CM31_CONLT
ID CM31_CONLT Reviewed; 69 AA.
AC Q2I2Q5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Iota-conotoxin LtIIIA;
DE AltName: Full=Lt3.1;
DE AltName: Full=Lt3a;
DE Flags: Precursor;
OS Conus litteratus (Lettered cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Elisaconus.
OX NCBI_TaxID=89445;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=16908117; DOI=10.1016/j.ygeno.2006.06.014;
RA Pi C., Liu J., Peng C., Liu Y., Jiang X., Zhao Y., Tang S., Wang L.,
RA Dong M., Chen S., Xu A.;
RT "Diversity and evolution of conotoxins based on gene expression profiling
RT of Conus litteratus.";
RL Genomics 88:809-819(2006).
RN [2]
RP PROTEIN SEQUENCE OF 53-69, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, GAMMA-CARBOXYGLUTAMATION AT GLU-54 AND GLU-57, AND
RP HYDROXYLATION AT PRO-58.
RC TISSUE=Venom;
RX PubMed=19562324; DOI=10.1007/s00204-009-0453-8;
RA Wang L., Liu J., Pi C., Zeng X., Zhou M., Jiang X., Chen S., Ren Z., Xu A.;
RT "Identification of a novel M-superfamily conotoxin with the ability to
RT enhance tetrodotoxin sensitive sodium currents.";
RL Arch. Toxicol. 83:925-932(2009).
CC -!- FUNCTION: Iota-conotoxins bind to voltage-gated sodium channels and act
CC as agonists by shifting the voltage-dependence of activation to more
CC hyperpolarized levels. This toxin enhances tetrodotoxin-sensitive
CC sodium current in rat dorsal root ganglion neurons.
CC {ECO:0000269|PubMed:19562324}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19562324}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:19562324}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 1 branch, since 1 residue stands between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1964.85; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19562324};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; DQ345377; ABC74985.1; -; mRNA.
DR AlphaFoldDB; Q2I2Q5; -.
DR TCDB; 8.B.28.1.8; the mu-conotoxin (mu-conotoxin) family.
DR ConoServer; 1163; LtIIIA precursor.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0044490; P:positive regulation of voltage-gated sodium channel activity in another organism; IDA:UniProtKB.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Hydroxylation; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..52
FT /evidence="ECO:0000269|PubMed:19562324"
FT /id="PRO_0000315525"
FT PEPTIDE 53..69
FT /note="Iota-conotoxin LtIIIA"
FT /id="PRO_0000315526"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000305|PubMed:19562324"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000305|PubMed:19562324"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:19562324"
FT DISULFID 55..67
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 56..65
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 61..68
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ SEQUENCE 69 AA; 7931 MW; 42B49205F3A7157A CRC64;
MLKMGVLLFT FLVLFPLTTL ELDTDRPVER HAAIKQDLKP QERRGIRLHA PRDECCEPQW
CDGACDCCS
