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. 2015 Apr 6;112(16):5087–5092. doi: 10.1073/pnas.1424435112

Table 1.

Comparison of δ-conotoxin sequences from various cone snail species

Species type Clade Conus species δ-Conotoxin (ref.) Amino acid sequence
Worm-hunting * * * ** *
Tesseliconus C. tessulatus TsVIA CAAFGSFCGL-PGLVDCCSGRCFIVCLL
C. eburneus ErVIA CAGIGSFCGL-PGLVDCCSGRCFIVCLP
Fish-hunting * * ** ** *
Chelyconus C. purpurascens PVIA (33) EACYAOGTFCGIKOGL- -CCSEFCLPGVCFG#
C. ermineus EVIA (35) EACYPOGTFCGIKOGL- -CCSELCLPAVCVG#
Pionoconus C. striatus SVIE (44) DGCSSGGTFCGIHOGL- -CCSEFCFLWCITFID
C. magus MVIA (34) DGCYNAGTFCGIROGL- -CCSEFCFLWCITFVDS#
C. consors CnVIA (34) YECYSTGTFCGINGGL- -CCSNLCLFFVCLTFS
C. aurisiacus AVIA (34) DGCSNAGAFCGIHOGL- -CCSEICIVWCT
Mollusc-hunting *
Cylinder C. textile TxVIA (31) WCKQSGEMCNLLDQN- -CCDGYCIVLVCT
C. gloriamaris GmVIA (45) VKPCRKEGQLCDPIFQN- -CCRGWNCVLFCV

The bold-font “C”s represent the cysteine amino acids that form the disulfide bonding framework of these delta conotoxin peptides. Asterisks represent conserved (non-Cys) amino acids within δ-conotoxins from fish-hunting cone snails. Underlining indicates conserved amino acids and conservative amino acid changes (similar biochemical properties) between worm hunters and fish hunters. All amino acid sequences were determined from peptides purified from venom, with the exceptions of MVIA and AVIA, which were determined by molecular cloning of the genes encoding these peptides. # indicates an amidated C terminus. O, hydroxyproline. Each dash is for alignment of conserved amino acids.