Q9BPE9 · CTA1_CONPE
- ProteinChi-conotoxin PnID
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2). Of the 3 native isomers, only the isomer with a ribbon disulfide configuration shows pharmacological activity and 3D structure similar to other chi-conotoxins. This ribbon isomer (disulfide pattern: C1-C4 and C2-C3) inhibits the rat norepinephrine transporter (IC50=10 uM). In contrast, the globular isomer of PnID shows more than ten times less activity against this transporter and the beaded isomer does not display any measurable biological activity.
Miscellaneous
Negative results: the 3 native isomers do not produce effects on the activity of the dopamine transporter (DAT/SLC6A3) and the serotonin transporter (SERT/SLC6A4).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | toxin activity |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameChi-conotoxin PnID
- Short namesPnID A ; PnID B ; PnID C
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Gastropoda > Caenogastropoda > Neogastropoda > Conoidea > Conidae > Conus > Darioconus
Accessions
- Primary accessionQ9BPE9
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, peptide, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MRCLPVFVILLLLTASGPSVDA | ||||||
Propeptide | PRO_0000404979 | 23-51 | ||||
Sequence: KVHLKTKGDGPLSSFRDNAKSTLQRLQDK | ||||||
Peptide | PRO_0000404980 | 52-63 | Chi-conotoxin PnID | |||
Sequence: STCCGYRMCVPC | ||||||
Disulfide bond | 54↔55 | beaded isomer; alternate | ||||
Sequence: CC | ||||||
Disulfide bond | 54↔60 | globular isomer; alternate | ||||
Sequence: CCGYRMC | ||||||
Disulfide bond | 54↔63 | ribbon isomer; alternate | ||||
Sequence: CCGYRMCVPC | ||||||
Disulfide bond | 55↔60 | ribbon isomer; alternate | ||||
Sequence: CGYRMC | ||||||
Disulfide bond | 55↔63 | globular isomer; alternate | ||||
Sequence: CGYRMCVPC | ||||||
Disulfide bond | 60↔63 | beaded isomer; alternate | ||||
Sequence: CVPC | ||||||
Modified residue | 63 | Cysteine amide | ||||
Sequence: C |
Post-translational modification
Three isomers are found in the venom. The ribbon isomer (C1-C4, C2-C3) is the only one active towards noradrenaline transporters.
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom duct.
Structure
Family & Domains
Domain
The cysteine framework is I (CC-C-C). Alpha4/2 pattern.
Sequence similarities
Belongs to the conotoxin T superfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length64
- Mass (Da)6,928
- Last updated2001-06-01 v1
- Checksum0AB87620FCCC1410
Keywords
- Technical term