CRVPB_VARVA
ID CRVPB_VARVA Reviewed; 242 AA.
AC Q2XXP1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Cysteine-rich venom protein VAR11;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein VAR11;
DE Short=CRISP-VAR11;
DE Flags: Precursor;
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 -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; DQ139904; AAZ75610.1; -; mRNA.
DR AlphaFoldDB; Q2XXP1; -.
DR SMR; Q2XXP1; -.
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..242
FT /note="Cysteine-rich venom protein VAR11"
FT /id="PRO_0000380662"
FT DOMAIN 41..169
FT /note="SCP"
FT DOMAIN 205..237
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 DISULFID 205..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 214..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 223..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 242 AA; 26944 MW; EB5B10FAA2292954 CRC64;
MILLKLYLTL AAILCQSRGM TSLDLDDLMT TNPEIQNEII NKHNDLRRTV DPPAKNMLKM
SWDNIIAESA KRAALRCNYK EHTSIAERTI GGVVCGENHF MSSNPRTWSS SIQSWFDERN
SFMFGFGPTI PGVMVGHYTQ VVWYKSYKVG CAINLCPAQS LKYFQVCQYC PGGNVAGRKY
EPYTIGEPCA ACPKDCDNGL CTNPCAYNDD YTSCPDLTKQ VGCNHPVTAN CKASCQCTTE
IQ