CRVP1_DISTY
ID CRVP1_DISTY Reviewed; 237 AA.
AC Q2XXQ6;
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 DIS1;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein DIS1;
DE Short=CRISP-DIS1;
DE Flags: Precursor;
OS Dispholidus typus (Boomslang) (Bucephalus typus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Dispholidus.
OX NCBI_TaxID=46295;
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: 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; DQ139889; AAZ75595.1; -; mRNA.
DR AlphaFoldDB; Q2XXQ6; -.
DR SMR; Q2XXQ6; -.
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..237
FT /note="Cysteine-rich venom protein DIS1"
FT /id="PRO_0000380649"
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 201..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 237 AA; 26723 MW; 55C1FEC5818F3299 CRC64;
MFVFILLSLA AVLQQSFGNV DFNSESPRIK AKQREIVDKH NAFRRSVRPT ASNMLRMEWY
SEAASNAERW AYRCILDHSP KTSRILNGIK CGENIYMSSI PMTWIDIIKL WHDEYKNFIY
GVGANPPGSV IGHYTQIVWY KSYRVGCAAS YCPPSSYNYF YVCQYCPAGN FAGLTATPYK
SGPTCGDCPS ACDNGLCTNP CSREDVFMNC KSLVAQSNCQ DDYIRKNCPA TCFCPNK
