C5FJE3 (DPP4_ARTOC) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 24.
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: 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 otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) [Complete proteome] | ||||
| Taxonomic identifier | 554155 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Arthrodermataceae › Arthroderma › ![]() |
Protein attributes
| Sequence length | 775 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
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 | Secreted By similarity. |
| Sequence similarities | Belongs to the peptidase S9B family. |
| Sequence caution | The sequence EEQ29564.1 differs from that shown. Reason: Erroneous initiation. |
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 – 15 | 15 | Potential | ||||||
| Chain | 16 – 775 | 760 | Dipeptidyl peptidase 4 | PRO_0000384087 | |||||
Sites | |||||||||
| Active site | 613 | 1 | Charge relay system By similarity | ||||||
| Active site | 690 | 1 | Charge relay system By similarity | ||||||
| Active site | 725 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 81 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 111 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 219 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 731 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Comparative genome analysis of Trichophyton rubrum and related dermatophytes reveals candidate genes involved in infection." Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W., Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E., Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I., Rossi A., Saif S. White T.C.MBio 3:E259-E259(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4605 / CBS 113480. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DS995702 Genomic DNA. Translation: EEQ29564.1. Different initiation. |
| RefSeq | XP_002849449.1. XM_002849403.1. |
3D structure databases | |
| ProteinModelPortal | C5FJE3. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.008. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 9226525. |
Phylogenomic databases | |
| OrthoDB | EOG4HB1TN. |
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_ARTOC | ||||||||
| Accession | Primary (citable) accession number: C5FJE3 | ||||||||
| 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
