CRVP_SISCA
ID CRVP_SISCA Reviewed; 239 AA.
AC B0VXV6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Cysteine-rich venom protein 2;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein 2;
DE Short=CRISP-2;
DE Flags: Precursor;
OS Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus
OS edwardsii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX NCBI_TaxID=8762;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=18096037; DOI=10.1186/1471-2199-8-115;
RA Pahari S., Mackessy S.P., Kini R.M.;
RT "The venom gland transcriptome of the Desert Massasauga rattlesnake
RT (Sistrurus catenatus edwardsii): towards an understanding of venom
RT composition among advanced snakes (Superfamily Colubroidea).";
RL BMC Mol. Biol. 8:115-115(2007).
CC -!- FUNCTION: Weakly 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; DQ464263; ABG26992.1; -; mRNA.
DR AlphaFoldDB; B0VXV6; -.
DR SMR; B0VXV6; -.
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..19
FT /evidence="ECO:0000250"
FT CHAIN 20..239
FT /note="Cysteine-rich venom protein 2"
FT /id="PRO_0000380663"
FT DOMAIN 38..166
FT /note="SCP"
FT DOMAIN 198..234
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 75..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 92..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 148..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 186..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 189..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 202..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 239 AA; 26542 MW; 91953EBD71514AD2 CRC64;
MIALIVLPIL AAVLQQSSGS VDFDSESPRK PEIQNKIVDL HNSLRRSVNP TASNMLKMEW
YSEAAANAER WAYRCIESHS PRDSRVLEGI KCGENIYMSS VPMKWTEIIH IWHGENKNFK
YGIGADPPNA VTGHYTQIVW YKSYRAGCAA AYCPSLEYSY FYVCQYCPAG NIRGKTATPY
KSGPPCGDCP SACDNGLCTN PCPKKISTQL PRFGPQAGCQ DKQMQSDCSA TCFCQNKII