ID INS2A_CONGE Reviewed; 130 AA. AC A0A0B5ABD9; DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot. DT 01-APR-2015, sequence version 1. DT 22-APR-2020, entry version 19. DE RecName: Full=Con-Ins G2 {ECO:0000303|PubMed:25605914}; DE AltName: Full=Insulin 2 {ECO:0000312|EMBL:AJD85826.1}; DE Contains: DE RecName: Full=Con-Ins G2 B chain {ECO:0000303|PubMed:25605914}; DE Contains: DE RecName: Full=Con-Ins G2 A chain {ECO:0000303|PubMed:25605914}; DE Flags: Precursor; OS Conus geographus (Geography cone) (Nubecula geographus). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium. OX NCBI_TaxID=6491; 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 -!- 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; KP268610; AJD85826.1; -; mRNA. DR SMR; A0A0B5ABD9; -. 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; IPR036438; Insulin-like_sf. DR InterPro; IPR016724; Insulin-rel_pep. DR InterPro; IPR022353; Insulin_CS. DR PIRSF; PIRSF018431; Molluscan_insulin_rel_peptide; 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 Hydroxylation; Secreted; Signal; Toxin. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT PEPTIDE 25..58 FT /note="Con-Ins G2 B chain" FT /id="PRO_5002112062" FT PROPEP 59..92 FT /note="C peptide" FT /evidence="ECO:0000305|PubMed:25605914" FT /id="PRO_0000439316" FT PEPTIDE 93..130 FT /note="Con-Ins G2 A chain" FT /evidence="ECO:0000250|UniProtKB:Q9NDE7, FT ECO:0000305|PubMed:25605914" FT /id="PRO_0000439317" FT MOD_RES 34 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95" FT MOD_RES 111 FT /note="4-carboxyglutamate; partial" FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95" FT DISULFID 29..100 FT /evidence="ECO:0000305" FT DISULFID 41..103 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95" FT DISULFID 53..116 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95" FT DISULFID 102..107 FT /evidence="ECO:0000250|UniProtKB:A0A0B5AC95" SQ SEQUENCE 130 AA; 14673 MW; C90688DA34517FAB CRC64; MTTSSYFLLV ALGLLLYVRQ SFSTHEHTCQ LDDPAHPQGK CGSDLVNYHE EKCEEEEARR GGTNDGGKKR RRASPLWKRR RFLSMLKARA KRTGYKGIAC ECCQHYCTDQ EFINYCPPVT ESSSSSSSAA //