CRVP_VIPBE
ID CRVP_VIPBE Reviewed; 239 AA.
AC B7FDI1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE Flags: Precursor;
OS Vipera berus (Common European adder) (Coluber berus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=31155;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19041663; DOI=10.1016/j.toxicon.2008.11.001;
RA Ramazanova A.S., Starkov V.G., Osipov A.V., Ziganshin R.H., Filkin S.Y.,
RA Tsetlin V.I., Utkin Y.N.;
RT "Cysteine-rich venom proteins from the snakes of Viperinae subfamily
RT - molecular cloning and phylogenetic relationship.";
RL Toxicon 53:162-168(2009).
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 (By similarity). {ECO:0000250}.
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; AM937250; CAP74089.1; -; mRNA.
DR AlphaFoldDB; B7FDI1; -.
DR SMR; B7FDI1; -.
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; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..239
FT /note="Cysteine-rich venom protein"
FT /id="PRO_5000417203"
FT DOMAIN 39..166
FT /note="SCP"
FT DOMAIN 202..234
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 75..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 92..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 148..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 186..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 189..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 202..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 211..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 239 AA; 26509 MW; AF3A6D61374A3EB9 CRC64;
MIAFLVLPIL AAVLQQSSGN VDFDSESPRK PEIQNEIIDL HNSLRRSVNP TASNMLKMEW
YPEAAANAER WAFRCILSHS PRDSRVIGGI KCGENIYMST SPMKWTAIIH EWHGEEKDFV
YGQGASPANA VVGHYTQIVW YKSYRSGCAA AYCPSSEYKY FYVCQYCPAG NMQGKTATPY
TSGPPCGDCP SACDNGLCTN PCTHEDKFTN CKDLVKQGCN NNYLKTNCPA SCSCHNEII