ID   CRVP_CERRY              Reviewed;         239 AA.
AC   D8VNS1; D8VNS2; D8VNS3; D8VNS4; D8VNS5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Cysteine-rich venom protein;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein;
DE            Short=CRISP;
DE   Flags: Precursor;
OS   Cerberus rynchops (Dog-faced water snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Homalopsidae; Cerberus.
OX   NCBI_TaxID=46267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20158271; DOI=10.1021/pr901044x;
RA   Ompraba G., Chapeaurouge A., Doley R., Devi K.R., Padmanaban P.,
RA   Venkatraman C., Velmurugan D., Lin Q., Kini R.M.;
RT   "Identification of a novel family of snake venom proteins Veficolins from
RT   Cerberus rynchops using a venom gland transcriptomics and proteomics
RT   approach.";
RL   J. Proteome Res. 9:1882-1893(2010).
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; GU065317; ADJ51056.1; -; mRNA.
DR   EMBL; GU065318; ADJ51057.1; -; mRNA.
DR   EMBL; GU065319; ADJ51058.1; -; mRNA.
DR   EMBL; GU065320; ADJ51059.1; -; mRNA.
DR   EMBL; GU065321; ADJ51060.1; -; mRNA.
DR   AlphaFoldDB; D8VNS1; -.
DR   SMR; D8VNS1; -.
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..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..239
FT                   /note="Cysteine-rich venom protein"
FT                   /id="PRO_0000414915"
FT   DOMAIN          37..165
FT                   /note="SCP"
FT   DOMAIN          201..234
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        74..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        91..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        147..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        185..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        210..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        219..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   CONFLICT        23
FT                   /note="Q -> R (in Ref. 1; ADJ51057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="T -> I (in Ref. 1; ADJ51059)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70..239
FT                   /note="Missing (in Ref. 1; ADJ51060)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="F -> L (in Ref. 1; ADJ51058)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  27049 MW;  03B660EBC216AB41 CRC64;
     MIVFILLSLA AVLQQSVADV DFQSESPRRT EKQTEIVDMH NSFRRSVNPT ARNMLKMEWY
     PEAADNAERW AYQCIYDHSA NYERVIGGIQ CGENIYKSSN PRAWSEMIQD WYDEYKNFVY
     GVGANPPGSM IGHYTQIVWY KSYRIGCAAA YCPSYPYNYF YVCQYCPVGN MEGLTATPYT
     SGPTCADCPS HCDDGLCTNP CPINNVFTNC DSLLQQSSCE DSYITTNCGA SCFCQDKII