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P01500

- APAM_APIME

UniProt

P01500 - APAM_APIME

Protein

Apamin

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

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

    Keywords - Molecular functioni

    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: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78458 mRNA. Translation: AAB34402.1.
    PIRiA56710. AMHB.
    RefSeqiNP_001011612.1. NM_001011612.1.
    UniGeneiAme.1216.

    Genome annotation databases

    EnsemblMetazoaiGB18161-RA; GB18161-PA; GB18161.
    GeneIDi406135.
    KEGGiame:406135.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 GB18161-RA ; GB18161-PA ; GB18161 .
    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 1, 2014
    This is version 79 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