CRVP_PROFL
ID CRVP_PROFL Reviewed; 240 AA.
AC Q8JI39;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Cysteine-rich venom protein triflin;
DE Short=CRVP;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12047379; DOI=10.1046/j.1432-1033.2002.02940.x;
RA Yamazaki Y., Koike H., Sugiyama Y., Motoyoshi K., Wada T., Hishinuma S.,
RA Mita M., Morita T.;
RT "Cloning and characterization of novel snake venom proteins that block
RT smooth muscle contraction.";
RL Eur. J. Biochem. 269:2708-2715(2002).
RN [2]
RP PROTEIN SEQUENCE OF 20-49, AND SUBUNIT WITH SSP-2.
RC TISSUE=Venom;
RX PubMed=17543280; DOI=10.1016/j.bbrc.2007.05.091;
RA Aoki N., Sakiyama A., Deshimaru M., Terada S.;
RT "Identification of novel serum proteins in a Japanese viper: homologs of
RT mammalian PSP94.";
RL Biochem. Biophys. Res. Commun. 359:330-334(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-240, AND DISULFIDE BONDS.
RX PubMed=15953617; DOI=10.1016/j.jmb.2005.05.020;
RA Shikamoto Y., Suto K., Yamazaki Y., Morita T., Mizuno H.;
RT "Crystal structure of a CRISP family Ca2+ -channel blocker derived from
RT snake venom.";
RL J. Mol. Biol. 350:735-743(2005).
CC -!- FUNCTION: Blocks contraction of smooth muscle elicited by high
CC potassium-induced depolarization (PubMed:12047379). May target voltage-
CC gated calcium channels (Cav) on smooth muscle.
CC {ECO:0000269|PubMed:12047379}.
CC -!- SUBUNIT: Forms a stable, non-covalent complex with SSP-2.
CC {ECO:0000269|PubMed:17543280}.
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; AF384219; AAM45665.1; -; mRNA.
DR PDB; 1WVR; X-ray; 2.40 A; A=20-240.
DR PDB; 6IMF; X-ray; 2.30 A; A=20-240.
DR PDBsum; 1WVR; -.
DR PDBsum; 6IMF; -.
DR AlphaFoldDB; Q8JI39; -.
DR SMR; Q8JI39; -.
DR TCDB; 8.B.9.1.1; the triflin toxin (triflin or crisp) family.
DR EvolutionaryTrace; Q8JI39; -.
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; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:17543280"
FT CHAIN 20..240
FT /note="Cysteine-rich venom protein triflin"
FT /id="PRO_0000006287"
FT DOMAIN 39..166
FT /note="SCP"
FT DOMAIN 202..235
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 75..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 92..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 148..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 186..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 189..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 202..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 211..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT DISULFID 220..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:15953617"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 156..168
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:1WVR"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6IMF"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6IMF"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6IMF"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:6IMF"
SQ SEQUENCE 240 AA; 26752 MW; 1EE3C9C426D974A0 CRC64;
MIAFIVLPIL AAVLQQSSGN VDFDSESPRK PEIQNEIIDL HNSLRRSVNP TASNMLKMEW
YPEAAANAER WAYRCIESHS SRDSRVIGGI KCGENIYMAT YPAKWTDIIH AWHGEYKDFK
YGVGAVPSDA VIGHYTQIVW YKSYRAGCAA AYCPSSKYSY FYVCQYCPAG NIIGKTATPY
KSGPPCGDCP SDCDNGLCTN PCTRENEFTN CDSLVQKSSC QDNYMKSKCP ASCFCQNKII
