ID   O16B_CONER              Reviewed;          29 AA.
AC   P69752;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Delta-conotoxin-like EVIB;
DE            Short=Delta-EVIB;
DE   AltName: Full=Delta-EVIA;
OS   Conus ermineus (Agate cone) (Chelyconus ermineus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX   NCBI_TaxID=55423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND HYDROXYLATION AT PRO-5.
RC   TISSUE=Venom duct;
RX   PubMed=11683628; DOI=10.1021/bi010683a;
RA   Bulaj G., DeLaCruz R., Azimi-Zonooz A., West P., Watkins M., Yoshikami D.,
RA   Olivera B.M.;
RT   "Delta-conotoxin structure/function through a cladistic analysis.";
RL   Biochemistry 40:13201-13208(2001).
CC   -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC       channels (Nav) and inhibit the inactivation process. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
CC   -!- CAUTION: This toxin was originally named EVIA. As another delta-
CC       conotoxin was named EVIA in 2004 for which structural studies were
CC       carried out, the present toxin was renamed here EVIB. {ECO:0000305}.
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DR   AlphaFoldDB; P69752; -.
DR   ConoServer; 1575; EVIB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012322; Conotoxin_d-typ_CS.
DR   PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Disulfide bond; Hydroxylation; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..29
FT                   /note="Delta-conotoxin-like EVIB"
FT                   /id="PRO_0000044471"
FT   MOD_RES         5
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:11683628"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         14
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         29
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..27
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   29 AA;  2932 MW;  8F51A4CFA5E80C87 CRC64;
     EACYPPGTFC GIKPGLCCSE LCLPAVCVG