ID   CRVP_CAURH              Reviewed;         116 AA.
AC   A7X4T8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Cysteine-rich venom protein Cau1;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein Cau1;
DE            Short=CRISP-Cau1;
DE   Flags: Fragment;
OS   Causus rhombeatus (Rhombic night adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Causus.
OX   NCBI_TaxID=44735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17855442; DOI=10.1074/mcp.m700094-mcp200;
RA   Fry B.G., Scheib H., van der Weerd L., Young B., McNaughtan J.,
RA   Ramjan S.F.R., Vidal N., Poelmann R.E., Norman J.A.;
RT   "Evolution of an arsenal: structural and functional diversification of the
RT   venom system in the advanced snakes (Caenophidia).";
RL   Mol. Cell. Proteomics 7:215-246(2008).
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; EU029755; ABU68555.1; -; mRNA.
DR   AlphaFoldDB; A7X4T8; -.
DR   SMR; A7X4T8; -.
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; 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; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10334; PTHR10334; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
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   Calcium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   CHAIN           <1..116
FT                   /note="Cysteine-rich venom protein Cau1"
FT                   /id="PRO_0000380642"
FT   DOMAIN          4..42
FT                   /note="SCP"
FT   DOMAIN          78..111
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        24..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        62..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        65..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        87..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        96..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   NON_TER         1
SQ   SEQUENCE   116 AA;  12784 MW;  7D7876F6439E22AF CRC64;
     ANPSYAVVGH YTQIVWYKSD RIGCAAAYCP SSVYNYFYVC QYCPAGNFAG RTATPYKSGP
     PCGDCPSACD NGLCTNPCRV EDEFINCKDM AESRDCQDNY MMTNCAAFCS CHNEII