ID   CRVP5_VARAC             Reviewed;         220 AA.
AC   Q2XXR0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Cysteine-rich venom protein VAR5;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein VAR5;
DE            Short=CRISP-VAR5;
DE   Flags: Precursor; Fragment;
OS   Varanus acanthurus (Ridge-tailed monitor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX   NCBI_TaxID=62035;
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 ryanodine receptors, and potassium channels.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 8 disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; DQ139885; AAZ75591.1; -; mRNA.
DR   AlphaFoldDB; Q2XXR0; -.
DR   SMR; Q2XXR0; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd05383; CAP_CRISP; 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; 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   Calcium channel impairing toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..>220
FT                   /note="Cysteine-rich venom protein VAR5"
FT                   /id="PRO_0000380656"
FT   DOMAIN          41..169
FT                   /note="SCP"
FT   DOMAIN          205..220
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        77..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        95..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        151..167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        189..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        192..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   NON_TER         220
SQ   SEQUENCE   220 AA;  24771 MW;  2A2FC2B7876DFC20 CRC64;
     MILLKLYLTL AAILCQSRGT TSLDLDDLMT TNPEIQNEII NKHNDLRRTV DPPAKNMLKM
     SWDNIIAESA KRAALRCNQN EHTPVSGRTI GGVVCGENYF MSSNPRTWSF GIQSWFDERN
     YFKFGFGPTR AGVMVGHYTQ VVWYKSYKMG CAINLCPNEP LKYFLVCQYC PGGNVVGRKY
     EPYAIGEPCA ACPNNCDNGL CTNPCEHSNQ YINCPDLTKQ