ID   CL1A_HOTJU              Reviewed;          64 AA.
AC   F1CIZ6;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Phi-buthitoxin-Hj1a {ECO:0000312|EMBL:ADY39527.1};
DE            Short=Phi-BUTX-Hj1a {ECO:0000305};
DE   Flags: Precursor;
OS   Hottentotta judaicus (Black scorpion) (Buthotus judaicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Hottentotta.
OX   NCBI_TaxID=6863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21329713; DOI=10.1016/j.toxicon.2011.02.001;
RA   Morgenstern D., Rohde B.H., King G.F., Tal T., Sher D., Zlotkin E.;
RT   "The tale of a resting gland: transcriptome of a replete venom gland from
RT   the scorpion Hottentotta judaicus.";
RL   Toxicon 57:695-703(2011).
CC   -!- FUNCTION: May increase intracellular calcium release through the
CC       activation of nuclear inositol 1,4,5-trisphosphate receptors (ITPR) of
CC       cardiomyocytes, thereby causing an increase in the contraction
CC       frequency of these cells. {ECO:0000250|UniProtKB:P0DM29}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21329713}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:21329713}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P59868}.
CC   -!- SIMILARITY: Belongs to the scorpion calcin-like family. {ECO:0000305}.
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DR   EMBL; HQ288104; ADY39527.1; -; mRNA.
DR   AlphaFoldDB; F1CIZ6; -.
DR   SMR; F1CIZ6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cardiotoxin; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..64
FT                   /note="Phi-buthitoxin-Hj1a"
FT                   /id="PRO_5003265156"
FT   DISULFID        29..43
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   DISULFID        36..49
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
SQ   SEQUENCE   64 AA;  7061 MW;  EE1A2F4D4D26FEEF CRC64;
     MNSFVVVLLL FIAILCNAEQ ESDENARSCN RLGKKCNSDG DCCRYGERCL SSGVGYYCKP
     DFGP