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UniProtKB/Swiss-Prot entry P50985


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CXAB_CONPE
Primary accession number P50985
Secondary accession number Q9BP57
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 16, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Alpha-conotoxin PnIB [Precursor]
Synonyms None
Gene name None
From
Conus pennaceus (Feathered cone) [TaxID: 37335] 
Taxonomy Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda; Apogastropoda; Caenogastropoda; Sorbeoconcha; Hypsogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11158371 [NCBI, ExPASy, EBI, Israel, Japan]
Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
"Mechanisms for evolving hypervariability: the case of conopeptides.";
Mol. Biol. Evol. 18:120-131(2001).
[2]
PROTEIN SEQUENCE OF 45-60.
TISSUE=Venom;
DOI=10.1021/bi00198a018; PubMed=8068627 [NCBI, ExPASy, EBI, Israel, Japan]
Fainzilber M., Hasson A., Oren R., Burlingame A.L., Gordon D., Spira M.E., Zlotkin E.;
"New mollusc-specific alpha-conotoxins block Aplysia neuronal acetylcholine receptors.";
Biochemistry 33:9523-9529(1994).
[3]
FUNCTION, SYNTHESIS, AND MUTAGENESIS OF LEU-54 AND SER-55.
DOI=10.1021/bi991252j; PubMed=10545176 [NCBI, ExPASy, EBI, Israel, Japan]
Luo S., Nguyen T.A., Cartier G.E., Olivera B.M., Yoshikami D., McIntosh J.M.;
"Single-residue alteration in alpha-conotoxin PnIA switches its nAChR subtype selectivity.";
Biochemistry 38:14542-14548(1999).
[4]
SULFATION AT TYR-59.
DOI=10.1002/(SICI)1096-9888(199904)34:4<447::AID-JMS801>3.3.CO;2-T; PubMed=10226369 [NCBI, ExPASy, EBI, Israel, Japan]
Wolfender J.L., Chu F., Ball H., Wolfender F., Fainzilber M., Baldwin M.A., Burlingame A.L.;
"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.";
J. Mass Spectrom. 34:447-454(1999).
[5]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 45-60, AND DISULFIDE BONDS.
DOI=10.1021/bi9713052; PubMed=9298951 [NCBI, ExPASy, EBI, Israel, Japan]
Hu S.H., Gehrmann J., Alewood P.F., Craik D.J., Martin J.L.;
"Crystal structure at 1.1-A resolution of alpha-conotoxin PnIB: comparison with alpha-conotoxins PnIA and GI.";
Biochemistry 36:11323-11330(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF215088; AAG60509.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B54877; B54877.
3D structure databases
PDB
1AKG; X-ray; 1.10 A; A=45-60.[ExPASy / RCSB / EBI]
PDBsum 1AKG; -.
ModBase P50985.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0045211; Cellular component: postsynaptic membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030550; Molecular function: acetylcholine receptor inhibitor activity (inferred from electronic annotation from InterPro).
GO:0009405; Biological process: pathogenesis (inferred from electronic annotation from InterPro).
GO:0007268; Biological process: synaptic transmission (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR009958; Conotoxin_a-typ.
Graphical view of domain structure.
Pfam PF07365; Toxin_8; 1.
Pfam graphical view of domain structure.
PROSITE PS60014; ALPHA_CONOTOXIN; 1.
Other
ProtoNet P50985.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylcholine receptor inhibitor; Amidation; Direct protein sequencing; Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Sulfation; Toxin.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1   21  21     Potential. 
PROPEP   22   44  23      PRO_0000034883
PEPTIDE   45   60  16     Alpha-conotoxin PnIB. PRO_0000034884
SITE   54   54  1     Direct interaction with nAChR alpha-7 subunit. 
MOD_RES   59   59        Sulfotyrosine. 
MOD_RES   60   60        Cysteine amide. 
DISULFID   46   52         
DISULFID   47   60         
MUTAGEN   54   54        L->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. 
MUTAGEN   55   55        S->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. 
HELIX   46   48  3      
HELIX   50   55  6      
TURN   57   59  3      
Sequence information
Length: 61 AA [This is the length of the unprocessed precursor] Molecular weight: 6363 Da [This is the MW of the unprocessed precursor] CRC64: 42E0033324D66922 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGMRMMFTVF LLVVLATTVV SFTSDRASDD GNAAASDLIA LTIKGCCSLP PCALSNPDYC 


G 

P50985 in FASTA format

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