CRVP_TRIBI
ID CRVP_TRIBI Reviewed; 236 AA.
AC Q2XXP4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Cysteine-rich venom protein TRI1;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein TRI1;
DE Short=CRISP-TRI1;
DE Flags: Precursor; Fragment;
OS Trimorphodon biscutatus (Western lyre snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Trimorphodon.
OX NCBI_TaxID=338818;
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; DQ139901; AAZ75607.1; -; mRNA.
DR AlphaFoldDB; Q2XXP4; -.
DR SMR; Q2XXP4; -.
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..>236
FT /note="Cysteine-rich venom protein TRI1"
FT /id="PRO_0000380648"
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 210..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT NON_TER 236
SQ SEQUENCE 236 AA; 26648 MW; 2F34ABB3DCCE461A CRC64;
MIVFILLSLA AVLEQSFGNV DFNSESPRRP EKQKEIVDRH NSFRRSVRPT ASNMLKMEWY
SEAASNAERW AYRCNLGHSP DSSRILDGIK CGENIYMSSN PRAWTEILQL WYDEYKNFVY
GVGANPPGSV TGHFSQMVWY KSYRIGCAAA YCPSSGYSYF YVCQYCPIGN IEGSTATPYK
SGPTCGDCPS ACDNGLCTNP CLREDKFTNC KSLVQQNSCQ HDWTRKNCPA TCFCHN