ID   H71_CONVC               Reviewed;          80 AA.
AC   W4VSB6;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Conotoxin Vc7.1 {ECO:0000305};
DE   AltName: Full=H_Vc7.1 {ECO:0000312|EMBL:JAB84707.1};
DE   Flags: Precursor;
OS   Conus victoriae (Queen Victoria cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=319920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=24505301; DOI=10.1371/journal.pone.0087648;
RA   Robinson S.D., Safavi-Hemami H., McIntosh L.D., Purcell A.W., Norton R.S.,
RA   Papenfuss A.T.;
RT   "Diversity of conotoxin gene superfamilies in the venomous snail, Conus
RT   victoriae.";
RL   PLoS ONE 9:E87648-E87648(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=25464369; DOI=10.1016/j.jprot.2014.11.003;
RA   Robinson S.D., Safavi-Hemami H., Raghuraman S., Imperial J.S.,
RA   Papenfuss A.T., Teichert R.W., Purcell A.W., Olivera B.M., Norton R.S.;
RT   "Discovery by proteogenomics and characterization of an RF-amide
RT   neuropeptide from cone snail venom.";
RL   J. Proteomics 114:38-47(2015).
CC   -!- FUNCTION: Probable toxin with unknown function (Probable).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25464369}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:25464369}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- DOMAIN: Displays a mini-granulin fold, a structure composed of two
CC       short, stacked beta-hairpins connected by two parallel disulfide bonds.
CC       This newly described fold is derived from the same cysteine
CC       connectivity as knottins (ICK fold). The name 'mini-granulin fold'
CC       comes from the structural homology with the N-terminal region of the
CC       human granulin. {ECO:0000250|UniProtKB:W4VS16}.
CC   -!- SIMILARITY: Belongs to the conotoxin H superfamily.
CC       {ECO:0000305|PubMed:25464369}.
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DR   EMBL; GAIH01000010; JAB84707.1; -; mRNA.
DR   AlphaFoldDB; W4VSB6; -.
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   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439426"
FT   PEPTIDE         50..80
FT                   /note="Conotoxin Vc7.1"
FT                   /id="PRO_5004850817"
FT   DISULFID        55..65
FT                   /evidence="ECO:0000250|UniProtKB:W4VS16"
FT   DISULFID        60..74
FT                   /evidence="ECO:0000250|UniProtKB:W4VS16"
FT   DISULFID        64..79
FT                   /evidence="ECO:0000250|UniProtKB:W4VS16"
SQ   SEQUENCE   80 AA;  8603 MW;  BCD6C7970F192DB2 CRC64;
     MNTAGRLLLL CLALGLVFES LGIPVADDVE AVRDTDPDEK DPSVHNSLKA VYGDCGGERC
     RFGCCKTDDG EEKCQHFGCP