M3A_CONQU
ID M3A_CONQU Reviewed; 15 AA.
AC P58841;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 1.
DT 22-APR-2020, entry version 48.
DE RecName: Full=Conotoxin QcIIIA;
OS Conus quercinus (Oak cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX NCBI_TaxID=101313;
RN [1]
RP PROTEIN SEQUENCE, HYDROXYLATION AT PRO-11, AND AMIDATION AT ASN-15.
RX PubMed=2165278; DOI=10.1126/science.2165278;
RA Olivera B.M., Rivier J., Clark C., Ramilo C.A., Corpuz G.P., Abogadie F.C.,
RA Mena E.E., Woodward S.R., Hillyard D.R., Cruz L.J.;
RT "Diversity of Conus neuropeptides.";
RL Science 249:257-263(1990).
CC -!- FUNCTION: Causes scratching in mice.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 2 branch, since 2 residues stand between the fourth and the fifth
CC cysteine residues.
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR ConoServer; 1514; QcIIIA.
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 Amidation; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..15
FT /note="Conotoxin QcIIIA"
FT /id="PRO_0000044501"
FT MOD_RES 11
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2165278"
FT MOD_RES 15
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:2165278"
FT DISULFID 1..13
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
FT DISULFID 2..9
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
FT DISULFID 6..12
FT /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ SEQUENCE 15 AA; 1601 MW; D479B5AEB4ED832D CRC64;
CCSQDCLVCI PCCPN