CTA11_CONAO
ID CTA11_CONAO Reviewed; 11 AA.
AC P0CI23;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 22-APR-2020, entry version 19.
DE RecName: Full=Chi-conotoxin-like Ar1311;
OS Conus araneosus (Cobweb cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX NCBI_TaxID=101286;
RN [1]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS,
RP HYDROXYLATION AT PRO-10, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=20843009; DOI=10.1021/ac101867e;
RA Gupta K., Kumar M., Balaram P.;
RT "Disulfide bond assignments by mass spectrometry of native natural
RT peptides: cysteine pairing in disulfide bonded conotoxins.";
RL Anal. Chem. 82:8313-8319(2010).
CC -!- FUNCTION: Chi-conotoxins inhibit the neuronal noradrenaline transporter
CC (NET/SLC6A2). {ECO:0000250|UniProtKB:P58808}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20843009}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:20843009}.
CC -!- DOMAIN: The cysteine framework is X (CC-CX[hydroxyPro]C).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydroxylation; Neurotoxin;
KW Secreted; Toxin.
FT PEPTIDE 1..11
FT /note="Chi-conotoxin-like Ar1311"
FT /evidence="ECO:0000269|PubMed:20843009"
FT /id="PRO_0000402419"
FT MOD_RES 10
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:20843009"
FT DISULFID 2..11
FT /evidence="ECO:0000269|PubMed:20843009"
FT DISULFID 3..8
FT /evidence="ECO:0000269|PubMed:20843009"
SQ SEQUENCE 11 AA; 1301 MW; 277AA974B6932B58 CRC64;
RCCGYKMCHP C