ID   CA4B_CONSE              Reviewed;          80 AA.
AC   P0CE76; P0C1Y3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Kappa-conotoxin-like SmIVB;
DE   Flags: Precursor;
OS   Conus stercusmuscarum (Fly-specked cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=89452;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=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-A-conotoxins bind and inhibit voltage-gated potassium
CC       channels. {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   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CE76; -.
DR   SMR; P0CE76; -.
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   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; 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:0000250"
FT                   /id="PRO_0000392709"
FT   PEPTIDE         39..75
FT                   /note="Kappa-conotoxin-like SmIVB"
FT                   /id="PRO_0000392710"
FT   PROPEP          76..80
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000392711"
FT   MOD_RES         40
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         72
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         75
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="O-linked (HexNAc...) serine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        46
FT                   /note="O-linked (HexNAc...) threonine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   80 AA;  8778 MW;  5FE60549491A0203 CRC64;
     MGMRMMFTVF LLVVLATTVV SIPSDRASDG RNAEVNERAP WLVPSTITTC CGYDPGSMCP
     PCMCNNTCKP KPKKSGRRNH