Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P50984

- CA1A_CONPE

UniProt

P50984 - CA1A_CONPE

Protein

Alpha-conotoxin PnIA

Gene
N/A
Organism
Conus pennaceus (Feathered cone) (Conus episcopus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4).2 Publications

    Keywords - Molecular functioni

    Acetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-conotoxin PnIA
    Short name:
    Alpha-PnIA
    OrganismiConus pennaceus (Feathered cone) (Conus episcopus)
    Taxonomic identifieri37335 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri75. Pni1.
    51. PnIA.

    Subcellular locationi

    GO - Cellular componenti

    1. other organism postsynaptic membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101A → L: Blocks nAChr alpha-7 subunits with higher potency than PnIA and PnIB. Blocks nAChR alpha-3/beta-2 subunits with a potency range between the potency of PnIA and PnIB. 1 Publication
    Mutagenesisi11 – 111N → S: Blocks nAChR alpha-7 subunits with lower potency than PnIA and PnIB. Blocks nAChR alpha-3/beta-2 subunits with a potency range between the potency of PnIA and PnIB. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 1616Alpha-conotoxin PnIAPRO_0000044462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi2 ↔ 82 Publications
    Disulfide bondi3 ↔ 162 Publications
    Modified residuei15 – 151Sulfotyrosine1 Publication
    Modified residuei16 – 161Cysteine amide1 Publication

    Keywords - PTMi

    Amidation, Disulfide bond, Sulfation

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-60493N.

    Structurei

    Secondary structure

    1
    16
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 43
    Helixi6 – 116
    Turni13 – 153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PENX-ray1.10A1-16[»]
    2BR8X-ray2.40F/G/H/I/J1-16[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50984.

    Family & Domainsi

    Domaini

    The cysteine framework is I (CC-C-C). Alpha4/7 pattern.

    Sequence similaritiesi

    Belongs to the conotoxin A superfamily.Curated

    Family and domain databases

    InterProiIPR018072. Conotoxin_a-typ_CS.
    [Graphical view]
    PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50984-1 [UniParc]FASTAAdd to Basket

    « Hide

    GCCSLPPCAA NNPDYC                                        16
    Length:16
    Mass (Da):1,628
    Last modified:October 1, 1996 - v1
    Checksum:i05310FF95EC99005
    GO

    Sequence databases

    PIRiA54877.

    Cross-referencesi

    Sequence databases

    PIRi A54877.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PEN X-ray 1.10 A 1-16 [» ]
    2BR8 X-ray 2.40 F/G/H/I/J 1-16 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60493N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 75. Pni1.
    51. PnIA.

    Miscellaneous databases

    EvolutionaryTracei P50984.

    Family and domain databases

    InterProi IPR018072. Conotoxin_a-typ_CS.
    [Graphical view ]
    PROSITEi PS60014. ALPHA_CONOTOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "New mollusc-specific alpha-conotoxins block Aplysia neuronal acetylcholine receptors."
      Fainzilber M., Hasson A., Oren R., Burlingame A.L., Gordon D., Spira M.E., Zlotkin E.
      Biochemistry 33:9523-9529(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION.
      Tissue: Venom.
    2. "Identification of tyrosine sulfation in Conus pennaceus conotoxins alpha-PnIA and alpha-PnIB: further investigation of labile sulfo- and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atmospheric pressure MALDI mass spectrometry."
      Wolfender J.L., Chu F., Ball H., Wolfender F., Fainzilber M., Baldwin M.A., Burlingame A.L.
      J. Mass Spectrom. 34:447-454(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-15.
    3. "Single-residue alteration in alpha-conotoxin PnIA switches its nAChR subtype selectivity."
      Luo S., Nguyen T.A., Cartier G.E., Olivera B.M., Yoshikami D., McIntosh J.M.
      Biochemistry 38:14542-14548(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SYNTHESIS, MUTAGENESIS OF ALA-10 AND ASN-11.
    4. "The 1.1 A crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus."
      Hu S.-H., Gehrmann J., Guddat L.W., Alewood P.F., Craik D.J., Martin J.L.
      Structure 4:417-423(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.

    Entry informationi

    Entry nameiCA1A_CONPE
    AccessioniPrimary (citable) accession number: P50984
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 75 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