TXC1A_CUPSA
ID TXC1A_CUPSA Reviewed; 35 AA.
AC P83619;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Cupiennin-1a {ECO:0000303|PubMed:11792701};
DE Short=Cu-1a {ECO:0000305};
DE AltName: Full=M-ctenitoxin-Cs1a;
DE Short=M-CNTX-Cs1a;
OS Cupiennius salei (American wandering spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Cupiennius.
OX NCBI_TaxID=6928;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, TOXIC DOSE, AND
RP AMIDATION AT 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).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10669026; DOI=10.1016/s0041-0101(99)00167-1;
RA Haeberli S., Kuhn-Nentwig L., Schaller J., Nentwig W.;
RT "Characterisation of antibacterial activity of peptides isolated from the
RT venom of the spider Cupiennius salei (Araneae: Ctenidae).";
RL Toxicon 38:373-380(2000).
RN [3]
RP FUNCTION IN SYNERGY WITH OTHER TOXINS.
RX PubMed=15914655; DOI=10.1242/jeb.01594;
RA Wullschleger B., Nentwig W., Kuhn-Nentwig L.;
RT "Spider venom: enhancement of venom efficacy mediated by different
RT synergistic strategies in Cupiennius salei.";
RL J. Exp. Biol. 208:2115-2121(2005).
RN [4]
RP FUNCTION.
RX PubMed=17313650; DOI=10.1111/j.1742-4658.2007.05726.x;
RA Pukala T.L., Doyle J.R., Llewellyn L.E., Kuhn-Nentwig L., Apponyi M.A.,
RA Separovic F., Bowie J.H.;
RT "Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical
RT wandering spider Cupiennius salei, also inhibits the formation of nitric
RT oxide by neuronal nitric oxide synthase.";
RL FEBS J. 274:1778-1784(2007).
RN [5]
RP STRUCTURE BY NMR, AND AMIDATION AT GLU-35.
RX PubMed=17319697; DOI=10.1021/bi062306+;
RA Pukala T.L., Boland M.P., Gehman J.D., Kuhn-Nentwig L., Separovic F.,
RA Bowie J.H.;
RT "Solution structure and interaction of cupiennin 1a, a spider venom
RT peptide, with phospholipid bilayers.";
RL Biochemistry 46:3576-3585(2007).
CC -!- FUNCTION: Has antimicrobial activity against B.subtilis, E.coli,
CC E.faecalis, P.denitrificans, P.aeruginosa, P.putida, S.aureus, and
CC S.epidermidis. Shows insecticidal and hemolytic activities. Probably
CC acts by disturbing membrane function with its amphipathic structure.
CC Synergistically increases the insecticidal activity of CSTX-1 (AC
CC P81694), CSTX-9 (AC P58604), and CSTX-13 (AC P83919) by up to 65%
CC (PubMed:15914655). Also inhibits the formation of nitric oxide by
CC neuronal nitric oxide synthase. {ECO:0000269|PubMed:10669026,
CC ECO:0000269|PubMed:11792701, ECO:0000269|PubMed:15914655,
CC ECO:0000269|PubMed:17313650}.
CC -!- SUBUNIT: Monomer (Probable). Interacts with CSTX-1 (AC P81694), CSTX-9
CC (AC P58604), and CSTX-13 (AC P83919) (PubMed:15914655).
CC {ECO:0000269|PubMed:15914655, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10669026}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10669026}.
CC -!- MASS SPECTROMETRY: Mass=3798.63; Mass_error=0.51; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11792701};
CC -!- MASS SPECTROMETRY: Mass=3798.03; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10669026};
CC -!- TOXIC DOSE: LD(50) is 5.9 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 PDB; 2K38; NMR; -; A=1-35.
DR PDBsum; 2K38; -.
DR AlphaFoldDB; P83619; -.
DR BMRB; P83619; -.
DR SMR; P83619; -.
DR ArachnoServer; AS000289; M-ctenitoxin-Cs1a.
DR EvolutionaryTrace; P83619; -.
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 3D-structure; Amidation; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Hemolysis; Neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..35
FT /note="Cupiennin-1a"
FT /evidence="ECO:0000269|PubMed:11792701"
FT /id="PRO_0000045038"
FT MOD_RES 35
FT /note="Glutamic acid 1-amide"
FT /evidence="ECO:0000269|PubMed:11792701,
FT ECO:0000269|PubMed:17319697"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:2K38"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:2K38"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:2K38"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2K38"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:2K38"
FT TURN 28..34
FT /evidence="ECO:0007829|PDB:2K38"
SQ SEQUENCE 35 AA; 3800 MW; 998800038BB82887 CRC64;
GFGALFKFLA KKVAKTVAKQ AAKQGAKYVV NKQME
