A1CHP1 (DPP4_ASPCL) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 13, 2012.
Version 30.
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 | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome] | ||||
| Taxonomic identifier | 344612 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › ![]() |
Protein attributes
| Sequence length | 768 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 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. |
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 membraneInferred from electronic annotation. Source: InterPro |
| Molecular_function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activityInferred 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 | 1 – 17 | 17 | Potential | ||||||
| Chain | 18 – 768 | 751 | Probable dipeptidyl peptidase 4 | PRO_0000397809 | |||||
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 | 38 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 81 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 104 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 113 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 221 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 282 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 468 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 668 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. Nierman W.C.PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DS027054 Genomic DNA. Translation: EAW10396.1. |
| RefSeq | XP_001271822.1. XM_001271821.1. |
3D structure databases | |
| ProteinModelPortal | A1CHP1. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.008. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADACLAT00005024; CADACLAP00004923; CADACLAG00005024. |
| GeneID | 4704099. |
| KEGG | act:ACLA_048680. |
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_ASPCL | ||||||||
| Accession | Primary (citable) accession number: A1CHP1 | ||||||||
| 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
