CRVP_TRIPP
ID CRVP_TRIPP Reviewed; 33 AA.
AC P81995;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 23-FEB-2022, entry version 47.
DE RecName: Full=Cysteine-rich venom protein tripurin;
DE Short=CRVP;
DE Flags: Fragment;
OS Trimeresurus purpureomaculatus (Mangrove pit viper) (Cryptelytrops
OS purpureomaculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=101163 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Venom {ECO:0000305};
RA Kini M.R.;
RL Submitted (AUG-1999) to UniProtKB.
CC -!- FUNCTION: Blocks contraction of smooth muscle elicited by high
CC potassium-induced depolarization, but does not block caffeine-
CC stimulated contraction. May target voltage-gated calcium channels on
CC smooth muscle (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- PTM: Contains 8 disulfide bonds. {ECO:0000250|UniProtKB:P84808}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR TCDB; 8.B.9.1.4; 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR035940; CAP_sf.
DR SUPFAM; SSF55797; SSF55797; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT CHAIN 1..>33
FT /note="Cysteine-rich venom protein tripurin"
FT /id="PRO_0000211530"
FT NON_TER 33
FT /evidence="ECO:0000305"
SQ SEQUENCE 33 AA; 3974 MW; E5602D4AFFADDE0E CRC64;
PRNPEIQNEI IDLHNYLRRS VNPXASNMLR SQW