ID   CT5A_CONPU              Reviewed;          63 AA.
AC   Q9U6Z6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Conotoxin p5a {ECO:0000303|PubMed:10521453};
DE   AltName: Full=P5.1 {ECO:0000303|PubMed:10521453};
DE   AltName: Full=PVA {ECO:0000305};
DE   Flags: Precursor;
OS   Conus purpurascens (Purple cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX   NCBI_TaxID=41690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-62, MASS SPECTROMETRY,
RP   AMIDATION AT LEU-62, SYNTHESIS OF 51-62, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=10521453; DOI=10.1074/jbc.274.43.30664;
RA   Walker C.S., Steel D., Jacobsen R.B., Lirazan M.B., Cruz L.J., Hooper D.,
RA   Shetty R., DelaCruz R.C., Nielsen J.S., Zhou L.M., Bandyopadhyay P.,
RA   Craig A.G., Olivera B.M.;
RT   "The T-superfamily of conotoxins.";
RL   J. Biol. Chem. 274:30664-30671(1999).
RN   [2]
RP   ERRATUM OF PUBMED:10521453.
RA   Walker C.S., Steel D., Jacobsen R.B., Lirazan M.B., Cruz L.J., Hooper D.,
RA   Shetty R., DelaCruz R.C., Nielsen J.S., Zhou L.M., Bandyopadhyay P.,
RA   Craig A.G., Olivera B.M.;
RL   J. Biol. Chem. 274:36030-36030(1999).
CC   -!- FUNCTION: In vivo, low levels of the peptide injected into male
CC       specimens of the Siamese fighting fish causes an immediate aggressive
CC       display in this fish in response to their reflection when placed in a
CC       mirrored aquarium; High levels of the peptide suppressed this behavior.
CC       No effect is observed when injected into mice.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10521453}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:10521453}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1337.5; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:10521453};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; AF167168; AAF03688.1; -; mRNA.
DR   PIR; F59147; F59147.
DR   AlphaFoldDB; Q9U6Z6; -.
DR   PRIDE; Q9U6Z6; -.
DR   ConoServer; 1733; PVA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000269|PubMed:10521453"
FT                   /id="PRO_0000035019"
FT   PEPTIDE         51..62
FT                   /note="Conotoxin p5a"
FT                   /evidence="ECO:0000269|PubMed:10521453"
FT                   /id="PRO_0000035020"
FT   MOD_RES         62
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:10521453"
FT   DISULFID        52..59
FT                   /evidence="ECO:0000269|PubMed:10521453"
FT   DISULFID        53..60
FT                   /evidence="ECO:0000269|PubMed:10521453"
SQ   SEQUENCE   63 AA;  7102 MW;  82A28478C13D7EA9 CRC64;
     MRCLPVFVIL LLLIPSAPCV DAHPKTKDDM PLASFHDNAK GTLQRFWKKR GCCPKQMRCC
     TLG