CRVP_PSEAU
ID CRVP_PSEAU Reviewed; 238 AA.
AC Q8AVA4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cysteine-rich venom protein pseudechetoxin;
DE Short=CRVP PsTx;
DE Flags: Precursor;
OS Pseudechis australis (Mulga snake) (King brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX NCBI_TaxID=8670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-35, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12234174; DOI=10.1021/bi026132h;
RA Yamazaki Y., Brown R.L., Morita T.;
RT "Purification and cloning of toxins from elapid venoms that target cyclic
RT nucleotide-gated ion channels.";
RL Biochemistry 41:11331-11337(2002).
RN [2]
RP PROTEIN SEQUENCE OF 28-35 AND 39-57, FUNCTION, AND CHARACTERIZATION.
RC TISSUE=Venom;
RX PubMed=9892706; DOI=10.1073/pnas.96.2.754;
RA Brown R.L., Haley T.L., West K.A., Crabb J.W.;
RT "Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:754-759(1999).
RN [3]
RP FUNCTION.
RX PubMed=14638933; DOI=10.1085/jgp.200308823;
RA Brown R.L., Lynch L.L., Haley T.L., Arsanjani R.;
RT "Pseudechetoxin binds to the pore turret of cyclic nucleotide-gated ion
RT channels.";
RL J. Gen. Physiol. 122:749-760(2003).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=16511147; DOI=10.1107/s1744309105020439;
RA Suzuki N., Yamazaki Y., Fujimoto Z., Morita T., Mizuno H.;
RT "Crystallization and preliminary X-ray diffraction analyses of
RT pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory
RT proteins that target cyclic nucleotide-gated ion channels.";
RL Acta Crystallogr. F 61:750-752(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 28-238, AND DISULFIDE BONDS.
RX PubMed=18931410; DOI=10.1107/s0907444908023512;
RA Suzuki N., Yamazaki Y., Brown R.L., Fujimoto Z., Morita T., Mizuno H.;
RT "Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich
RT secretory proteins that target cyclic nucleotide-gated ion channels:
RT implications for movement of the C-terminal cysteine-rich domain.";
RL Acta Crystallogr. D 64:1034-1042(2008).
CC -!- FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) cyclic
CC nucleotide-gated (CNG) ion channel currents. Does not inhibit retinal
CC (CNGA3) currents. It forms high-affinity contacts with the pore turret
CC region and most likely inhibits CNG channel current by blocking the
CC external entrance to the transmembrane pore. Is really more potent that
CC Pseudecin. Does not affect neither depolarization- nor caffeine-induced
CC contraction arterial smooth muscle. {ECO:0000269|PubMed:12234174,
CC ECO:0000269|PubMed:14638933, ECO:0000269|PubMed:9892706}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=23815.7; Mass_error=109.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12234174};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY072695; AAL65291.1; -; mRNA.
DR PDB; 2DDA; X-ray; 2.25 A; A/B/C/D=28-238.
DR PDBsum; 2DDA; -.
DR AlphaFoldDB; Q8AVA4; -.
DR SMR; Q8AVA4; -.
DR EvolutionaryTrace; Q8AVA4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Metal-binding; Neurotoxin; Secreted; Signal;
KW Toxin; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:12234174,
FT ECO:0000269|PubMed:9892706"
FT /id="PRO_0000006282"
FT CHAIN 28..238
FT /note="Cysteine-rich venom protein pseudechetoxin"
FT /id="PRO_0000006283"
FT DOMAIN 38..164
FT /note="SCP"
FT DOMAIN 200..233
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT DISULFID 75..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 92..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 148..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 184..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 187..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 200..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 209..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT ECO:0000269|PubMed:18931410"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:2DDA"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:2DDA"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2DDA"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:2DDA"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:2DDA"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2DDA"
SQ SEQUENCE 238 AA; 26475 MW; 8BACDDB5647CEDE4 CRC64;
MIAFIVLLSL AAVLQQSSGT ADFASESSNK KNYQKEIVDK HNALRRSVKP TARNMLQMKW
NSRAAQNAKR WANRCTFAHS PPNKRTVGKL RCGENIFMSS QPFPWSGVVQ AWYDEIKNFV
YGIGAKPPGS VIGHYTQVVW YKSYLIGCAS AKCSSSKYLY VCQYCPAGNI RGSIATPYKS
GPPCADCPSA CVNKLCTNPC KRNNDFSNCK SLAKKSKCQT EWIKKKCPAS CFCHNKII
