I2BA_CONSP
ID I2BA_CONSP Reviewed; 32 AA.
AC P0C615;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Kappa-conotoxin SrXIA;
DE Short=Kappa-SrXIA;
DE AltName: Full=I2-superfamily conotoxin sr11a;
OS Conus spurius (Alphabet cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lindaconus.
OX NCBI_TaxID=192919;
RN [1]
RP PROTEIN SEQUENCE, GAMMA-CARBOXYGLUTAMATION AT GLU-9,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-10, AMIDATION AT PRO-32, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17166627; DOI=10.1016/j.peptides.2006.08.024;
RA Aguilar M.B., Lopez-Vera E., Heimer de la Cotera E.P., Falcon A.,
RA Olivera B.M., Maillo M.;
RT "I-conotoxins in vermivorous species of the West Atlantic: peptide sr11a
RT from Conus spurius.";
RL Peptides 28:18-23(2007).
RN [2]
RP FUNCTION, TOXIN TARGET, 3D-STRUCTURE MODELING, AND SITES ARG-17 AND ARG-29.
RC TISSUE=Venom;
RX PubMed=20403399; DOI=10.1016/j.peptides.2010.04.007;
RA Aguilar M.B., Perez-Reyes L.I., Lopez Z., de la Cotera E.P., Falcon A.,
RA Ayala C., Galvan M., Salvador C., Escobar L.I.;
RT "Peptide sr11a from Conus spurius is a novel peptide blocker for Kv1
RT potassium channels.";
RL Peptides 31:1287-1291(2010).
CC -!- FUNCTION: Kappa-conotoxins bind and inhibit voltage-gated potassium
CC channels. This toxin inhibits Kv1.2/KCNA2 and Kv1.6/KCNA6. Produces
CC stiffening of body, limbs and tail when injected intracranially into
CC mice. {ECO:0000269|PubMed:17166627, ECO:0000269|PubMed:20403399}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17166627}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:17166627}.
CC -!- DOMAIN: The cysteine framework is XI (C-C-CC-CC-C-C).
CC -!- MASS SPECTROMETRY: Mass=3651.78; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17166627};
CC -!- MISCELLANEOUS: Has no effect on Kv1.3/KCNA3 channels.
CC {ECO:0000305|PubMed:20403399}.
CC -!- SIMILARITY: Belongs to the conotoxin I2 superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C615; -.
DR SMR; P0C615; -.
DR TCDB; 8.B.16.1.5; the maurocalcine (maca) family.
DR PRIDE; P0C615; -.
DR ConoServer; 2802; SrXIA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR013141; Conotoxin-I_CS.
DR InterPro; IPR020242; Conotoxin_I2-superfamily.
DR Pfam; PF17557; Conotoxin_I2; 1.
DR PROSITE; PS60019; I_CONOTOXIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Gamma-carboxyglutamic acid; Ion channel impairing toxin; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..32
FT /note="Kappa-conotoxin SrXIA"
FT /id="PRO_0000314091"
FT SITE 17
FT /note="Pharmacophore"
FT /evidence="ECO:0000305"
FT SITE 29
FT /note="Pharmacophore"
FT /evidence="ECO:0000305"
FT MOD_RES 9
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:17166627"
FT MOD_RES 10
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:17166627"
FT MOD_RES 32
FT /note="Proline amide"
FT /evidence="ECO:0000269|PubMed:17166627"
FT DISULFID 1..15
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 8..20
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 14..24
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
FT DISULFID 19..28
FT /evidence="ECO:0000250|UniProtKB:Q7Z094"
SQ SEQUENCE 32 AA; 3660 MW; 48D975B724F47F8F CRC64;
CRTEGMSCEE NQQCCWRSCC RGECEAPCRF GP
