CAURO_UROYA
ID CAURO_UROYA Reviewed; 68 AA.
AC L0GBR1;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Urocalcin {ECO:0000303|PubMed:27114612};
DE Short=UrCa {ECO:0000303|PubMed:27114612};
DE AltName: Full=Calcium-channel toxin-like 20 {ECO:0000312|EMBL:AGA82762.1};
DE Flags: Precursor;
OS Urodacus yaschenkoi (Inland robust scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Urodacinae; Urodacus.
OX NCBI_TaxID=1273102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=23182832; DOI=10.1016/j.toxicon.2012.11.017;
RA Luna-Ramirez K., Quintero-Hernandez V., Vargas-Jaimes L., Batista C.V.,
RA Winkel K.D., Possani L.D.;
RT "Characterization of the venom from the Australian scorpion Urodacus
RT yaschenkoi: molecular mass analysis of components, cDNA sequences and
RT peptides with antimicrobial activity.";
RL Toxicon 63:44-54(2013).
RN [2]
RP FUNCTION, SYNTHESIS OF 36-68, NOMENCLATURE, 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 only weakly stabilizes ryanodine receptor 1 (RyR1)
CC opening in a long-lasting subconductance state (55% of the full
CC conductance state obtained only at high concentrations (1 uM))
CC (PubMed:27114612). In addition, it has been shown to dose-dependently
CC stimulate ryanodine binding to RyR1 with the lowest activity of all
CC calcins (EC(50)=376 nM) (PubMed:27114612). It also augments the bell-
CC shaped calcium-[3H]ryanodine binding curve that is maximal at about 10
CC uM calcium concentration (PubMed:27114612). It binds a different site
CC as ryanodine (By similarity). It acts synergistically with caffeine (By
CC similarity). In contrast to other calcins, it does not trigger calcium
CC release from sarcoplasmic vesicles even at high concentration (1 uM)
CC (PubMed:27114612). In vivo, intracerebroventricular injection into mice
CC induces neurotoxic symptoms, followed by death (By similarity).
CC {ECO:0000250|UniProtKB:A0A1L4BJ42, ECO:0000250|UniProtKB:B8QG00,
CC ECO:0000250|UniProtKB:P59868, ECO:0000250|UniProtKB:P60254,
CC ECO:0000269|PubMed:27114612}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23182832}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23182832}.
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 family. {ECO:0000305}.
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DR EMBL; JX274248; AGA82762.1; -; mRNA.
DR AlphaFoldDB; L0GBR1; -.
DR SMR; L0GBR1; -.
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 3: Inferred from homology;
KW Calcium channel impairing toxin; 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..35
FT /evidence="ECO:0000255"
FT /id="PRO_5001091939"
FT CHAIN 36..68
FT /note="Urocalcin"
FT /id="PRO_5001091940"
FT REGION 57..59
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 66
FT /note="Essential for stimulation of [3H]ryanodine binding
FT to RYR1"
FT /evidence="ECO:0000250|UniProtKB:P59868"
FT SITE 68
FT /note="Essential for stimulation of [3H]ryanodine binding
FT to RYR1"
FT /evidence="ECO:0000250|UniProtKB:P59868"
FT DISULFID 38..52
FT /evidence="ECO:0000250|UniProtKB:P59868"
FT DISULFID 45..56
FT /evidence="ECO:0000250|UniProtKB:P59868"
FT DISULFID 51..67
FT /evidence="ECO:0000250|UniProtKB:P59868"
SQ SEQUENCE 68 AA; 7793 MW; 2EB936121DE062E6 CRC64;
MKASTLVVIF IVIFITISSF SIHDVQASGV EKREQKDCLK KLKLCKENKD CCSKSCKRRG
TNIEKRCR
