CRVP_HELHO
ID CRVP_HELHO Reviewed; 242 AA.
AC Q91055; P46693;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cysteine-rich venom protein helothermine;
DE Short=CRVP HLTx;
DE Flags: Precursor;
OS Heloderma horridum horridum (Mexican beaded lizard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX NCBI_TaxID=8552;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=7647234; DOI=10.1016/s0006-3495(95)80410-8;
RA Morrissette J., Kraetzschmar J., Haendler B., El-Hayek R.,
RA Mochca-Morales J., Martin B.M., Patel J.R., Moss R.L., Schleuning W.-D.,
RA Coronado R., Possani L.D.;
RT "Primary structure and properties of helothermine, a peptide toxin that
RT blocks ryanodine receptors.";
RL Biophys. J. 68:2280-2288(1995).
RN [2]
RP PROTEIN SEQUENCE OF 20-39, AND CHARACTERIZATION.
RC TISSUE=Venom;
RX PubMed=1693019; DOI=10.1016/0041-0101(90)90065-f;
RA Mochca-Morales J., Martin B.M., Possani L.D.;
RT "Isolation and characterization of helothermine, a novel toxin from
RT Heloderma horridum horridum (Mexican beaded lizard) venom.";
RL Toxicon 28:299-309(1990).
RN [3]
RP FUNCTION.
RX PubMed=8071987; DOI=10.1007/bf00232674;
RA Nobile M., Magnelli V., Lagostena L., Mochca-Morales J., Possani L.D.,
RA Prestipino G.;
RT "The toxin helothermine affects potassium currents in newborn rat
RT cerebellar granule cells.";
RL J. Membr. Biol. 139:49-55(1994).
RN [4]
RP FUNCTION.
RX PubMed=8817251; DOI=10.1007/bf00241369;
RA Nobile M., Noceti F., Prestipino G., Possani L.D.;
RT "Helothermine, a lizard venom toxin, inhibits calcium current in cerebellar
RT granules.";
RL Exp. Brain Res. 110:15-20(1996).
CC -!- FUNCTION: Alters a variety of ion channel activities, including
CC voltage-gated potassium channels (Kv) (PubMed:8071987), voltage-gated
CC calcium channels (L-, N-, and P-type) (Cav) (PubMed:8817251) and
CC ryanodine receptors (RyR) (PubMed:7647234). Is toxic to mice (causes
CC lethargy, partial paralysis of rear limbs and lowering of body
CC temperature). {ECO:0000269|PubMed:7647234, ECO:0000269|PubMed:8071987,
CC ECO:0000269|PubMed:8817251}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: IC(50)=0.52 uM on IA-type current, and 0.86 uM on
CC delayed rectifier current. {ECO:0000305|PubMed:8071987}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; U13619; AAC59730.1; -; mRNA.
DR PIR; A34859; A34859.
DR AlphaFoldDB; Q91055; -.
DR SMR; Q91055; -.
DR TCDB; 8.B.9.1.3; the triflin toxin (triflin or crisp) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd05383; CAP_CRISP; 1.
DR Gene3D; 1.10.10.740; -; 1.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR042076; Crisp-like_dom.
DR InterPro; IPR001283; CRISP-related.
DR InterPro; IPR013871; Cysteine_rich_secretory.
DR InterPro; IPR034117; SCP_CRISP.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF08562; Crisp; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01009; CRISP_1; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW Signal; Toxin; Voltage-gated calcium channel impairing toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1693019"
FT CHAIN 20..242
FT /note="Cysteine-rich venom protein helothermine"
FT /id="PRO_0000006272"
FT DOMAIN 41..169
FT /note="SCP"
FT DOMAIN 205..237
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 77..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 94..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 150..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 189..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 205..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 214..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 223..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 242 AA; 27493 MW; 0E183FC2F925DF3C CRC64;
MILLSLYLCL AAMLHQSEGE ASPKLPGLMT SNPDQQTEIT DKHNNLRRIV EPTASNMLKM
TWSNKIAQNA QRSANQCTLE HTSKEERTID GVECGENLFF SSAPYTWSYA IQNWFDERKY
FRFNYGPTAQ NVMIGHYTQV VWYRSYELGC AIAYCPDQPT YKYYQVCQYC PGGNIRSRKY
TPYSIGPPCG DCPDACDNGL CTNPCKQNDV YNNCPDLKKQ VGCGHPIMKD CMATCKCLTE
IK
