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CAHAD_HOFGE
ID   CAHAD_HOFGE             Reviewed;          74 AA.
AC   B8QG00; P85499;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Hadrucalcin {ECO:0000303|Ref.2};
DE            Short=HdCa {ECO:0000303|PubMed:19389159, ECO:0000303|Ref.2};
DE   Flags: Precursor;
OS   Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Iuroidea; Hadrurus.
OX   NCBI_TaxID=380989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-74, FUNCTION ON RYR1 AND
RP   RYR2, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Telson, and Venom;
RX   PubMed=19389159; DOI=10.1111/j.1476-5381.2009.00147.x;
RA   Schwartz E.F., Capes E.M., Diego-Garcia E., Zamudio F.Z., Fuentes O.,
RA   Possani L.D., Valdivia H.H.;
RT   "Characterization of hadrucalcin, a peptide from Hadrurus gertschi scorpion
RT   venom with pharmacological activity on ryanodine receptors.";
RL   Br. J. Pharmacol. 157:392-403(2009).
RN   [2]
RP   FUNCTION.
RA   Capes E.M., Schwartz E.F., Diego-Garcia E., Zamudio F.Z., Possani L.D.,
RA   Valdivia H.H.;
RT   "Hadrucalcin, a novel member of the Calcin scorpion toxin family, rapidly
RT   penetrates cellular membranes to bind ryanodine receptors and alter calcium
RT   release.";
RL   Biophys. J. 94:2631-2631(2008).
RN   [3]
RP   FUNCTION, SYNTHESIS OF 40-74, AND 3D-STRUCTURE MODELING.
RX   PubMed=27114612; DOI=10.1085/jgp.201511499;
RA   Xiao L., Gurrola G.B., Zhang J., Valdivia C.R., SanMartin M., Zamudio F.Z.,
RA   Zhang L., Possani L.D., Valdivia H.H.;
RT   "Structure-function relationships of peptides forming the calcin family of
RT   ryanodine receptor ligands.";
RL   J. Gen. Physiol. 147:375-394(2016).
CC   -!- FUNCTION: This toxin activates ryanodine receptors RyR1 and RyR2 by
CC       inducing a long-lasting subconductance state (35% of the full
CC       conductance stateon RyR1) (PubMed:19389159, PubMed:27114612).
CC       Furthermore, it triggers calcium release from sarcoplasmic vesicles
CC       (11.8 nM are enough to induce a sharp release on RyR1, and 55% of the
CC       total calcium is released after toxin (100 nM) addition on RyR1)
CC       probably by acting as a cell-penetrating peptide (CPP)
CC       (PubMed:19389159). In addition, it has been shown to dose-dependently
CC       stimulate ryanodine binding to RyR1 (EC(50)=14.8 nM) (PubMed:27114612).
CC       It also augments the bell-shaped calcium-[3H]ryanodine binding curve
CC       that is maximal at about 10 uM calcium concentration (PubMed:27114612).
CC       It binds a different site as ryanodine (By similarity). It acts
CC       synergistically with caffeine (PubMed:19389159). In vivo,
CC       intracerebroventricular injection into mice induces neurotoxic
CC       symptoms, followed by death (By similarity).
CC       {ECO:0000250|UniProtKB:A0A1L4BJ42, ECO:0000250|UniProtKB:P59868,
CC       ECO:0000250|UniProtKB:P60254, ECO:0000269|PubMed:19389159,
CC       ECO:0000269|PubMed:27114612, ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19389159}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19389159}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P59868}.
CC   -!- MASS SPECTROMETRY: Mass=4190.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19389159};
CC   -!- SIMILARITY: Belongs to the scorpion calcin family. {ECO:0000255}.
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DR   EMBL; EU496812; ACC99422.1; -; mRNA.
DR   AlphaFoldDB; B8QG00; -.
DR   SMR; B8QG00; -.
DR   TCDB; 8.B.16.1.3; the maurocalcine (maca) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012632; Scorpion_calcine.
DR   Pfam; PF08099; Toxin_27; 1.
DR   PROSITE; PS60028; SCORPION_CALCINE; 1.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..39
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:19389159"
FT                   /id="PRO_0000383671"
FT   PEPTIDE         40..74
FT                   /note="Hadrucalcin"
FT                   /evidence="ECO:0000269|PubMed:19389159"
FT                   /id="PRO_5000433512"
FT   REGION          64..65
FT                   /note="Essential for stimulation of [3H]ryanodine binding
FT                   to RYR1"
FT                   /evidence="ECO:0000250|UniProtKB:P59868,
FT                   ECO:0000250|UniProtKB:P60254"
FT   SITE            72
FT                   /note="Essential for stimulation of [3H]ryanodine binding
FT                   to RYR1"
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   SITE            74
FT                   /note="Essential for stimulation of [3H]ryanodine binding
FT                   to RYR1"
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   DISULFID        51..62
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
FT   DISULFID        57..73
FT                   /evidence="ECO:0000250|UniProtKB:P59868"
SQ   SEQUENCE   74 AA;  8593 MW;  12D5F2B54C1640A2 CRC64;
     MKTSSLTIIF IAVIITIICL NIHDIEAREI EFNAGRVVRS EKDCIKHLQR CRENKDCCSK
     KCSRRGTNPE KRCR
 
 
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