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P11494

- BDS1_ANESU

UniProt

P11494 - BDS1_ANESU

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Protein
Antihypertensive protein BDS-1
Gene
N/A
Organism
Anemonia sulcata (Mediterranean snakelocks sea anemone) (Anemonia viridis)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Blocks specifically the Kv3.4/KCNC4 potassium channel. Reduces blood pressure.1 Publication

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Protein family/group databases

TCDBi8.B.11.1.3. the sea anemone peptide toxin (apetx) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Antihypertensive protein BDS-1
Alternative name(s):
Blood depressing substance I
Short name:
BDS-I
OrganismiAnemonia sulcata (Mediterranean snakelocks sea anemone) (Anemonia viridis)
Taxonomic identifieri6108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaNynantheaeActiniidaeAnemonia

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. nematocyst Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4343Antihypertensive protein BDS-1
PRO_0000221541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 392 Publications
Disulfide bondi6 ↔ 322 Publications
Disulfide bondi22 ↔ 402 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Beta strandi14 – 163
Beta strandi31 – 344
Beta strandi37 – 404

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDSNMR-A1-43[»]
2BDSNMR-A1-43[»]
ProteinModelPortaliP11494.
SMRiP11494. Positions 1-43.

Miscellaneous databases

EvolutionaryTraceiP11494.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.20.20.10. 1 hit.
InterProiIPR012414. BDS_K_chnl_tox.
IPR023355. Myo_neuro_toxin.
[Graphical view]
PfamiPF07936. Defensin_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11494-1 [UniParc]FASTAAdd to Basket

« Hide

AAPCFCSGKP GRGDLWILRG TCPGGYGYTS NCYKWPNICC YPH          43
Length:43
Mass (Da):4,714
Last modified:October 1, 1989 - v1
Checksum:i7C17846E88E2F1D8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181L → F.

Sequence databases

PIRiA33041.

Cross-referencesi

Sequence databases

PIRi A33041.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BDS NMR - A 1-43 [» ]
2BDS NMR - A 1-43 [» ]
ProteinModelPortali P11494.
SMRi P11494. Positions 1-43.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 8.B.11.1.3. the sea anemone peptide toxin (apetx) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P11494.

Family and domain databases

Gene3Di 2.20.20.10. 1 hit.
InterProi IPR012414. BDS_K_chnl_tox.
IPR023355. Myo_neuro_toxin.
[Graphical view ]
Pfami PF07936. Defensin_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiBDS1_ANESU
AccessioniPrimary (citable) accession number: P11494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 16, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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