ID   I1BA_CONAE              Reviewed;          75 AA.
AC   P0C607;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Conotoxin ar11a;
DE   AltName: Full=Ar11.1;
DE   Flags: Precursor;
OS   Conus arenatus (Sand-dusted cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=89451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-75, SYNTHESIS OF
RP   [L-LEU-37]AR11A AND [D-LEU-37]AR11A, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=17996262; DOI=10.1016/j.toxicon.2007.09.006;
RA   Buczek O., Jimenez E.C., Yoshikami D., Imperial J.S., Watkins M.,
RA   Morrison A., Olivera B.M.;
RT   "I(1)-superfamily conotoxins and prediction of single D-amino acid
RT   occurrence.";
RL   Toxicon 51:218-229(2008).
CC   -!- FUNCTION: Both natural (L-Leu form) and synthetic (D-Leu from) peptides
CC       equally cause sensitivity to touch and body tremor. Neither L-Leu form
CC       nor D-Leu form is active on nerve-muscle preparation.
CC       {ECO:0000269|PubMed:17996262}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17996262}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000269|PubMed:17996262}.
CC   -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C).
CC   -!- MASS SPECTROMETRY: Mass=4533; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17996262};
CC   -!- SIMILARITY: Belongs to the conotoxin I1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C607; -.
DR   SMR; P0C607; -.
DR   ConoServer; 2801; ArXIA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   PROSITE; PS60019; I_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..36
FT                   /evidence="ECO:0000269|PubMed:17996262"
FT                   /id="PRO_0000314082"
FT   CHAIN           37..75
FT                   /note="Conotoxin ar11a"
FT                   /id="PRO_0000314083"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        52..63
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT   DISULFID        57..70
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ   SEQUENCE   75 AA;  8377 MW;  93AD875E576F8EB4 CRC64;
     MKLCATFLLV LVTLPLVTGE KSSERSLSGA ILRGVRRTCS RRGHRCIRDS QCCGGMCCQG
     NRCFVAIRRC FHLPF