ID   O16A_CONST              Reviewed;          72 AA.
AC   P28880; Q9UB26;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Omega-conotoxin SVIA {ECO:0000303|PubMed:1390774};
DE   AltName: Full=SNX-157 {ECO:0000303|PubMed:1390774};
DE   Flags: Precursor;
OS   Conus striatus (Striated cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=10573284; DOI=10.1016/s0196-9781(99)00116-3;
RA   Lu B.-S., Yu F., Zhao D., Huang P.-T., Huang C.-F.;
RT   "Conopeptides from Conus striatus and Conus textile by cDNA cloning.";
RL   Peptides 20:1139-1144(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 49-72, FUNCTION, SYNTHESIS OF 49-72, HYDROXYLATION AT
RP   PRO-55, AMIDATION AT THR-72, SUBCELLULAR LOCATION, AND TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=1390774; DOI=10.1021/bi00156a009;
RA   Ramilo C., Zafaralla G.C., Nadasdi L., Hammerland L.G., Yoshikami D.,
RA   Gray W.R., Kristipati R., Ramachandran J., Miljanich G.P., Olivera B.M.,
RA   Cruz L.J.;
RT   "Novel alpha- and omega-conotoxins from Conus striatus venom.";
RL   Biochemistry 31:9919-9926(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-72, AND VARIANTS PRO-51; PRO-54; SER-55;
RP   ALA-59 AND SER-67.
RC   TISSUE=Venom duct;
RX   PubMed=16183187; DOI=10.1016/j.biochi.2005.08.001;
RA   Pi C., Liu Y., Peng C., Jiang X., Liu J., Xu B., Yu X., Yu Y., Jiang X.,
RA   Wang L., Dong M., Chen S., Xu A.-L.;
RT   "Analysis of expressed sequence tags from the venom ducts of Conus
RT   striatus: focusing on the expression profile of conotoxins.";
RL   Biochimie 88:131-140(2006).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). In vivo, this toxin is a
CC       potent paralytic toxic in lower vertebrate species, but it is much less
CC       effective in mammals. {ECO:0000269|PubMed:1390774}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1390774}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:1390774}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P28881}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- TOXIC DOSE: On fish, this toxin causes paralysis and death on
CC       intramuscular injection at doses of approximately 20 pmol/g. It does
CC       not kill mice even at extremely high doses.
CC       {ECO:0000269|PubMed:1390774}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
CC   -!- CAUTION: Thr-72 is not followed in the nucleotide sequence by the
CC       expected Gly residue required to produce amidation. {ECO:0000305}.
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DR   EMBL; AF146347; AAD31907.1; -; mRNA.
DR   PIR; B44379; B44379.
DR   AlphaFoldDB; P28880; -.
DR   SMR; P28880; -.
DR   ConoServer; 863; SVIA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..48
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000034924"
FT   PEPTIDE         49..72
FT                   /note="Omega-conotoxin SVIA"
FT                   /evidence="ECO:0000269|PubMed:1390774"
FT                   /id="PRO_0000034925"
FT   REGION          25..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:1390774"
FT   MOD_RES         72
FT                   /note="Threonine amide"
FT                   /evidence="ECO:0000269|PubMed:1390774"
FT   DISULFID        49..63
FT                   /evidence="ECO:0000250|UniProtKB:P28881"
FT   DISULFID        56..66
FT                   /evidence="ECO:0000250|UniProtKB:P28881"
FT   DISULFID        62..71
FT                   /evidence="ECO:0000250|UniProtKB:P28881"
FT   VARIANT         51
FT                   /note="S -> P (in SVIA-1, SVIA-2 and SVIA-5)"
FT                   /evidence="ECO:0000269|PubMed:16183187"
FT   VARIANT         54
FT                   /note="S -> P (in SVIA-4)"
FT                   /evidence="ECO:0000269|PubMed:16183187"
FT   VARIANT         55
FT                   /note="P -> S (in SVIA-3)"
FT                   /evidence="ECO:0000269|PubMed:16183187"
FT   VARIANT         59
FT                   /note="T -> A (in SVIA-5)"
FT                   /evidence="ECO:0000269|PubMed:16183187"
FT   VARIANT         67
FT                   /note="Y -> S (in SVIA-2 and SVIA-5)"
FT                   /evidence="ECO:0000269|PubMed:16183187"
SQ   SEQUENCE   72 AA;  7830 MW;  4A6A412E450469A1 CRC64;
     MKLTCVMIVA VLLLTACQLI TAEDSRGTQK HRTLRSTARR SKSESTTRCR SSGSPCGVTS
     ICCGRCYRGK CT