P11494 (BDS1_ANESU) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 76.
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: Antihypertensive protein BDS-1 Alternative name(s): Blood depressing substance I Short name=BDS-I |
| Organism | Anemonia sulcata (Mediterranean snakelocks sea anemone) (Anemonia viridis) |
| Taxonomic identifier | 6108 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Cnidaria › Anthozoa › Hexacorallia › Actiniaria › Nynantheae › Actiniidae › Anemonia![]() |
Protein attributes
| Sequence length | 43 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Blocks specifically the Kv3.4/KCNC4 potassium channel. Reduces blood pressure. Ref.2 |
| Subcellular location | |
| Sequence similarities | Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nematocyst Secreted |
| Molecular function | Ion channel impairing toxin Neurotoxin Potassium channel inhibitor Toxin |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | pathogenesis Inferred from electronic annotation. Source: InterPro |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nematocystInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | potassium channel inhibitor 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 | |||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 43 | 43 | Antihypertensive protein BDS-1 | PRO_0000221541 | |||||||||||||
Amino acid modifications | |||||||||||||||||
| Disulfide bond | 4 ↔ 39 | Ref.3 Ref.4 | |||||||||||||||
| Disulfide bond | 6 ↔ 32 | Ref.3 Ref.4 | |||||||||||||||
| Disulfide bond | 22 ↔ 40 | Ref.3 Ref.4 | |||||||||||||||
Natural variations | |||||||||||||||||
| Natural variant | 18 | 1 | L → F. | ||||||||||||||
Secondary structure | |||||||||||||||||
Helix Strand Turn | |||||||||||||||||
| Beta strand | 4 – 6 | 3 | |||||||||||||||
| Beta strand | 14 – 16 | 3 | |||||||||||||||
| Beta strand | 31 – 34 | 4 | |||||||||||||||
| Beta strand | 37 – 40 | 4 | |||||||||||||||
Sequences
References
| [1] | "Polypeptides, process for their preparation, and their use as hypotensive active compounds." Doppelfeld I.-S., Henschen-Edman A., Graf E., Zwick J., Beress L., Etschenberg E. Patent number DE3324689, 17-JAN-1985 Cited for: PROTEIN SEQUENCE. |
| [2] | "Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4." Diochot S., Schweitz H., Beress L., Lazdunski M. J. Biol. Chem. 273:6744-6749(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION. |
| [3] | "A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure." Driscoll P.C., Clore G.M., Beress L., Gronenborn A.M. Biochemistry 28:2178-2187(1989) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, DISULFIDE BONDS. |
| [4] | "Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing." Driscoll P.C., Gronenborn A.M., Beress L., Clore G.M. Biochemistry 28:2188-2198(1989) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, DISULFIDE BONDS. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A33041. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P11494. | ||||||||||||||||||
| SMR | P11494. Positions 1-43. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| TCDB | 8.B.11.1.3. sea anemone peptide toxin (APETx) family. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| Gene3D | 2.20.20.10. 1 hit. | ||||||||||||||||||
| InterPro | IPR012414. BDS_K_chnl_tox. IPR023355. Myo_neuro_toxin. [Graphical view] | ||||||||||||||||||
| Pfam | PF07936. Defensin_4. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P11494. | ||||||||||||||||||
Entry information
| Entry name | BDS1_ANESU | ||||||||
| Accession | Primary (citable) accession number: P11494 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Animal Toxin Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
