ID   CRVPA_VARVA             Reviewed;         231 AA.
AC   Q2XXP2;
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 VAR10;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein VAR10;
DE            Short=CRISP-VAR10;
DE   Flags: Precursor; Fragment;
OS   Varanus varius (Lace monitor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Paleoanguimorpha; Varanoidea; Varanidae; Varanus.
OX   NCBI_TaxID=8559;
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; DQ139903; AAZ75609.1; -; mRNA.
DR   AlphaFoldDB; Q2XXP2; -.
DR   SMR; Q2XXP2; -.
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; 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; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..>231
FT                   /note="Cysteine-rich venom protein VAR10"
FT                   /id="PRO_0000380661"
FT   DOMAIN          41..169
FT                   /note="SCP"
FT   DOMAIN          205..231
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        214..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   NON_TER         231
SQ   SEQUENCE   231 AA;  25880 MW;  922E1C8CD1F3B595 CRC64;
     MILLKLYLTL AAILCQSRGM TSLDLDDLMT TNPEIQNEII NKHNDLRRTV DPPAKNMLKM
     SWDNIIAESA KRAALRCNYK EHTSIAERTI GGVVCGENYF MSSNPRTWSS SIQSWFDERN
     NFMFGFGPTI PGVMVGHYTQ VVWYKSYKVG CAINLCPAQS LKYFQVCQYC PGGNVAGRKY
     EPYTIGEPCA ARPKDCDNGL CTNPCAYNDD YTSCPDLTKQ VGCHHPVTAN C