ID   CRVP_ERYPO              Reviewed;         233 AA.
AC   Q2XXQ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Cysteine-rich venom protein LIO1;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein LIO1;
DE            Short=CRISP-LIO1;
DE   Flags: Precursor; Fragment;
OS   Erythrolamprus poecilogyrus (Water snake) (Liophis poecilogyrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Erythrolamprus.
OX   NCBI_TaxID=338838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16292255; DOI=10.1038/nature04328;
RA   Fry B.G., Vidal N., Norman J.A., Vonk F.J., Scheib H., Ramjan S.F.R.,
RA   Kuruppu S., Fung K., Blair Hedges S., Richardson M.K., Hodgson W.C.,
RA   Ignjatovic V., Summerhayes R., Kochva E.;
RT   "Early evolution of the venom system in lizards and snakes.";
RL   Nature 439:584-588(2006).
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; DQ139895; AAZ75601.1; -; mRNA.
DR   AlphaFoldDB; Q2XXQ0; -.
DR   SMR; Q2XXQ0; -.
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   2: Evidence at transcript 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..>233
FT                   /note="Cysteine-rich venom protein LIO1"
FT                   /id="PRO_0000380646"
FT   DOMAIN          37..165
FT                   /note="SCP"
FT   DOMAIN          201..233
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   NON_TER         233
SQ   SEQUENCE   233 AA;  26528 MW;  B6E9F278123E23DB CRC64;
     MIVFILLSFA AVLQQSFGRI DIDSQSTRRP EIQNLIVDTH NSYRRSVSPT ATNMLKMEWY
     PEAAANAERW AYQCVYDHSQ KYERVLDGIQ CGENIYMYSE FRPWTEVMQS WYDEYRNFIF
     GVGAHPANAL IGHYTQIVWY KSYRVGCAIA NCPSYPYNYF YVCQYCPAGN FGGQTATPYN
     SGTTCADCPS ACDNGLCTNP CTSENVFTNC NDMVKESGCQ DERMKSICPA SCF