CRVP_TRIST
ID CRVP_TRIST Reviewed; 233 AA.
AC P60623;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein;
DE AltName: Full=Stecrisp;
DE Flags: Precursor; Fragment;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Guo M., Teng M.-K., Niu L.-W.;
RT "Purification and molecular cloning of a novel snake venom protein that
RT belongs to CRISP family.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 13-233, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=15596436; DOI=10.1074/jbc.m413566200;
RA Guo M., Teng M.-K., Niu L.-W., Liu Q., Huang Q., Hao Q.;
RT "Crystal structure of the cysteine-rich secretory protein stecrisp reveals
RT that the cysteine-rich domain has a K+ channel inhibitor-like fold.";
RL J. Biol. Chem. 280:12405-12412(2005).
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY423708; AAQ98964.1; -; mRNA.
DR PDB; 1RC9; X-ray; 1.60 A; A=13-233.
DR PDBsum; 1RC9; -.
DR AlphaFoldDB; P60623; -.
DR SMR; P60623; -.
DR EvolutionaryTrace; P60623; -.
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 1: Evidence at protein level;
KW 3D-structure; Calcium channel impairing toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL <1..12
FT /evidence="ECO:0000255"
FT CHAIN 13..233
FT /note="Cysteine-rich venom protein"
FT /id="PRO_0000006290"
FT DOMAIN 31..159
FT /note="SCP"
FT DOMAIN 195..228
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 68..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 85..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 141..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 179..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 182..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 195..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 204..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT DISULFID 213..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15596436"
FT NON_TER 1
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:1RC9"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1RC9"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 149..161
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1RC9"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:1RC9"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1RC9"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:1RC9"
SQ SEQUENCE 233 AA; 26294 MW; A9E326F5242DD249 CRC64;
PILAAVLQQS SGNVDFDSES PRKPEIQNEI VDLHNSLRRS VNPTASNMLR MEWYPEAADN
AERWAYRCIE SHSSYESRVI EGIKCGENIY MSPYPMKWTD IIHAWHDEYK DFKYGVGADP
PNAVTGHYTQ IVWYKSYRIG CAAAYCPSSP YSYFFVCQYC PAGNFIGKTA TPYTSGTPCG
DCPSDCDNGL CTNPCTRENK FTNCNTMVQQ SSCQDNYMKT NCPASCFCQN KII
