Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tertiapin

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.6 Publications

Miscellaneous

Tertiapin-Q is a stable (non-oxidizable) and functionally similar derivative of tertiapin whose Met-13 residue is replaced with a Gln residue.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei12Is responsible of pH dependence of the channel block1
Sitei13Susceptible to oxidation1 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionCalcium-activated potassium channel impairing toxin, Calmodulin-binding, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Presynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Tertiapin1 Publication
Short name:
TPN1 Publication
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaHymenopteraApocritaAculeataApoideaApidaeApis
Proteomesi
  • UP000005203 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1A → Y: Inhibits with high affinity rat but not human Kir1.1 channels stably expressed in HEK293 cells; when associated with K-12 and Q-13. 1 Publication1
Mutagenesisi12H → K: Eliminates the pH dependence of the channel block; when associated with Q-13. Inhibits with high affinity rat but not human Kir1.1 channels stably expressed in HEK293 cells; when associated with Y-1 and Q-13. 2 Publications1
Mutagenesisi13M → Q: Stable fully functional peptide. Inhibits with high affinity rat but not human Kir1.1 channels stably expressed in HEK293 cells; when associated with Y-1 and K-12. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000445391 – 21Tertiapin2 PublicationsAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 141 PublicationImported
Disulfide bondi5 ↔ 181 PublicationImported

Post-translational modificationi

Oxidation of Met-13 results in the loss of biological activity.1 Publication
An amidation at Lys-21 is suggested in Ref. 1.1 Publication

Keywords - PTMi

Disulfide bond, Oxidation

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Interactioni

GO - Molecular functioni

Structurei

Secondary structure

121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SMRiP56587
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56587

Family & Domainsi

Family and domain databases

InterProiView protein in InterPro
IPR035361 Bee_toxin
PfamiView protein in Pfam
PF17454 Bee_toxin, 1 hit

Sequencei

Sequence statusi: Complete.

P56587-1 [UniParc]FASTAAdd to basket
« Hide
        10         20 
ALCNCNRIII PHMCWKKCGK K
Length:21
Mass (Da):2,460
Last modified:December 15, 1998 - v1
Checksum:i7B3C2D5A490339B8
GO

Mass spectrometryi

Molecular mass is 2458 Da from positions 1 - 21. Determined by MALDI. 1 Publication

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Tertiapin entry

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TERNMR-A1-21[»]
SMRiP56587
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56587

Family and domain databases

InterProiView protein in InterPro
IPR035361 Bee_toxin
PfamiView protein in Pfam
PF17454 Bee_toxin, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTERT_APIME
AccessioniPrimary (citable) accession number: P56587
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: October 10, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again