ID   O27A_CONRA              Reviewed;          38 AA.
AC   P0C1M8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Conotoxin r7a;
DE   AltName: Full=Light sleeper;
DE   Flags: Precursor; Fragment;
OS   Conus radiatus (Rayed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX   NCBI_TaxID=61198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-38, FUNCTION, MASS
RP   SPECTROMETRY, BROMINATION AT TRP-6; TRP-15 AND TRP-38, AND
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-10; GLU-11; GLU-20 AND GLU-31.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=15379573; DOI=10.1021/bi0489412;
RA   Jimenez E.C., Watkins M., Olivera B.M.;
RT   "Multiple 6-bromotryptophan residues in a sleep-inducing peptide.";
RL   Biochemistry 43:12343-12348(2004).
CC   -!- FUNCTION: Induces a sleep-like state in mice.
CC       {ECO:0000269|PubMed:15379573}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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   -!- MASS SPECTROMETRY: Mass=4203.61; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15379573};
CC   -!- MISCELLANEOUS: Equilibrates slowly between two distinct conformers.
CC       These two conformational states are clearly interconvertible.
CC   -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1M8; -.
DR   SMR; P0C1M8; -.
DR   ConoServer; 1495; RVIIA precursor.
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   Bromination; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Knottin; Neurotoxin; Secreted;
KW   Toxin.
FT   PROPEP          <1..5
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT                   /id="PRO_0000246035"
FT   PEPTIDE         6..38
FT                   /note="Conotoxin r7a"
FT                   /id="PRO_0000246036"
FT   MOD_RES         6
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         10
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         11
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         15
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         20
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         31
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   MOD_RES         38
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:15379573"
FT   DISULFID        12..26
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..30
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..35
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   38 AA;  4317 MW;  F1F5CA48136141F7 CRC64;
     APAKRWFGHE ECTYWLGPCE VDDTCCSASC ESKFCGLW