CRVP_DEMVE
ID CRVP_DEMVE Reviewed; 238 AA.
AC A6MFK9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein;
DE Short=CRISP;
DE Flags: Precursor;
OS Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX NCBI_TaxID=412038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=17608513; DOI=10.1021/pr0701613;
RA St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Diversity of toxic components from the venom of the evolutionarily
RT distinct black whip snake, Demansia vestigiata.";
RL J. Proteome Res. 6:3093-3107(2007).
CC -!- FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) cyclic
CC nucleotide-gated (CNG) ion channel currents. Does not inhibit retinal
CC (CNGA3) currents. It forms high-affinity contacts with the pore turret
CC region and most likely inhibits CNG channel current by blocking the
CC external entrance to the transmembrane pore. Does not affect neither
CC depolarization- nor caffeine-induced contraction arterial smooth muscle
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; DQ917520; ABK63549.1; -; mRNA.
DR AlphaFoldDB; A6MFK9; -.
DR SMR; A6MFK9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion 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 Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000250"
FT /id="PRO_0000380669"
FT CHAIN 28..238
FT /note="Cysteine-rich venom protein"
FT /id="PRO_5000254113"
FT DOMAIN 39..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; 26470 MW; DE3ECA461D23D41F CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK GENQKQIVKK HNALRRSVKP PARNMLQMEW
NSRAAQNAKR WAERCSFTHS PPSLRTVGKL RCGENLLQSS QPLPWSKVVQ AWYDENKNFV
YGIGAKPPGS VVGHYTQVVW YKSRLLGCAS VKCSPTKYLY VCQYCPAGNI IGSQATPYKS
GPRCADCPSA CVKGLCTNPC KREDDYSNCK SLAEKNKCME EWMKSKCPAS CFCHNKII