TU92_IOTCI
ID TU92_IOTCI Reviewed; 70 AA.
AC P0DKT4;
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 Ici9.2;
DE Flags: Precursor;
OS Iotyrris cingulifera (Sea snail) (Pleurotoma cingulifera).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Turridae; Iotyrris.
OX NCBI_TaxID=553733;
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; P0DKT4; -.
DR SMR; P0DKT4; -.
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 InterPro; IPR001239; Prot_inh_Kazal-m.
DR Pfam; PF00050; Kazal_1; 1.
DR PRINTS; PR00290; KAZALINHBTR.
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 Ici9.2"
FT /id="PRO_0000420718"
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; 7621 MW; FEA2F77B5DE9A963 CRC64;
MKVYCLLLVL LVGLVSQAQG QLDKKCQTMC TMEYLPVCGS DGTTYPNKCT LTSTACVNQM
DITVLHNGEC