CRVP_DRYCN
ID CRVP_DRYCN Reviewed; 238 AA.
AC F8J2D4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein;
DE Short=CRISP;
DE Flags: Precursor;
OS Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Drysdalia.
OX NCBI_TaxID=66186;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21133350; DOI=10.1021/pr1008916;
RA Chatrath S.T., Chapeaurouge A., Lin Q., Lim T.K., Dunstan N., Mirtschin P.,
RA Kumar P.P., Kini R.M.;
RT "Identification of novel proteins from the venom of a cryptic snake
RT Drysdalia coronoides by a combined transcriptomics and proteomics
RT approach.";
RL J. Proteome Res. 10:739-750(2011).
CC -!- FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) CNG channel
CC currents. Does not affect neither depolarization- nor caffeine-induced
CC contraction of 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; FJ752452; ACR78474.1; -; mRNA.
DR AlphaFoldDB; F8J2D4; -.
DR SMR; F8J2D4; -.
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 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:0000255"
FT CHAIN 20..238
FT /note="Cysteine-rich venom protein"
FT /id="PRO_0000425514"
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; 26388 MW; B2634E97C7F6124B CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK KDYRKEIVDK HNALRRSVKP TARNMLQMEW
NSHAAQNAKR WADRCTFAHS PPHTRTVGQL RCGENIFMSS QPFAWSGVVQ AWYDEVKKFV
YGIGAKPPGS VIGHYTQVVW YKSHLLGCAS AKCSSTKYLY VCQYCPAGNI RGSIATPYKS
GPTCGDCPSA CVNGLCTNPC KYEDAFTNCN ELAKETKCKT EWIKSKCPAT CFCHTEII