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-NOV-2017, entry version 13. 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; Lophotrochozoa; Mollusca; Gastropoda; OC Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae; OC Conus. 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., RA Ueberheide B., Douglass A.D., Schlegel A., Imperial J.S., Watkins M., RA Bandyopadhyay P.K., Yandell M., Li Q., Purcell A.W., Norton R.S., RA 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 CC peptide into zebrafish lowers blood glucose with the same potency CC than human insulin. In vivo, when applied to water, this peptide CC reduces overall locomotor activity of zebrafish larvae, observed CC as a significant decrease in the percentage of time spent swimming CC and movement 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 Gene3D; 1.10.100.10; -; 1. 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; KW Hormone; Hydroxylation; Secreted; Signal; Toxin. FT SIGNAL 1 24 {ECO:0000255}. FT PEPTIDE 25 58 Con-Ins G2 B chain. FT /FTId=PRO_5002112062. FT PROPEP 59 92 C peptide. {ECO:0000305|PubMed:25605914}. FT /FTId=PRO_0000439316. FT PEPTIDE 93 130 Con-Ins G2 A chain. FT {ECO:0000250|UniProtKB:Q9NDE7, FT ECO:0000305|PubMed:25605914}. FT /FTId=PRO_0000439317. FT MOD_RES 34 34 4-hydroxyproline; partial. FT {ECO:0000250|UniProtKB:A0A0B5AC95}. FT MOD_RES 111 111 4-carboxyglutamate; partial. FT {ECO:0000250|UniProtKB:A0A0B5AC95}. FT DISULFID 29 100 {ECO:0000305}. FT DISULFID 41 103 Interchain (between B and A chains). FT {ECO:0000250|UniProtKB:A0A0B5AC95}. FT DISULFID 53 116 Interchain (between B and A chains). FT {ECO:0000250|UniProtKB:A0A0B5AC95}. FT DISULFID 102 107 {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 //