CRVP_LATSE
ID CRVP_LATSE Reviewed; 238 AA.
AC Q8JI38;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cysteine-rich venom protein latisemin;
DE Short=CRVP;
DE Flags: Precursor;
OS Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda
OS semifasciata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX NCBI_TaxID=8631;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12047379; DOI=10.1046/j.1432-1033.2002.02940.x;
RA Yamazaki Y., Koike H., Sugiyama Y., Motoyoshi K., Wada T., Hishinuma S.,
RA Mita M., Morita T.;
RT "Cloning and characterization of novel snake venom proteins that block
RT smooth muscle contraction.";
RL Eur. J. Biochem. 269:2708-2715(2002).
CC -!- FUNCTION: Blocks contraction of smooth muscle elicited by high
CC potassium-induced depolarization (PubMed:12047379). May target voltage-
CC gated calcium channels (Cav) on smooth muscle.
CC {ECO:0000269|PubMed:12047379}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AF384220; AAM45666.1; -; mRNA.
DR AlphaFoldDB; Q8JI38; -.
DR SMR; Q8JI38; -.
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: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; PS01010; CRISP_2; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 2: Evidence at transcript level;
KW Calcium channel impairing toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..238
FT /note="Cysteine-rich venom protein latisemin"
FT /id="PRO_0000006278"
FT DOMAIN 38..164
FT /note="SCP"
FT DOMAIN 200..233
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 75..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 92..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 148..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 184..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 187..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 200..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 209..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 238 AA; 26416 MW; 2CBE6FFA231CA4CF CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK RENQKEIVDK HNALRRSVRP TARNMLQMEW
NSDAAQNAQR WADRCSFAHS PSHLRTVGKF SCGENLFMSS QPYAWSRVIQ SWYDENKNFI
YDVGANPPGS VIGHYTQIVW YKSHLLGCAA ARCSSSKYLY VCQYCPAGNI IGSIATPYKS
GPPCGDCPSA CVNGLCTNPC KHENEFTNCQ SLVKQTGCQN TWIQSKCPAS CFCRTEII