O261_CONAA
ID O261_CONAA Reviewed; 84 AA.
AC A0A2L2P6T1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 23-FEB-2022, entry version 14.
DE RecName: Full=Conotoxin Am6.1 {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am3286 {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am3408 {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am3452 {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am6.1a {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am6.1b {ECO:0000303|PubMed:29447903};
DE AltName: Full=Am6.1c {ECO:0000303|PubMed:29447903};
DE Flags: Precursor;
OS Conus amadis (Amadis cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Leptoconus.
OX NCBI_TaxID=198732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 48-77,
RP BROMINATION AT TRP-51, GAMMA-CARBOXYGLUTAMATION AT GLU-60 AND GLU-64,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=29447903; DOI=10.1016/j.toxicon.2018.02.005;
RA Vijayasarathy M., Balaram P.;
RT "Mass spectrometric identification of bromotryptophan containing conotoxin
RT sequences from the venom of C.amadis.";
RL Toxicon 144:68-74(2018).
CC -!- FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation
CC pacemaker channels (HCN). {ECO:0000250|UniProtKB:P56711}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29447903}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:29447903}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- PTM: Three forms of this peptides have been described. The unmodified
CC Am6.1a (Am3286) is not detected in the venom; Am6.1b (Am3408) is only
CC Trp brominated, while Am6.1c (Am3452) is both Trp brominated and Glu
CC gamma-carboxyglutamated. Both Am6.1b and Am6.1c are detected in the
CC venom. {ECO:0000269|PubMed:29447903}.
CC -!- SIMILARITY: Belongs to the conotoxin O2 family. {ECO:0000305}.
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DR EMBL; MG721537; AVH76830.1; -; Genomic_DNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Bromination; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Ion channel impairing toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..47
FT /evidence="ECO:0000305|PubMed:29447903"
FT /id="PRO_0000453597"
FT PEPTIDE 48..77
FT /note="Conotoxin Am6.1"
FT /evidence="ECO:0000269|PubMed:29447903"
FT /id="PRO_5014623542"
FT PROPEP 78..84
FT /evidence="ECO:0000305|PubMed:29447903"
FT /id="PRO_0000453598"
FT MOD_RES 51
FT /note="6'-bromotryptophan; in Am6.1b"
FT /evidence="ECO:0000269|PubMed:29447903"
FT MOD_RES 60
FT /note="4-carboxyglutamate; partial; in Am6.1b and Am6.1c"
FT /evidence="ECO:0000269|PubMed:29447903"
FT MOD_RES 64
FT /note="4-carboxyglutamate; partial; in Am6.1b and Am6.1c"
FT /evidence="ECO:0000269|PubMed:29447903"
FT DISULFID 48..62
FT /evidence="ECO:0000250|UniProtKB:Q26443"
FT DISULFID 55..66
FT /evidence="ECO:0000250|UniProtKB:Q26443"
FT DISULFID 61..71
FT /evidence="ECO:0000250|UniProtKB:Q26443"
SQ SEQUENCE 84 AA; 9373 MW; 2374D3854A645FDA CRC64;
MEKLTILLLV AAVLMSTHAM FQGGGEKSRK AINFSETRKL ARNKQKRCDG WSTYCHDDSE
CCSETCANSY CTLIKGVRTT SHPI
