Q0GY40 (KBX3_HADGE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hge-scorpine Alternative name(s): Hg-scorpine-like 1 Short name=HgeScplp1 Short name=Hgscplike1 Cleaved into the following chain: Hge36
Organism	Hadrurus gertschi (Scorpion)
Taxonomic identifier	380989 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Arachnida › Scorpiones › Iurida › Iuroidea › Caraboctonidae › Hadrurinae › Hadrurus

Protein attributes

Sequence length	95 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hge-scorpine has antibacterial activity against B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic activities. Ref.3 Hge36 peptide blocks Kv1.1/KCNA1 (IC50=185 nM) potassium channels. Shows a weak hemolytic activity. Ref.3
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Miscellaneous	The C-terminus (AA 52-95) blocks Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA2 potassium channels, showing a potential important role of AA 48-51. Hge36 peptide does not block Kv1.2/KCNA2 and Kv1.3/KCNA3 (Ref.3).
Sequence similarities	Belongs to the long chain scorpion toxin family. Class 3 subfamily.
Mass spectrometry	Molecular mass is 8370.0 Da from positions 20 - 95. Determined by ESI. Ref.2 Molecular mass is 8370.0 Da from positions 20 - 95. Determined by MALDI. Ref.3 Molecular mass is 5294.95 Da from positions 48 - 95. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Cytolysis
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Fungicide Ion channel impairing toxin Potassium channel inhibitor Toxin
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW killing of cells of other organism 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
	Signal peptide	1 – 19	19	Ref.2 Ref.3
	Chain	20 – 95	76	Hge-scorpine		PRO_0000274682
	Chain	48 – 95	48	Hge36		PRO_0000356887
Amino acid modifications
	Disulfide bond	58 ↔ 81		By similarity
	Disulfide bond	68 ↔ 86		By similarity
	Disulfide bond	72 ↔ 88		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0GY40 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: EA797C1F58CF6C3C	FASTA	95	10,412
	10 20 30 40 50 60 MNTKLTVLCF LGIVTIVSCG WMSEKKVQGI LDKKLPEGII RNAAKAIVHK MAKNQFGCFA 70 80 90 NVDVKGDCKR HCKAEDKEGI CHGTKCKCGV PISYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones)." Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D. BMC Genomics 8:119-119(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Venom gland.
[2]	"Wide phylogenetic distribution of scorpine and long-chain beta-KTx-like peptides in scorpion venoms: identification of 'orphan' components." Diego-Garcia E., Schwartz E.F., D'Suze G., Gonzalez S.A., Batista C.V., Garcia B.I., Rodriguez de la Vega R.C., Possani L.D. Peptides 28:31-37(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-64, MASS SPECTROMETRY. Tissue: Venom and Venom gland.
[3]	"Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like peptides purified from scorpion venoms." Diego-Garcia E., Abdel-Mottaleb Y., Schwartz E.F., Rodriguez de la Vega R.C., Tytgat J., Possani L.D. Cell. Mol. Life Sci. 65:187-200(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-64, MASS SPECTROMETRY, FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ465351 mRNA. Translation: ABE98267.1. EF613116 Genomic DNA. Translation: ABU94956.1. EL698908 mRNA. No translation available.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

KBX3_HADGE

Accession

Primary (citable) accession number: Q0GY40
Secondary accession number(s): A8SDT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	October 3, 2006
Last modified:	March 6, 2013
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program