ID   INS1_CONIM              Reviewed;         150 AA.
AC   A0A0B5A7M7;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Con-Ins Im1 {ECO:0000303|PubMed:25605914};
DE   AltName: Full=Insulin 1 {ECO:0000312|EMBL:AJD85819.1};
DE   Contains:
DE     RecName: Full=Con-Ins I1 B chain {ECO:0000303|PubMed:25605914};
DE   Contains:
DE     RecName: Full=Con-Ins I1 A chain {ECO:0000303|PubMed:25605914};
DE   Flags: Precursor;
OS   Conus imperialis (Imperial cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=35631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=25605914; DOI=10.1073/pnas.1423857112;
RA   Safavi-Hemami H., Gajewiak J., Karanth S., Robinson S.D., Ueberheide B.,
RA   Douglass A.D., Schlegel A., Imperial J.S., Watkins M., Bandyopadhyay P.K.,
RA   Yandell M., Li Q., Purcell A.W., Norton R.S., Ellgaard L., Olivera B.M.;
RT   "Specialized insulin is used for chemical warfare by fish-hunting cone
RT   snails.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:1743-1748(2015).
CC   -!- FUNCTION: This venom insulin facilitates prey capture by rapidly
CC       inducing hypoglycemic shock. Intraperitoneal injection of this peptide
CC       into zebrafish lowers blood glucose with the same potency than human
CC       insulin. In vivo, when applied to water, this peptide reduces overall
CC       locomotor activity of zebrafish larvae, observed as a significant
CC       decrease in the percentage of time spent swimming and movement
CC       frequency. {ECO:0000250|UniProtKB:A0A0B5AC95}.
CC   -!- SUBUNIT: Heterodimer of A and B chains; disulfide-linked.
CC       {ECO:0000250|UniProtKB:A0A0B5AC95}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0B5AC95}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25605914}.
CC   -!- SIMILARITY: Belongs to the insulin family.
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DR   EMBL; KP268603; AJD85819.1; -; mRNA.
DR   AlphaFoldDB; A0A0B5A7M7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR016724; Insulin-rel_pep.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PIRSF; PIRSF018431; Molluscan_insulin_rel_peptide; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Glucose metabolism; Hormone;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         26..63
FT                   /note="Con-Ins I1 B chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_5002112925"
FT   PROPEP          64..111
FT                   /note="C peptide"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_0000439322"
FT   PEPTIDE         112..150
FT                   /note="Con-Ins I1 A chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_0000439323"
FT   MOD_RES         144
FT                   /note="4-carboxyglutamate; partial"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        31..133
FT                   /evidence="ECO:0000305"
FT   DISULFID        46..136
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        58..149
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        135..140
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
SQ   SEQUENCE   150 AA;  16659 MW;  075FC0ED2606F6DD CRC64;
     MATSLLSPLL VAMLGFLLHV HVARAGLEHT CTLETRMQGA HPQGICGSKL PDIVHTVCQV
     MGRGYAGGQR QLRKRTSMID SDDMEAEGGS RGGFLMSKRR ALSYLQKETN PLVMAGYERR
     GIQKRHGEQG ITCECCYNHC SFRELVQYCN