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Protein

Alpha-conotoxin PnIB

Gene
N/A
Organism
Conus pennaceus (Feathered cone) (Conus episcopus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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-7 > alpha-3/beta-2).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei54 – 541Direct interaction with nAChR alpha-7 subunit

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

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

Organism-specific databases

ConoServeri36. PnIB precursor.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541L → A: Blocks nAChR alpha-7 subunits with lower potency than PnIB and PnIA. Blocks nAChR alpha-3/beta-2 subunits with a potency range between the potency of PnIB and PnIA. 1 Publication
Mutagenesisi55 – 551S → N: Blocks nAChr alpha-7 subunits with higher potency than PnIB and PnIA. Blocks nAChR alpha-3/beta-2 subunits with a potency range between the potency of PnIB and PnIA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 44231 PublicationPRO_0000034883Add
BLAST
Peptidei45 – 6016Alpha-conotoxin PnIBPRO_0000034884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 521 Publication
Disulfide bondi47 ↔ 601 Publication
Modified residuei59 – 591Sulfotyrosine1 Publication
Modified residuei60 – 601Cysteine amide1 Publication

Keywords - PTMi

Amidation, Disulfide bond, Sulfation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
61
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 483Combined sources
Helixi50 – 556Combined sources
Turni57 – 593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKGX-ray1.10A45-60[»]
ProteinModelPortaliP50985.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50985.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]
PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50985-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMRMMFTVF LLVVLATTVV SFTSDRASDD GNAAASDLIA LTIKGCCSLP
60
PCALSNPDYC G
Length:61
Mass (Da):6,363
Last modified:January 16, 2004 - v2
Checksum:i42E0033324D66922
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF215088 mRNA. Translation: AAG60509.1.
PIRiB54877.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF215088 mRNA. Translation: AAG60509.1.
PIRiB54877.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKGX-ray1.10A45-60[»]
ProteinModelPortaliP50985.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri36. PnIB precursor.

Miscellaneous databases

EvolutionaryTraceiP50985.

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]
PROSITEiPS60014. ALPHA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mechanisms for evolving hypervariability: the case of conopeptides."
    Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.
    Mol. Biol. Evol. 18:120-131(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 OF 45-60, AMIDATION AT CYS-60.
    Tissue: Venom.
  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 OF 45-60, MUTAGENESIS OF LEU-54 AND SER-55.
  4. "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-59.
  5. "Crystal structure at 1.1-A resolution of alpha-conotoxin PnIB: comparison with alpha-conotoxins PnIA and GI."
    Hu S.H., Gehrmann J., Alewood P.F., Craik D.J., Martin J.L.
    Biochemistry 36:11323-11330(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 45-60, DISULFIDE BONDS.

Entry informationi

Entry nameiCA1B_CONPE
AccessioniPrimary (citable) accession number: P50985
Secondary accession number(s): Q9BP57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: July 22, 2015
This is version 87 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

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

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 one 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.