INS1A_CONQU
ID INS1A_CONQU Reviewed; 131 AA.
AC A0A0B5ABE6;
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 Q1 {ECO:0000303|PubMed:25605914};
DE AltName: Full=Insulin 1 {ECO:0000312|EMBL:AJD85836.1};
DE Contains:
DE RecName: Full=Con-Ins Q1 B chain {ECO:0000303|PubMed:25605914};
DE Contains:
DE RecName: Full=Con-Ins Q1 A chain {ECO:0000303|PubMed:25605914};
DE Flags: Precursor;
OS Conus quercinus (Oak cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX NCBI_TaxID=101313;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT SER-130.
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; KP268604; AJD85836.1; -; mRNA.
DR AlphaFoldDB; A0A0B5ABE6; -.
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 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 Q1 B chain"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT /id="PRO_5002099671"
FT PROPEP 59..92
FT /note="C peptide"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT /id="PRO_0000439326"
FT PEPTIDE 93..130
FT /note="Con-Ins Q1 A chain"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5ABD9"
FT /id="PRO_0000439327"
FT MOD_RES 118
FT /note="4-carboxyglutamate; partial"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT MOD_RES 130
FT /note="Serine amide"
FT /evidence="ECO:0000305|PubMed:25605914"
FT DISULFID 29..107
FT /evidence="ECO:0000305"
FT DISULFID 41..110
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT DISULFID 53..123
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
FT DISULFID 109..114
FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95"
SQ SEQUENCE 131 AA; 14435 MW; 6F3FCEFDB0629479 CRC64;
MTTSSYFLLV ALGLLLYLCQ SSFGTEHTCE PGASPHPQGK CRPELAEFHE TMCEVEESLQ
GGTDDARKKR GRASLLRKRR GFLSMLKARA KRNEASPLPR AGRGIVCECC KNSCTYEEIT
EYCPPVTEGS G