ID   CU51B_CONCL             Reviewed;          76 AA.
AC   D2Y170;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Conotoxin Cal5a L2 {ECO:0000303|PubMed:21172372};
DE   Contains:
DE     RecName: Full=Conotoxin Cal5b L2 {ECO:0000303|PubMed:21172372};
DE   Contains:
DE     RecName: Full=Conotoxin Cal5.1 {ECO:0000303|PubMed:21172372};
DE   Flags: Precursor;
OS   Californiconus californicus (California cone) (Conus californicus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Californiconus.
OX   NCBI_TaxID=1736779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=21172372; DOI=10.1016/j.toxicon.2010.12.008;
RA   Elliger C.A., Richmond T.A., Lebaric Z.N., Pierce N.T., Sweedler J.V.,
RA   Gilly W.F.;
RT   "Diversity of conotoxin types from Conus californicus reflects a diversity
RT   of prey types and a novel evolutionary history.";
RL   Toxicon 57:311-322(2011).
CC   -!- FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion
CC       channels. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21172372}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:21172372}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC).
CC       {ECO:0000305|PubMed:21172372}.
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; GU290200; ADB43127.1; -; mRNA.
DR   AlphaFoldDB; D2Y170; -.
DR   ConoServer; 3982; Cal5.1 L3 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_5000566285"
FT   PEPTIDE         44..74
FT                   /note="Conotoxin Cal5a L2"
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_0000414962"
FT   PEPTIDE         54..74
FT                   /note="Conotoxin Cal5b L2"
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_0000414963"
FT   PEPTIDE         61..74
FT                   /note="Conotoxin Cal5.1"
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_5000566286"
FT   MOD_RES         50
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         62
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         64
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   76 AA;  8367 MW;  1D3706E321A38844 CRC64;
     MRFYIGLMAA LMLTSILRTD SASVGQTGTK SELALIERVI RQRDAADVKP VARHNDGPGR
     DPAPCCQHPI ETCCRR