Skip Header

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

P01500

- APAM_APIME

UniProt

P01500 - APAM_APIME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Apamin

Gene
N/A
Organism
Apis mellifera (Honeybee)
Status
Reviewed - 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: Unassembled WGS sequence, UP000005203: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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.
OMAiNCKAPET.

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 .
PIRi A56710. AMHB.
RefSeqi NP_001011612.1. NM_001011612.1.
UniGenei Ame.1216.

3D structure databases

ProteinModelPortali P01500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7460.P01500.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai GB40697-RA ; GB40697-PA ; GB40697 .
GeneIDi 406135.
KEGGi ame:406135.

Organism-specific databases

CTDi 406135.

Phylogenomic databases

HOGENOMi HOG000033980.
OMAi NCKAPET.

Family and domain databases

ProtoNeti Search...

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(1995) [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(1967) [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(1967)
    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(1988) [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(1991) [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: October 29, 2014
This is version 80 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