Reviewed, UniProtKB/Swiss-Prot P59944 (KAX1D_LEIQH)

Names and origin

Protein names	Recommended name:     Potassium channel toxin alpha-KTx 1.13 Alternative name(s):     Charybdotoxin c       Short name=ChTx-c
Organism	Leiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifier	6884 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Leiurus

Protein attributes

Sequence length	37 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Blocks calcium-activated potassium channels By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 1 subfamily.

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Ionic channel inhibitor Neurotoxin Potassium channel inhibitor Toxin
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	potassium channel inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Peptide	1 – 37	37	Potassium channel toxin alpha-KTx 1.13		PRO_0000044892
Regions
	Region	26 – 33	8	Interaction with Ca(2+)-activated K(+) channels Potential
Amino acid modifications
	Modified residue	1	1	Pyrrolidone carboxylic acid
	Disulfide bond	7 ↔ 28		By similarity
	Disulfide bond	13 ↔ 33		By similarity
	Disulfide bond	17 ↔ 35		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59944-1 [UniParc]. Last modified October 31, 2003. Version 1. Checksum: 29319BCB43994EE2	FASTA	37	4,318
	10 20 30 QFTNVSCTTS KECWSVCEKL YNTSRGKCMN KKCRCYS

References

[1]	"Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium, and chloride channels." Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M. J. Mol. Evol. 48:187-196(1999) [PubMed: 9929387] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001947. Scorpion_toxinS. [Graphical view]
Pfam	PF00451. Toxin_2. 1 hit. [Graphical view]
PRINTS	PR00286. CHARYBDTOXIN.
ProDom	PD003586. Scorpion_toxinS. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS01138. SCORP_SHORT_TOXIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KAX1D_LEIQH

Accession

Primary (citable) accession number: P59944

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 31, 2003
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)