ID   CRVP_PSETE              Reviewed;         238 AA.
AC   Q3SB05;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Cysteine-rich venom protein pseudechetoxin-like;
DE            Short=CRVP;
DE   Flags: Precursor;
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA   St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT   "Identification and analysis of venom gland-specific genes from the coastal
RT   taipan (Oxyuranus scutellatus) and related species.";
RL   Cell. Mol. Life Sci. 62:2679-2693(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 219-238 AND 227-234.
RC   TISSUE=Venom;
RX   PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA   Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA   Lavin M.F.;
RT   "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT   textilis.";
RL   Mol. Cell. Proteomics 5:379-389(2006).
CC   -!- FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) CNG channel
CC       currents. Does not affect neither depolarization- nor caffeine-induced
CC       contraction of 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; DQ084037; AAZ38982.1; -; mRNA.
DR   AlphaFoldDB; Q3SB05; -.
DR   SMR; Q3SB05; -.
DR   Ensembl; ENSPTXT00000009319; ENSPTXP00000009010; ENSPTXG00000006481.
DR   GeneTree; ENSGT00940000162013; -.
DR   OMA; KCEKATG; -.
DR   Proteomes; UP000472273; Unplaced.
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: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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   PROPEP          20..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380666"
FT   CHAIN           29..238
FT                   /note="Cysteine-rich venom protein pseudechetoxin-like"
FT                   /id="PRO_5000140334"
FT   DOMAIN          38..164
FT                   /note="SCP"
FT   DOMAIN          200..233
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        75..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        92..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        148..162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        184..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        187..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        200..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        209..227
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        218..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   238 AA;  26429 MW;  84831E07A345EC10 CRC64;
     MIAFLVLLSL AAVLQQSSGT VDFASESSNK NDYQKEIVDK HNDLRRSVKP TARNMLQMKW
     NSRAAQNAKR WANRCTFAHS PPYTRTVGKL RCGENIFMSS QPFAWSGVVQ AWYDEVKKFV
     YGIGAKPPSS VTGHYTQVVW YKSHLLGCAS AKCSSTKYLY VCQYCPAGNI VGSIATPYKS
     GPPCGDCPSA CDNGLCTNPC KHNDDLSNCK TLVKKHKCQT EWIKSKCPAT CFCRTEII