D4APE2 (DPP4_ARTBC) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 13, 2012.
Version 16.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable dipeptidyl peptidase 4 EC=3.4.14.5 Alternative name(s): Dipeptidyl peptidase IV Short name=DPP IV Short name=DppIV | ||||
| Gene names |
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| Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) [Complete proteome] | ||||
| Taxonomic identifier | 663331 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Arthrodermataceae › Arthroderma › ![]() |
Protein attributes
| Sequence length | 778 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. Contributes to pathogenicity By similarity. |
| 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 | |
| Sequence similarities | Belongs to the peptidase S9B family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Virulence |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Aminopeptidase Hydrolase Protease Serine protease |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: InterPro |
| Molecular_function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||
| Chain | 19 – 778 | 760 | Probable dipeptidyl peptidase 4 | PRO_0000397808 | |||||
Sites | |||||||||
| Active site | 616 | 1 | Charge relay system By similarity | ||||||
| Active site | 693 | 1 | Charge relay system By similarity | ||||||
| Active site | 728 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 84 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 114 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 222 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Comparative and functional genomics provide insights into the pathogenicity of dermatophytic fungi." Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O., Schroeckh V. Brakhage A.A.Genome Biol. 12:R7.1-R7.16(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. Strain: ATCC MYA-4681 / CBS 112371. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABSU01000004 Genomic DNA. Translation: EFE35153.1. |
| RefSeq | XP_003015798.1. XM_003015752.1. |
3D structure databases | |
| ProteinModelPortal | D4APE2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 9526080. |
| KEGG | abe:ARB_06110. |
Phylogenomic databases | |
| KO | K01278. |
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... |
Entry information
| Entry name | DPP4_ARTBC | ||||||||
| Accession | Primary (citable) accession number: D4APE2 | ||||||||
| Entry history |
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| 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 |

Clusters with
