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Kappa-conotoxin RIIIJ (Kappa-M-RIIIJ)

 CM3J_CONRA              Reviewed;          25 AA.
P0CG45;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 1.
22-NOV-2017, entry version 18.
RecName: Full=Kappa-conotoxin RIIIJ;
Short=Kappa-M-RIIIJ;
Conus radiatus (Rayed cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=61198;
[1]
PROTEIN SEQUENCE, FUNCTION, TOXIN TARGET, ASSAY ON RAT
ISCHEMIA/REPERFUSION MODEL, MUTAGENESIS OF 6-THR--HIS-11;
6-THR--PRO-8; 9-LYS--HIS-11 AND 10-LYS-HIS-11, SITE, HYDROXYLATION AT
PRO-2; PRO-3; PRO-7; PRO-8; PRO-13; PRO-15 AND PRO-21, AND MASS
SPECTROMETRY.
TISSUE=Venom;
PubMed=20220134; DOI=10.1074/jbc.M109.068486;
Chen P., Dendorfer A., Finol-Urdaneta R.K., Terlau H., Olivera B.M.;
"Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel
blocker: evaluation of cardioprotective effects of kappaM-
conotoxins.";
J. Biol. Chem. 285:14882-14889(2010).
-!- FUNCTION: Kappa-conotoxins inhibits voltage-gated potassium
channels. This toxin dose-dependently and reversibly inhibits the
Kv1.2/KCNA2 channel in mammalia. Does not exert protective effect
on cardiac tissue when administered after an ischemic event.
{ECO:0000269|PubMed:20220134}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
-!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in
the M-4 branch, since 4 residues stand between the fourth and the
fifth cysteine residues.
-!- MASS SPECTROMETRY: Mass=2805.84; Method=Electrospray; Range=1-25;
Note=monoisotopic.; Evidence={ECO:0000269|PubMed:20220134};
-!- MISCELLANEOUS: Has no or very low potency for Kv1.1/KCNA1,
Kv1.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5, Kv1.6/KCNA6, Kv7.2/KCNQ2-
Kv7.3/KCNQ3, and KCa1.1/KCNMA1. {ECO:0000305|PubMed:20220134}.
-!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0019870; F:potassium channel inhibitor activity; IDA:CACAO.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Hydroxylation;
Ion channel impairing toxin; Neurotoxin;
Potassium channel impairing toxin; Secreted; Toxin;
Voltage-gated potassium channel impairing toxin.
PEPTIDE 1 25 Kappa-conotoxin RIIIJ.
/FTId=PRO_0000395613.
SITE 9 9 Significant for high potency for
Kv1.2/KCNA2.
MOD_RES 2 2 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 3 3 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 7 7 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 8 8 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 13 13 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 15 15 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
MOD_RES 21 21 4-hydroxyproline.
{ECO:0000269|PubMed:20220134}.
DISULFID 4 17 {ECO:0000250}.
DISULFID 5 22 {ECO:0000250}.
DISULFID 12 23 {ECO:0000250}.
MUTAGEN 6 11 TPPKKH->SLNLRL: 11-fold decrease in
potency for Kv1.2/KCNA2.
{ECO:0000269|PubMed:20220134}.
MUTAGEN 6 8 TPP->SLN: 2-fold decrease in potency for
Kv1.2/KCNA2.
{ECO:0000269|PubMed:20220134}.
MUTAGEN 9 11 KKH->LRL: 10-fold decrease in potency for
Kv1.2/KCNA2.
{ECO:0000269|PubMed:20220134}.
MUTAGEN 10 11 KH->RL: 1.5-fold decrease in potency for
Kv1.2/KCNA2.
{ECO:0000269|PubMed:20220134}.
SEQUENCE 25 AA; 2701 MW; DDE9E2F99524B5F3 CRC64;
LPPCCTPPKK HCPAPACKYK PCCKS


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