CRVP_ECHCO
ID CRVP_ECHCO Reviewed; 220 AA.
AC P0DMT4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE AltName: Full=ECO_00025;
OS Echis coloratus (Carpet viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=64175;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23747272; DOI=10.1016/j.toxicon.2013.05.017;
RA Conlon J.M., Attoub S., Arafat H., Mechkarska M., Casewell N.R.,
RA Harrison R.A., Calvete J.J.;
RT "Cytotoxic activities of [Ser49]phospholipase A(2) from the venom of the
RT saw-scaled vipers Echis ocellatus, Echis pyramidum leakeyi, Echis carinatus
RT sochureki, and Echis coloratus.";
RL Toxicon 71:96-104(2013).
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 in
CC smooth muscle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=24682; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23747272};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DMT4; -.
DR SMR; P0DMT4; -.
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 InterPro; IPR002413; V5_allergen-like.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF08562; Crisp; 1.
DR PRINTS; PR00838; V5ALLERGEN.
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 1: Evidence at protein level;
KW Calcium channel impairing toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT CHAIN 1..220
FT /note="Cysteine-rich venom protein"
FT /evidence="ECO:0000250|UniProtKB:B7FDI0"
FT /id="PRO_0000432599"
FT DOMAIN 20..147
FT /note="SCP"
FT /evidence="ECO:0000250|UniProtKB:B7FDI0"
FT DOMAIN 183..215
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 56..134
FT /evidence="ECO:0000250"
FT DISULFID 73..148
FT /evidence="ECO:0000250"
FT DISULFID 129..145
FT /evidence="ECO:0000250"
FT DISULFID 167..174
FT /evidence="ECO:0000250"
FT DISULFID 170..179
FT /evidence="ECO:0000250"
FT DISULFID 183..215
FT /evidence="ECO:0000250"
FT DISULFID 192..209
FT /evidence="ECO:0000250"
FT DISULFID 200..213
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 24699 MW; 7F454E35DDF7064E CRC64;
NVDFDSESPR KPEIQNEIID LHNSLRRSVN PTASNMLRME WYPEAAANAE RWAFRCTLNH
SPRDSRVIDG IKCGENIYMS PYPIKWTAII HKWHDEKKNF VYGIGASPAN AVIGHYTQIV
WYKSYRGGCA AAYCPSSAYK YFYVCQYCPA GNIIGKTATP YKSGPPCGDC PSACDNGLCT
NPCTREDEFI NCNDLVKQGC QTDYLKSNCA ASCFCHSEIK