ID   INS1_CONFO              Reviewed;         128 AA.
AC   A0A0B5AC98;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Con-Ins F1 {ECO:0000303|PubMed:25605914};
DE   AltName: Full=Insulin 1 {ECO:0000312|EMBL:AJD85837.1};
DE   Contains:
DE     RecName: Full=Con-Ins F1 B chain {ECO:0000303|PubMed:25605914};
DE   Contains:
DE     RecName: Full=Con-Ins F1 A chain {ECO:0000303|PubMed:25605914};
DE   Flags: Precursor;
OS   Conus floridulus (Cone snail) (Lividoconus floridulus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX   NCBI_TaxID=97180;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT SER-127.
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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KP268605; AJD85837.1; -; mRNA.
DR   AlphaFoldDB; A0A0B5AC98; -.
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   1: Evidence at protein level;
KW   Amidation; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Glucose metabolism; Hormone;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         25..58
FT                   /note="Con-Ins F1 B chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_5002098284"
FT   PROPEP          59..89
FT                   /note="C peptide"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_0000439332"
FT   PEPTIDE         90..127
FT                   /note="Con-Ins F1 A chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_0000439333"
FT   MOD_RES         115
FT                   /note="4-carboxyglutamate; partial"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   MOD_RES         127
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000305|PubMed:25605914"
FT   DISULFID        29..104
FT                   /evidence="ECO:0000305"
FT   DISULFID        41..107
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        53..120
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        106..111
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
SQ   SEQUENCE   128 AA;  13900 MW;  36DD950703DC141F CRC64;
     MTTSSYFLLV TLGLLLYVCR SSFGTEHTCE SDASPHPQGV CGSPLAEAVE AACELEEYLQ
     GGTGKKRGRA SPLRKRRAFL SMLKARAKRN EASPLQRSGR GIVCECCKNH CNIEELTEYC
     PPVTEGSG