ID   ACTP_CONCN              Reviewed;         248 AA.
AC   P0DKQ8; S6CRD8;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Conoporin-Cn1 {ECO:0000303|PubMed:22705119};
DE   Flags: Precursor;
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
CC   -!- FUNCTION: Pore-forming protein that forms pores of around 1 nm and
CC       causes cardiac stimulation and hemolysis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Target cell membrane {ECO:0000250}.
CC       Note=Forms an alpha-helical membrane channel in the prey.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- PTM: 9 isoforms are detected in the injectable venom, mainly
CC       corresponding to different oxidative states.
CC   -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- MISCELLANEOUS: The mature peptide contains 1 cysteine residue.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the actinoporin family. Conoidea subfamily.
CC       {ECO:0000305}.
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DR   EMBL; HE856388; CCI55501.1; -; mRNA.
DR   AlphaFoldDB; P0DKQ8; -.
DR   ConoServer; 5534; Conoporin-Cn1 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.270.20; -; 1.
DR   InterPro; IPR015926; Cytolysin/lectin.
DR   SUPFAM; SSF63724; SSF63724; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Hemolysis; Ion transport; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..248
FT                   /note="Conoporin-Cn1"
FT                   /id="PRO_0000419897"
SQ   SEQUENCE   248 AA;  27969 MW;  C6AF74F374DBE68E CRC64;
     MGVQFPALKT MVTVFLLLMG NMSPVVMKSS IPLRKVKMVA SKVVTPGSSL YGVALKDLAD
     TSYNITCTLQ VENWIRYRLI VPSVQMVYGV VTTTPIAIEP AKREAFAVRK TSDTASGVAG
     SVSWELEKAR RRFVIMWSVP DNFNSFGYWM GLGMTREGLV DPDKDWYGQM YSGSSDGDLT
     FTRKDFSYNT DSIIYSNDKF EVEGDMTNTQ HAQIKIVIRP SSNNWKDLAP KIRRKLKKKP
     KPARQRDN