CRVP1_PSEPL
ID CRVP1_PSEPL Reviewed; 239 AA.
AC Q2XXQ3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Cysteine-rich venom protein ENH1;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein ENH1;
DE Short=CRISP-ENH1;
DE Flags: Precursor;
OS Pseudoferania polylepis (Macleay's water snake) (Enhydris polylepis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Homalopsidae; Pseudoferania.
OX NCBI_TaxID=338839;
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; DQ139892; AAZ75598.1; -; mRNA.
DR AlphaFoldDB; Q2XXQ3; -.
DR SMR; Q2XXQ3; -.
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 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; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..239
FT /note="Cysteine-rich venom protein ENH1"
FT /id="PRO_0000380643"
FT DOMAIN 37..165
FT /note="SCP"
FT DOMAIN 201..234
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"
SQ SEQUENCE 239 AA; 26994 MW; 0CB8486F227E8D5E CRC64;
MIVFILLSLA AVLQQFVADV NFESESPRRT EKQTEIVDMH NSFRRSVNPT ARNMLKMEWY
PEAADNAERW AYQCIYDHSA NSERVIGGIQ CGENIYKSSN PRAWTEIIQS WYDEIQNFEY
GVGANPPGSV IGHYTQIVWY KSYRIGCAAA YCPSYPYNYF YVCQYCPTGN MEGLTATPYT
SGPTCADCPS HCDDGLCTNP CPITNTFTNC DSLLQQNSCE DSYIKTNCGA SCFCQDKII