Dipeptidyl peptidase 4 precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q2UH35 (DPP4_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 44. History...

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

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Short name=DppIV

Gene names

Name:	dpp4
ORF Names:	AO090023000602

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	771 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	Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Ref.1
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.
Subcellular location	Secreted Ref.1.
Sequence similarities	Belongs to the peptidase S9B family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0. is active between pH 4.0 and 9.0. Ref.1
Sequence caution	The sequence CAA05343.1 differs from that shown. Reason: Frameshift at positions 63 and 87.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Aminopeptidase Hydrolase Protease Serine protease
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

16

Potential

Chain

755

Dipeptidyl peptidase 4

PRO_5000064328

Sites

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Active site

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q2UH35 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 25A9C096B0258A7B
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771

86,875

        10         20         30         40         50         60 
MKYSKLLLLL VSVVQALDVP RKPHAPTGEG SKRLTFNETV VKQAITPTSR SVQWLSGAED 

        70         80         90        100        110        120 
GSYVYAAEDG SLTIENIVTN ESRTLIPADK IPTGKEAFNY WIHPDLSSVL WASNHTKQYR 

       130        140        150        160        170        180 
HSFFADYYVQ DVESLKSVPL MPDQEGDIQY AQWSPVGNTI AFVRENDLYV WDNGTVTRIT 

       190        200        210        220        230        240 
DDGGPDMFHG VPDWIYEEEI LGDRYALWFS PDGEYLAYLS FNETGVPTYT VQYYMDNQEI 

       250        260        270        280        290        300 
APAYPWELKI RYPKVSQTNP TVTLSLLNIA SKEVKQAPID AFESTDLIIG EVAWLTDTHT 

       310        320        330        340        350        360 
TVAAKAFNRV QDQQKVVAVD TASNKATVIS DRDGTDGWLD NLLSMKYIGP IKPSDKDAYY 

       370        380        390        400        410        420 
IDISDHSGWA HLYLFPVSGG EPIPLTKGDW EVTSILSIDQ ERQLVYYLST QHHSTERHLY 

       430        440        450        460        470        480 
SVSYSTFAVT PLVDDTVAAY WSASFSANSG YYILTYGGPD VPYQELYTTN STKPLRTITD 

       490        500        510        520        530        540 
NAKVLEQIKD YALPNITYFE LPLPSGETLN VMQRLPPGFS PDKKYPILFT PYGGPGAQEV 

       550        560        570        580        590        600 
TKRWQALNFK AYVASDSELE YVTWTVDNRG TGFKGRKFRS AVTRQLGLLE AEDQIYAAQQ 

       610        620        630        640        650        660 
AANIPWIDAD HIGIWGWSFG GYLTSKVLEK DSGAFTLGVI TAPVSDWRFY DSMYTERYMK 

       670        680        690        700        710        720 
TLSTNEEGYE TSAVRKTDGF KNVEGGFLIQ HGTGDDNVHF QNSAALVDLL MGDGVSPEKL 

       730        740        750        760        770 
HSQWFTDSDH GISYHGGGVF LYKQLARKLY QEKNRQTQVL MHQWTKKDLE E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the prolyl dipeptidyl peptidase gene (dppIV) from the koji mold Aspergillus oryzae." Doumas A., van den Broek P., Affolter M., Monod M. Appl. Environ. Microbiol. 64:4809-4815(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ002369 Genomic DNA. Translation: CAA05343.1. Frameshift. AP007157 Genomic DNA. Translation: BAE59130.1.
RefSeq	XP_001821132.1. XM_001821080.2.
3D structure databases
ProteinModelPortal	Q2UH35.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00007556.
Protein family/group databases
MEROPS	S09.008.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00007710; CADAORAP00007556; CADAORAG00007710.
GeneID	5993134.
KEGG	aor:AOR_1_1034144.
Phylogenomic databases
eggNOG	COG1506.
HOGENOM	HOG000189891.
KO	K01278.
OrthoDB	EOG4HB1TN.
Family and domain databases
InterPro	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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPP4_ASPOR

Accession

Primary (citable) accession number: Q2UH35
Secondary accession number(s): O42812

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	January 24, 2006
Last modified:	May 29, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents