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Protein

Apamin

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Neurotoxin that blocks voltage-independent calcium-activated potassium channels (KCNN1=SK1, KCNN2=SK2, KCNN3=SK3).

Keywords - Molecular functioni

Calcium-activated potassium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Apamin
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
ProteomesiUP000005203 Componentsi: Unassembled WGS sequence, Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27272 PublicationsAdd
BLAST
Peptidei28 – 4518ApaminPRO_0000018611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 38
Disulfide bondi30 ↔ 42
Modified residuei45 – 451Histidine amide

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Protein-protein interaction databases

STRINGi7460.P01500.

Structurei

3D structure databases

ProteinModelPortaliP01500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 412Essential for toxin activity

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000033980.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01500-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
MISMLRCIYL FLSVILITSY FVTPVMPCNC KAPETALCAR RCQQHG
Length:46
Mass (Da):5,223
Last modified:October 1, 1996 - v2
Checksum:i92694A07501AEE33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78458 mRNA. Translation: AAB34402.1.
PIRiA56710. AMHB.
RefSeqiNP_001011612.1. NM_001011612.1.
UniGeneiAme.1216.

Genome annotation databases

EnsemblMetazoaiGB40697-RA; GB40697-PA; GB40697.
GeneIDi406135.
KEGGiame:406135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78458 mRNA. Translation: AAB34402.1.
PIRiA56710. AMHB.
RefSeqiNP_001011612.1. NM_001011612.1.
UniGeneiAme.1216.

3D structure databases

ProteinModelPortaliP01500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7460.P01500.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiGB40697-RA; GB40697-PA; GB40697.
GeneIDi406135.
KEGGiame:406135.

Organism-specific databases

CTDi406135.

Phylogenomic databases

HOGENOMiHOG000033980.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon."
    Gmachl M., Kreil G.
    J. Biol. Chem. 270:12704-12708(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Sequence analysis of bee venom neurotoxin (apamine) from its tryptic and chymotryptic cleavage products."
    Haux P., Sawerthal H., Habermann E.
    Hoppe-Seyler's Z. Physiol. Chem. 348:737-738(1966) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-45.
    Tissue: Venom.
  3. Shipolini R., Bradbury A.F., Callewaert G.L., Vernon C.A.
    J. Chem. Soc. Chem. Commun. 1967:679-680(1966)
    Cited for: PROTEIN SEQUENCE OF 28-45.
    Tissue: Venom.
  4. "Solution structure of apamin determined by nuclear magnetic resonance and distance geometry."
    Pease J.H.B., Wemmer D.E.
    Biochemistry 27:8491-8498(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 28-45.
  5. "Spatial structure of apamin in solution."
    Andrianov A.M., Akhrem A.A.
    Mol. Biol. (Mosk.) 25:937-945(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 28-45.
  6. Cited for: SYNTHESIS, ACTIVITY OF ANALOGS.

Entry informationi

Entry nameiAPAM_APIME
AccessioniPrimary (citable) accession number: P01500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.