KBX3_PANIM
ID KBX3_PANIM Reviewed; 94 AA.
AC P56972;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Scorpine;
DE Short=Scorpin;
DE AltName: Full=Panscorpine;
DE Flags: Precursor;
OS Pandinus imperator (Emperor scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX NCBI_TaxID=55084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-94, CHARACTERIZATION,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10767415; DOI=10.1016/s0014-5793(00)01384-3;
RA Conde R., Zamudio F.Z., Rodriguez M.H., Possani L.D.;
RT "Scorpine, an anti-malaria and anti-bacterial agent purified from scorpion
RT venom.";
RL FEBS Lett. 471:165-168(2000).
CC -!- FUNCTION: Has antibacterial activity against B.subtilis and
CC K.pneumoniae and a potent inhibitory effect on the ookinete (ED(50) 0.7
CC uM) and gamete (ED(50) 10 uM) stages of Plasmodium berghei development.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=8350; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10767415};
CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ292361; CAB96789.1; -; mRNA.
DR PDB; 7M1D; NMR; -; A=48-94.
DR PDB; 7M1E; NMR; -; A=20-47.
DR PDBsum; 7M1D; -.
DR PDBsum; 7M1E; -.
DR AlphaFoldDB; P56972; -.
DR SMR; P56972; -.
DR TCDB; 1.C.47.3.1; the insect/fungal defensin (insect/fungal defensin) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; 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; Direct protein sequencing;
KW Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:10767415"
FT CHAIN 20..94
FT /note="Scorpine"
FT /id="PRO_0000035355"
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 DISULFID 68..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:7M1E"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:7M1E"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:7M1E"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:7M1D"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:7M1D"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:7M1D"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7M1D"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7M1D"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7M1D"
SQ SEQUENCE 94 AA; 10394 MW; 04E57F04BAECC89F CRC64;
MNSKLTALIF LGLIAIAYCG WINEEKIQKK IDERMGNTVL GGMAKAIVHK MAKNEFQCMA
NMDMLGNCEK HCQTSGEKGY CHGTKCKCGT PLSY