ID   TU91_GEMLI              Reviewed;          70 AA.
AC   P0DKT5;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Turripeptide Gli9.1;
DE   Flags: Precursor;
OS   Gemmula lisajoni (Gem-turris).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Turridae; Gemmula.
OX   NCBI_TaxID=439589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22954218; DOI=10.1111/j.1749-6632.2012.06603.x;
RA   Olivera B.M., Watkins M., Bandyopadhyay P., Imperial J.S.,
RA   de la Cotera E.P., Aguilar M.B., Vera E.L., Concepcion G.P., Lluisma A.;
RT   "Adaptive radiation of venomous marine snail lineages and the accelerated
RT   evolution of venom peptide genes.";
RL   Ann. N. Y. Acad. Sci. 1267:61-70(2012).
CC   -!- FUNCTION: Acts as a neurotoxin by inhibiting an ion channel (By
CC       similarity). May also act as a serine protease inhibitor, since it
CC       possess the kazal serine protease inhibitor signature. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is IX (C-C-C-C-C-C).
CC   -!- SIMILARITY: Belongs to the conopeptide P-like superfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DKT5; -.
DR   SMR; P0DKT5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   Pfam; PF00050; Kazal_1; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..70
FT                   /note="Turripeptide Gli9.1"
FT                   /id="PRO_0000420719"
FT   DOMAIN          21..70
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   SITE            32..33
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        26..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        30..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        38..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   70 AA;  7783 MW;  78A4F62A092298A5 CRC64;
     MKVYCLLLVF LVGLVSQAHG RLDKRCMTVC TMEYWPVCGS DGKTYPNKCH LTSTACTSQK
     DITVLHVGKC