ID   TXC1B_CUPSA             Reviewed;          35 AA.
AC   P83620;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Cupiennin-1b {ECO:0000303|PubMed:11792701};
DE            Short=Cu-1b {ECO:0000305};
DE   AltName: Full=M-ctenitoxin-Cs1b;
DE            Short=M-CNTX-Cs1b;
OS   Cupiennius salei (American wandering spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Cupiennius.
OX   NCBI_TaxID=6928 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, TOXIC DOSE, AND AMIDATION AT
RP   GLU-35.
RC   TISSUE=Venom;
RX   PubMed=11792701; DOI=10.1074/jbc.m111099200;
RA   Kuhn-Nentwig L., Mueller J., Schaller J., Walz A., Dathe M., Nentwig W.;
RT   "Cupiennin 1, a new family of highly basic antimicrobial peptides in the
RT   venom of the spider Cupiennius salei (Ctenidae).";
RL   J. Biol. Chem. 277:11208-11216(2002).
CC   -!- FUNCTION: Has antimicrobial activity against E.coli, E.faecalis,
CC       P.aeruginosa, and S.aureus. Has insecticidal and hemolytic activities.
CC       Probably acts by disturbing membrane function with its amphipathic
CC       structure. {ECO:0000269|PubMed:11792701, ECO:0000303|PubMed:11792701}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3800.25; Mass_error=0.28; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11792701};
CC   -!- TOXIC DOSE: LD(50) is 4.7 pmol/mg on Drosophila.
CC       {ECO:0000269|PubMed:11792701}.
CC   -!- SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 01
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P83620; -.
DR   ArachnoServer; AS000290; M-ctenitoxin-Cs1b.
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   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR035164; Cupiennin.
DR   Pfam; PF17563; Cu; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..35
FT                   /note="Cupiennin-1b"
FT                   /id="PRO_0000045039"
FT   MOD_RES         35
FT                   /note="Glutamic acid 1-amide"
FT                   /evidence="ECO:0000269|PubMed:11792701"
SQ   SEQUENCE   35 AA;  3802 MW;  AE1660038BA72A04 CRC64;
     GFGSLFKFLA KKVAKTVAKQ AAKQGAKYIA NKQME