M3B_CONBE
ID M3B_CONBE Reviewed; 15 AA.
AC P58624;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 22-APR-2020, entry version 50.
DE RecName: Full=BtIIIB {ECO:0000303|Ref.2};
DE AltName: Full=Conotoxin BeTXIb {ECO:0000303|PubMed:10591037};
OS Conus betulinus (Beech cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX NCBI_TaxID=89764;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=10591037;
RA Chen J.-S., Fan C.-X., Hu K.-P., Wei K.-H., Zhong M.-N.;
RT "Studies on conotoxins of Conus betulinus.";
RL J. Nat. Toxins 8:341-349(1999).
RN [2]
RP PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RA Zhao T.-Y., Cao Y., Dai X.-D., Fan C.-X., Chen J.-S.;
RT "Purification, sequence and disulfide bonding pattern of a novel conotoxin
RT BtIIIB.";
RL Acta Chim. Sin. 63:163-168(2005).
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 -!- MASS SPECTROMETRY: Mass=1642.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10591037};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR ConoServer; 1481; BeTXIb.
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; Neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..15
FT /note="BtIIIB"
FT /id="PRO_0000044500"
FT DISULFID 1..13
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 2..9
FT /evidence="ECO:0000269|Ref.2"
FT DISULFID 6..12
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 15 AA; 1650 MW; 3749B4F08E311337 CRC64;
CCELPCHGCV PCCWP