificity	Intestinal epithelium, dendritic cells and several immune system tissues.
Post-translational modification	The soluble form (SDPP) derives from the membrane form (MDPP) by proteolytic processing By similarity.
Sequence similarities	Belongs to the peptidase S9B family. DPPIV subfamily.

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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 plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 765

765

Dipeptidyl peptidase 4 membrane form

PRO_0000027209

Chain

38 – 765

728

Dipeptidyl peptidase 4 soluble form By similarity

PRO_0000027210

Regions

Topological domain

1 – 6

Cytoplasmic Potential

Transmembrane

7 – 29

Signal-anchor for type II membrane protein Potential

Topological domain

30 – 765

736

Extracellular Potential

Sites

Active site

629

Charge relay system By similarity

Active site

707

Charge relay system By similarity

Active site

739

Charge relay system By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) By similarity

Glycosylation

N-linked (GlcNAc...) By similarity

Glycosylation

149

N-linked (GlcNAc...) Potential

Glycosylation

218

N-linked (GlcNAc...) By similarity

Glycosylation

228

N-linked (GlcNAc...) By similarity

Glycosylation

271

N-linked (GlcNAc...) Potential

Glycosylation

280

N-linked (GlcNAc...) By similarity

Glycosylation

320

N-linked (GlcNAc...) By similarity

Glycosylation

392

N-linked (GlcNAc...) Potential

Glycosylation

495

N-linked (GlcNAc...) Potential

Glycosylation

684

N-linked (GlcNAc...) By similarity

Disulfide bond

384 ↔ 393

By similarity

Disulfide bond

443 ↔ 446

By similarity

Disulfide bond

453 ↔ 471

By similarity

Disulfide bond

648 ↔ 761

By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P81425-1 [UniParc].

Last modified July 26, 2002. Version 3.
Checksum: E32165421F43E116
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FASTA

765

88,369

        10         20         30         40         50         60 
MKTPWKVLLG LLAIAALVTV ITVPVVLLTK GNDASTDSRR TYTLADYLKN TFRMKFYNLR 

        70         80         90        100        110        120 
WVSDHEYLYK QENNILLFNA EYGNSSIFLE NSTFDEFGHS INDYSVSPDR QYILFEYNYV 

       130        140        150        160        170        180 
KQWRHSYTAS YDIYDLNKRQ LITEERIPNN TQWITWSSVG HKLAYVWNND IYVKNEPNSP 

       190        200        210        220        230        240 
SQRITWTGKK DVIYNGITDW VYEEEVFSAY SALWWSPNST FLAYAQFNDT EVPLIEYSFY 

       250        260        270        280        290        300 
SDESLQYPKT VKIPYPKAGA VNPTIKFFVV NISSLSPNIN ATSQQIVPPG SVLIGDHYLC 

       310        320        330        340        350        360 
DVTWVTEERI SLQWLRRIQN YSIMDICDYD RSTGRWISSV GRQHIEISTT GWVGRFRPAE 

       370        380        390        400        410        420 
PHFTSDGNSF YKIISNEEGY KHICHFQTDK RNCTFITKGA WEVIGIEALT SDYLYYISNE 

       430        440        450        460        470        480 
YKGMPGARNL YKIQLNDYTK VTCLSCELNP DRCQYYSVSF SQEAKYYQLR CSGPGLPLYT 

       490        500        510        520        530        540 
LHNSNNDKEL RVLENNSDLD QVLQDVQMPS KKLDFIHLHG TKFWYQMILP PHFDKSKKYP 

       550        560        570        580        590        600 
LLLEVYAGPC SQKADAIFRL NWATYLASTE NIIVASFDGR GSGYQGDKIM HAINRRLGTF 

       610        620        630        640        650        660 
EVEDQIEATR QFSKMGFVDD KRIAIWGWSY GGYVTSMVLG AGSGVFKCGI AVAPVSKWEY 

       670        680        690        700        710        720 
YDSVYTERYM GLPTPEDNLD SYRNSTVMSR AENFKQVEYL LIHGTADDNV HFQQSAQISK 

       730        740        750        760 
ALVDAGVDFQ SMWYTDEDHG IASSTAHQHI YTHMSHFLKQ CFSLL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of bovine CD26 upregulated by a staphylococcal superantigen." Lee S.-U., Park Y.-H., Davis W.C., Hamilton M.J., Naessens J., Bohach G.A. Immunogenetics 54:216-220(2002) [PubMed: 12073152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphocyte.
[2]	"CD26 is expressed on a restricted subpopulation of dendritic cells in vivo." Gliddon D.R., Howard C.J. Eur. J. Immunol. 32:1472-1481(2002) [PubMed: 11981836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-17. Tissue: Thymus.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[4]	"Identity of activation molecule 3 on superantigen-stimulated bovine cells is CD26." Lee S.-U., Ferens W., Davis W.C., Hamilton M.J., Park Y.-H., Fox L.K., Naessens J., Bohach G.A. Infect. Immun. 69:7190-7193(2001) [PubMed: 11598101] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-24. Tissue: T-cell.
[5]	"The CP-I subunit of adenosine deaminase complexing protein from calf kidney is identical to human, mouse, and rat dipeptidyl peptidase IV." Ben-Shooshan I., Parola A.H. Comp. Biochem. Physiol. 119B:289-292(1998) [PubMed: 9629661] [Abstract] Cited for: PROTEIN SEQUENCE OF 537-546. Tissue: Kidney.

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Cross-references

Sequence databases
	AF461806 mRNA. Translation: AAL67836.1. AY056834 mRNA. Translation: AAL23628.1. BC102523 mRNA. Translation: AAI02524.1.
IPI	IPI00702238.
RefSeq	NP_776464.1.
UniGene	Bt.8282
3D structure databases
HSSP	HSSP built from PDB template 1PFQ based on UniProtKB P27487.
SMR	P81425. Positions 38-764.
ModBase	Search...
Protein-protein interaction databases
STRING	P81425.
Protein family/group databases
MEROPS	S09.003.
Genome annotation databases
Ensembl	ENSBTAT00000056886; ENSBTAP00000049191; ENSBTAG00000015330; Bos taurus. [Genome view]
GeneID	281122.
KEGG	bta:281122.
Organism-specific databases
CTD	281122.
Phylogenomic databases
HOVERGEN	P81425.
Enzyme and pathway databases
BRENDA	3.4.14.5. 251.
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...

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Entry information

Entry name

DPP4_BOVIN

Accession

Primary (citable) accession number: P81425
Secondary accession number(s): Q3ZCC2, Q8WMG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 26, 2002
Last modified:	October 13, 2009
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents