ID   O16H_CONAB              Reviewed;          74 AA.
AC   Q9UA95;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Conotoxin AbVIH;
DE   Flags: Precursor; Fragment;
OS   Conus abbreviatus (Abbreviated cone) (Miliariconus abbreviatus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virroconus.
OX   NCBI_TaxID=100123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=10359796; DOI=10.1073/pnas.96.12.6820;
RA   Duda T.F. Jr., Palumbi S.R.;
RT   "Molecular genetics of ecological diversification: duplication and rapid
RT   evolution of toxin genes of the venomous gastropod Conus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6820-6823(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=15306367; DOI=10.1098/rspb.2004.2708;
RA   Duda T.F. Jr., Palumbi S.R.;
RT   "Gene expression and feeding ecology: evolution of piscivory in the
RT   venomous gastropod genus Conus.";
RL   Proc. R. Soc. B 271:1165-1174(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF089983; AAD48238.1; -; mRNA.
DR   AlphaFoldDB; Q9UA95; -.
DR   ConoServer; 960; ABVIH precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Knottin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          <1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..40
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000392124"
FT   PEPTIDE         43..74
FT                   /note="Conotoxin AbVIH"
FT                   /id="PRO_0000392125"
FT   REGION          19..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..68
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   74 AA;  8063 MW;  452051C6850ED548 CRC64;
     VLIIAVLFLT ACQLTTAETS SRGKQKHRAL RSTDKDSRMT KRCTPAGDAC DATTKCCIPF
     CNLATKKCQV PTFP