B1A4F7 (VDDP4_VESVU) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 17.
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: Venom dipeptidyl peptidase 4 EC=3.4.14.5 Alternative name(s): Venom dipeptidyl peptidase IV Allergen=Ves v 3 |
| Organism | Vespula vulgaris (Yellow jacket) (Wasp) |
| Taxonomic identifier | 7454 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Vespoidea › Vespidae › Vespinae › Vespula![]() |
Protein attributes
| Sequence length | 776 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 | Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process venom proteins into their activ forms and/or modulate the chemotactic activity of immune cells after the insect sting. 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. Ref.1 |
| Enzyme regulation | Inhibited by diprotin A. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. Ref.1 |
| Allergenic properties | Causes an allergic reaction in human. Ref.1 |
| Sequence similarities | Belongs to the peptidase S9B family. DPPIV subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Disease | Allergen |
| Domain | Signal |
| Molecular function | Aminopeptidase Hydrolase Protease |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Direct protein sequencing |
| 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: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||||
| Chain | 26 – 776 | 751 | Venom dipeptidyl peptidase 4 | PRO_0000401924 | |||||||
Sites | |||||||||||
| Active site | 638 | 1 | Charge relay system By similarity | ||||||||
| Active site | 717 | 1 | Charge relay system By similarity | ||||||||
| Active site | 749 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 44 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 66 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 329 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 504 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 577 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 688 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 693 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 449 ↔ 452 | By similarity | |||||||||
| Disulfide bond | 462 ↔ 480 | By similarity | |||||||||
| Disulfide bond | 658 ↔ 769 | By similarity | |||||||||
Sequences
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References
| [1] | "Identification, recombinant expression, and characterization of the 100 kDa high molecular weight hymenoptera venom allergens Api m 5 and Ves v 3." Blank S., Seismann H., Bockisch B., Braren I., Cifuentes L., McIntyre M., Ruhl D., Ring J., Bredehorst R., Ollert M.W., Grunwald T., Spillner E. J. Immunol. 184:5403-5413(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 83-86; 301-309; 536-539; 548-555 AND 606-613, MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLERGEN. Tissue: Venom and Venom duct. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EU420987 mRNA. Translation: ACA00159.1. |
3D structure databases | |
| ProteinModelPortal | B1A4F7. |
| ModBase | Search... |
Protein family/group databases | |
| Allergome | 5767. Ves v 3. 5768. Ves v 3.0101. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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] |
| ProtoNet | Search... |
Entry information
| Entry name | VDDP4_VESVU | ||||||||
| Accession | Primary (citable) accession number: B1A4F7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Allergens Nomenclature of allergens and list of entries |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
