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Protein

Alpha-conotoxin PrXA

Gene
N/A
Organism
Conus parius (Cone snail)
Status
Reviewed-Annotation score: -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 inhibits both adult and fetal (alpha-1/beta-1/epsilon/delta and alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR). In vivo, it causes paralysis and death in mice and fish.1 Publication

GO - Molecular functioni

Keywordsi

Molecular functionAcetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-conotoxin PrXACurated
Short name:
Alpha-C-PrXA1 Publication
OrganismiConus parius (Cone snail)
Taxonomic identifieri505247 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConusPhasmoconus

Organism-specific databases

ConoServeri2859 PrXA

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000044420324 – 511 PublicationAdd BLAST28
PeptideiPRO_000036603252 – 83Alpha-conotoxin PrXA1 PublicationAdd BLAST32

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei614-hydroxyproline1 Publication1
Disulfide bondi64 ↔ 711 Publication
Modified residuei754-hydroxyproline1 Publication1
Modified residuei794-hydroxyproline1 Publication1
Modified residuei83Glutamic acid 1-amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0C8S5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The cysteine framework is C-C.Curated

Keywords - Domaini

Signal

Sequencei

Sequence statusi: Complete.

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

P0C8S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTAYWVMVM MMVMWITAPL SEGGKPKLII RGLVPNDLTP QRILRSLISG
60 70 80
RTYGIYDAKP PFSCAGLRGG CVLPPNLRPK FKEGR
Length:85
Mass (Da):9,492
Last modified:May 23, 2018 - v2
Checksum:iD4886B945F09A0FB
GO

Mass spectrometryi

Molecular mass is 3540.7 Da from positions 1 - 83. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ981401 mRNA Translation: ADN79120.1

Similar proteinsi

Entry informationi

Entry nameiCCAA_CONPI
AccessioniPrimary (citable) accession number: P0C8S5
Secondary accession number(s): E2DEK9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: May 23, 2018
Last modified: May 23, 2018
This is version 18 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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