KBX3_HOFGE
ID KBX3_HOFGE Reviewed; 95 AA.
AC Q0GY40; A8SDT6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Hge-scorpine;
DE AltName: Full=Hg-scorpine-like 1;
DE Short=HgeScplp1;
DE Short=Hgscplike1;
DE Contains:
DE RecName: Full=Hge36 {ECO:0000303|PubMed:18030427};
DE Flags: Precursor;
OS Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Iuroidea; Hadrurus.
OX NCBI_TaxID=380989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=17506894; DOI=10.1186/1471-2164-8-119;
RA Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D.;
RT "Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus
RT gertschi (Arachnida: Scorpiones).";
RL BMC Genomics 8:119-119(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-64, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17141373; DOI=10.1016/j.peptides.2006.06.012;
RA Diego-Garcia E., Schwartz E.F., D'Suze G., Gonzalez S.A., Batista C.V.,
RA Garcia B.I., Rodriguez de la Vega R.C., Possani L.D.;
RT "Wide phylogenetic distribution of scorpine and long-chain beta-KTx-like
RT peptides in scorpion venoms: identification of 'orphan' components.";
RL Peptides 28:31-37(2007).
RN [3]
RP PROTEIN SEQUENCE OF 20-64, MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=18030427; DOI=10.1007/s00018-007-7370-x;
RA Diego-Garcia E., Abdel-Mottaleb Y., Schwartz E.F.,
RA Rodriguez de la Vega R.C., Tytgat J., Possani L.D.;
RT "Cytolytic and K+ channel blocking activities of beta-KTx and scorpine-like
RT peptides purified from scorpion venoms.";
RL Cell. Mol. Life Sci. 65:187-200(2008).
RN [4] {ECO:0007744|PDB:5IPO, ECO:0007744|PDB:5JYH}
RP STRUCTURE BY NMR OF 48-95, DISULFIDE BONDS, AND MUTAGENESIS OF
RP 1-MET--MET-51.
RX PubMed=27314815; DOI=10.1002/1873-3468.12255;
RA Flores-Solis D., Toledano Y., Rodriguez-Lima O., Cano-Sanchez P.,
RA Ramirez-Cordero B.E., Landa A., Rodriguez de la Vega R.C.,
RA Del Rio-Portilla F.;
RT "Solution structure and antiparasitic activity of scorpine-like peptides
RT from Hoffmannihadrurus gertschi.";
RL FEBS Lett. 590:2286-2296(2016).
CC -!- FUNCTION: [Hge-scorpine]: Has antibacterial activity against
CC B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic
CC activities. {ECO:0000269|PubMed:18030427}.
CC -!- FUNCTION: [Hge36]: Blocks Kv1.1/KCNA1 (IC(50)=185 nM) potassium
CC channels. Shows a weak hemolytic activity.
CC {ECO:0000269|PubMed:18030427, ECO:0000269|PubMed:27314815}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: [Hge-scorpine]: Mass=8370.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17141373};
CC -!- MASS SPECTROMETRY: [Hge-scorpine]: Mass=8370.0; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18030427};
CC -!- MASS SPECTROMETRY: [Hge36]: Mass=5294.95; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18030427};
CC -!- MISCELLANEOUS: The C-terminus (AA 52-95) blocks Kv1.1/KCNA1,
CC Kv1.2/KCNA2, and Kv1.3/KCNA2 potassium channels, showing a potential
CC important role of AA 48-51.
CC -!- MISCELLANEOUS: Hge36 peptide does not block Kv1.2/KCNA2 and
CC Kv1.3/KCNA3. {ECO:0000305|PubMed:18030427}.
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ465351; ABE98267.1; -; mRNA.
DR EMBL; EF613116; ABU94956.1; -; Genomic_DNA.
DR EMBL; EL698908; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 5IPO; NMR; -; A=48-95.
DR PDB; 5JYH; NMR; -; A=52-95.
DR PDBsum; 5IPO; -.
DR PDBsum; 5JYH; -.
DR AlphaFoldDB; Q0GY40; -.
DR SMR; Q0GY40; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR029237; Long_scorpion_toxin.
DR Pfam; PF14866; Toxin_38; 1.
DR PROSITE; PS51862; BSPN_CSAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Fungicide;
KW Ion channel impairing toxin; Potassium channel impairing toxin; Secreted;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:17141373,
FT ECO:0000269|PubMed:18030427"
FT CHAIN 20..95
FT /note="Hge-scorpine"
FT /evidence="ECO:0000269|PubMed:17141373,
FT ECO:0000269|PubMed:18030427"
FT /id="PRO_0000274682"
FT CHAIN 48..95
FT /note="Hge36"
FT /evidence="ECO:0000269|PubMed:17141373,
FT ECO:0000269|PubMed:18030427"
FT /id="PRO_0000356887"
FT DOMAIN 55..94
FT /note="BetaSPN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 58..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209,
FT ECO:0000269|PubMed:27314815, ECO:0007744|PDB:5IPO,
FT ECO:0007744|PDB:5JYH"
FT DISULFID 68..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209,
FT ECO:0000269|PubMed:27314815, ECO:0007744|PDB:5IPO,
FT ECO:0007744|PDB:5JYH"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209,
FT ECO:0000269|PubMed:27314815, ECO:0007744|PDB:5IPO,
FT ECO:0007744|PDB:5JYH"
FT MUTAGEN 1..51
FT /note="Missing: In HgeD; enhanced potassium channel-
FT blocking and antiparasitic activities."
FT /evidence="ECO:0000269|PubMed:27314815"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5IPO"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5IPO"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:5IPO"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5IPO"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5IPO"
SQ SEQUENCE 95 AA; 10412 MW; EA797C1F58CF6C3C CRC64;
MNTKLTVLCF LGIVTIVSCG WMSEKKVQGI LDKKLPEGII RNAAKAIVHK MAKNQFGCFA
NVDVKGDCKR HCKAEDKEGI CHGTKCKCGV PISYL
