ID   INS_CONVC               Reviewed;         123 AA.
AC   A0A0F7YYV0;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Insulin-like peptide-1 {ECO:0000303|PubMed:26301480};
DE            Short=ILP-1 {ECO:0000303|PubMed:26301480};
DE   Contains:
DE     RecName: Full=ILP-1 B chain {ECO:0000303|PubMed:26301480};
DE   Contains:
DE     RecName: Full=ILP-1 A chain {ECO:0000303|PubMed:26301480};
DE   Flags: Precursor;
OS   Conus victoriae (Queen Victoria cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=319920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24505301; DOI=10.1371/journal.pone.0087648;
RA   Robinson S.D., Safavi-Hemami H., McIntosh L.D., Purcell A.W., Norton R.S.,
RA   Papenfuss A.T.;
RT   "Diversity of conotoxin gene superfamilies in the venomous snail, Conus
RT   victoriae.";
RL   PLoS ONE 9:E87648-E87648(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-110,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-107, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=26301480; DOI=10.1016/j.ygcen.2015.07.012;
RA   Robinson S.D., Li Q., Bandyopadhyay P.K., Gajewiak J., Yandell M.,
RA   Papenfuss A.T., Purcell A.W., Norton R.S., Safavi-Hemami H.;
RT   "Hormone-like peptides in the venoms of marine cone snails.";
RL   Gen. Comp. Endocrinol. 244:11-18(2017).
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:0000269|PubMed:26301480}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000269|PubMed:26301480}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; GAIH01000104; JAI08985.1; -; mRNA.
DR   AlphaFoldDB; A0A0F7YYV0; -.
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   Pfam; PF00049; Insulin; 1.
DR   PIRSF; PIRSF018431; Molluscan_insulin_rel_peptide; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW   Glucose metabolism; Hormone; Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         25..58
FT                   /note="ILP-1 B chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_5002525828"
FT   PROPEP          59..102
FT                   /note="C peptide"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT                   /id="PRO_0000439359"
FT   PEPTIDE         103..123
FT                   /note="ILP-1 A chain"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9,
FT                   ECO:0000269|PubMed:26301480"
FT                   /id="PRO_0000439360"
FT   MOD_RES         34
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   MOD_RES         107
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:26301480"
FT   MOD_RES         117
FT                   /note="4-carboxyglutamate; partial"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        29..106
FT                   /evidence="ECO:0000305"
FT   DISULFID        41..109
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        53..122
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT   DISULFID        108..113
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
SQ   SEQUENCE   123 AA;  13727 MW;  D9B6A80634FEA3CE CRC64;
     MTTSSYFLLV ALGLLLYVCQ SSFGGEHVCW LDDPNHPEGI CGPQVSDIVE IRCEEKEAEQ
     GGANNARAYT GRTSSLMKRR GFLSLLKKRG KRDEGSLQRS GRGIVCECCK HHCTKEELTE
     YCH