ID   H72_CONVC               Reviewed;          74 AA.
AC   W4VS16;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Conotoxin Vc7.2 {ECO:0000305};
DE   AltName: Full=H-Vc7.2 {ECO:0000303|PubMed:25464369, ECO:0000303|PubMed:30975904};
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 duct;
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 duct;
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).
RN   [3]
RP   STRUCTURE BY NMR OF 50-74, PROTEIN SEQUENCE OF 50-74, FUNCTION, DISULFIDE
RP   BOND, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=30975904; DOI=10.1074/jbc.ra119.007491;
RA   Nielsen L.D., Foged M.M., Albert A., Bertelsen A.B., Soeltoft C.L.,
RA   Robinson S.D., Petersen S.V., Purcell A.W., Olivera B.M., Norton R.S.,
RA   Vasskog T., Safavi-Hemami H., Teilum K., Ellgaard L.;
RT   "The three-dimensional structure of an H-superfamily conotoxin reveals a
RT   granulin fold arising from a common ICK cysteine framework.";
RL   J. Biol. Chem. 294:8745-8759(2019).
CC   -!- FUNCTION: Probable toxin with unknown function (Probable). Does not
CC       produce any changes in intracellular calcium levels in mouse dorsal
CC       root ganglion cells (PubMed:30975904). In vivo, does not produce
CC       behavioral changes when intracranially injected into mice
CC       (PubMed:30975904). {ECO:0000269|PubMed:30975904}.
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:0000305|PubMed:30975904}.
CC   -!- MASS SPECTROMETRY: Mass=2785.15; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:30975904};
CC   -!- SIMILARITY: Belongs to the conotoxin H superfamily.
CC       {ECO:0000305|PubMed:25464369}.
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DR   EMBL; GAIH01000011; JAB84706.1; -; mRNA.
DR   PDB; 6Q5Z; NMR; -; A=50-74.
DR   PDBsum; 6Q5Z; -.
DR   AlphaFoldDB; W4VS16; -.
DR   BMRB; W4VS16; -.
DR   SMR; W4VS16; -.
DR   TCDB; 8.B.37.1.1; the conotoxin-teretoxin (c-t) family.
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   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:30975904"
FT                   /id="PRO_0000439427"
FT   PEPTIDE         50..74
FT                   /note="Conotoxin Vc7.2"
FT                   /evidence="ECO:0000269|PubMed:30975904"
FT                   /id="PRO_5004850996"
FT   DISULFID        53..63
FT                   /evidence="ECO:0000269|PubMed:30975904,
FT                   ECO:0007744|PDB:6Q5Z"
FT   DISULFID        58..68
FT                   /evidence="ECO:0000269|PubMed:30975904,
FT                   ECO:0007744|PDB:6Q5Z"
FT   DISULFID        62..73
FT                   /evidence="ECO:0000269|PubMed:30975904,
FT                   ECO:0007744|PDB:6Q5Z"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:6Q5Z"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:6Q5Z"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:6Q5Z"
SQ   SEQUENCE   74 AA;  8258 MW;  C3EF6CE505CB65D4 CRC64;
     MNTAGRLLLL CLVLGLVFES LGIPVADDLE ADRDTDPDEK DPSVHNYWRN VNCGGVPCKF
     GCCREDRCRE IDCD