CRVP_PSEPO
ID CRVP_PSEPO Reviewed; 238 AA.
AC Q8AVA3;
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 pseudecin;
DE Short=CRVP Pdc;
DE Flags: Precursor;
OS Pseudechis porphyriacus (Red-bellied black snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX NCBI_TaxID=8671;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-34, 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 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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-238 ALONE AND IN COMPLEX WITH
RP ZINC, ZINC BINDING SITES, 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) CNG channel
CC currents. Is really less potent that Pseudechetoxin. Does not affect
CC neither depolarization- nor caffeine-induced contraction of smooth
CC muscle. {ECO:0000269|PubMed:12234174}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12234174}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:12234174}.
CC -!- MASS SPECTROMETRY: Mass=23651.9; Mass_error=82.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12234174};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY072696; AAL65292.1; -; mRNA.
DR PDB; 2DDB; X-ray; 1.90 A; A/B/C/D=29-238.
DR PDB; 2EPF; X-ray; 2.30 A; A/B/C/D=29-238.
DR PDBsum; 2DDB; -.
DR PDBsum; 2EPF; -.
DR AlphaFoldDB; Q8AVA3; -.
DR SMR; Q8AVA3; -.
DR PRIDE; Q8AVA3; -.
DR EvolutionaryTrace; Q8AVA3; -.
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..28
FT /evidence="ECO:0000269|PubMed:12234174"
FT /id="PRO_0000006284"
FT CHAIN 29..238
FT /note="Cysteine-rich venom protein pseudecin"
FT /evidence="ECO:0000305|PubMed:12234174"
FT /id="PRO_0000006285"
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:0000269|PubMed:18931410"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18931410"
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..45
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:2DDB"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 105..113
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:2DDB"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2DDB"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:2DDB"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:2DDB"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2EPF"
SQ SEQUENCE 238 AA; 26452 MW; 0EE4018E1274D85B CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK KNYQKEIVDK HNALRRSVKP TARNMLQMKW
NSHAAQNAKR WADRCTFAHS PPNTRTVGKL RCGENIFMSS QPFPWSGVVQ AWYDEIKNFV
YGIGAKPPGS VIGHYTQVVW YKSHLIGCAS AKCSSSKYLY VCQYCPAGNI RGSIATPYKS
GPPCADCPSA CVNRLCTNPC NYNNDFSNCK SLAKKSKCQT EWIKKKCPAS CFCHNKII
