ID   CA4A_CONMA              Reviewed;          79 AA.
AC   P0C1X1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Kappa-conotoxin-like MIVA;
DE   Flags: Precursor;
OS   Conus magus (Magical cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-74, HYDROXYLATION AT
RP   PRO-40; PRO-55; PRO-60; PRO-61; PRO-69; PRO-70 AND PRO-74, AMIDATION AT
RP   PRO-74, GAMMA-CARBOXYGLUTAMATION AT GLU-41, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=14701840; DOI=10.1074/jbc.m309654200;
RA   Santos A.D., McIntosh J.M., Hillyard D.R., Cruz L.J., Olivera B.M.;
RT   "The A-superfamily of conotoxins: structural and functional divergence.";
RL   J. Biol. Chem. 279:17596-17606(2004).
CC   -!- FUNCTION: Kappa-conotoxins bind and inhibit voltage-gated potassium
CC       channels (By similarity). This highly potent excitatory peptide elicits
CC       repetitive action potentials and causes the same spastic symptomatology
CC       as kappa-conotoxin SIVA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC   -!- PTM: Contains 3 disulfide bonds (By similarity). They are not added,
CC       since framework IV presents two different connectivities (I-V, II-III,
CC       IV-VI and I-III, II-V, IV-VI). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=5095.3; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:14701840};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1X1; -.
DR   SMR; P0C1X1; -.
DR   ConoServer; 18; MIVA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..38
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT                   /id="PRO_0000249800"
FT   PEPTIDE         39..74
FT                   /note="Kappa-conotoxin-like MIVA"
FT                   /id="PRO_0000249801"
FT   PROPEP          75..79
FT                   /id="PRO_0000249802"
FT   MOD_RES         40
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         41
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         60
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         61
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         69
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         70
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         74
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   MOD_RES         74
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:14701840"
FT   CARBOHYD        45
FT                   /note="O-linked (HexNAc...) threonine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        47
FT                   /note="O-linked (HexNAc...) threonine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   79 AA;  8680 MW;  46AC083059DF97CA CRC64;
     MGMRMMFTVF LLVVLATTVV SIPSDRASDG RNAVVHERAP ELVVTATTNC CGYNPMTICP
     PCMCTYSCPP KRKPGRRND