ID   CA1Z_CONTE              Reviewed;          61 AA.
AC   P0DPL9;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Alpha-conotoxin-like Tx1.2 {ECO:0000303|PubMed:26948522};
DE   AltName: Full=Conotoxin Tx1.1 {ECO:0000303|Ref.1};
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Watkins M., Olivera B.M., Hillyard D.R., McIntosh J.M., Jones R.M.;
RT   "Alpha-conotoxin peptides.";
RL   Patent number US6797808, 22-OCT-2002.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   HYDROXYLATION AT PRO-44 AND PRO-50.
RC   TISSUE=Venom;
RX   PubMed=22709442; DOI=10.1021/pr300312h;
RA   Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA   Yates J.R. III, Bern M.;
RT   "Constrained de novo sequencing of conotoxins.";
RL   J. Proteome Res. 11:4191-4200(2012).
RN   [3]
RP   FUNCTION, AND SYNTHESIS OF 44-60.
RX   PubMed=26948522; DOI=10.1002/anie.201600297;
RA   Carstens B.B., Berecki G., Daniel J.T., Lee H.S., Jackson K.A., Tae H.S.,
RA   Sadeghi M., Castro J., O'Donnell T., Deiteren A., Brierley S.M.,
RA   Craik D.J., Adams D.J., Clark R.J.;
RT   "Structure-activity studies of cysteine-rich alpha-conotoxins that inhibit
RT   high-voltage-activated calcium channels via GABA(B) receptor activation
RT   reveal a minimal functional motif.";
RL   Angew. Chem. Int. Ed. 55:4692-4696(2016).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). This toxin also inhibits high voltage-activated (HVA)
CC       calcium channel currents in rat DRG neurons (8% inhibition at 1 uM
CC       toxin) probably by activating GABA(B) receptors (GABBR1 and/or GABBR2)
CC       (PubMed:26948522). {ECO:0000250|UniProtKB:P0CE73,
CC       ECO:0000269|PubMed:26948522}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22709442}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22709442}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   -!- CAUTION: The synthetic peptide described in PubMed:26948522 is one
CC       residue shorter than the mature sequence shown in this entry (44-60)
CC       (the Arg-43 is removed) and the Cys-60 is amidated.
CC       {ECO:0000305|PubMed:26948522}.
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DR   EMBL; BD261400; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; AR584807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DPL9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   Pfam; PF07365; Toxin_8; 1.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond; Hydroxylation;
KW   Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..42
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000445056"
FT   PEPTIDE         43..60
FT                   /note="Alpha-conotoxin-like Tx1.2"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000445057"
FT   REGION          48..50
FT                   /note="Ser-Xaa-Pro motif, crucial for potent interaction
FT                   with nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   MOD_RES         44
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   MOD_RES         50
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
FT   DISULFID        47..60
FT                   /evidence="ECO:0000250|UniProtKB:P56636"
SQ   SEQUENCE   61 AA;  6597 MW;  7E4888D551E05691 CRC64;
     MFTVFLLVVL ATTVVSFTSG RSTFRGRNAA AKASGLVSLT DRRPQCCSHP ACNVDHPEIC
     R