ID   CRVP_OXYMI              Reviewed;         238 AA.
AC   Q3SB06; Q2XXP9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Cysteine-rich venom protein pseudechetoxin-like;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein OXY1;
DE            Short=CRISP-OXY1;
DE   Flags: Precursor;
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=111177;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16292255; DOI=10.1038/nature04328;
RA   Fry B.G., Vidal N., Norman J.A., Vonk F.J., Scheib H., Ramjan S.F.R.,
RA   Kuruppu S., Fung K., Blair Hedges S., Richardson M.K., Hodgson W.C.,
RA   Ignjatovic V., Summerhayes R., Kochva E.;
RT   "Early evolution of the venom system in lizards and snakes.";
RL   Nature 439:584-588(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; DQ084036; AAZ38981.1; -; mRNA.
DR   EMBL; DQ139896; AAZ75602.1; -; mRNA.
DR   AlphaFoldDB; Q3SB06; -.
DR   SMR; Q3SB06; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   PROPEP          20..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380667"
FT   CHAIN           29..238
FT                   /note="Cysteine-rich venom protein pseudechetoxin-like"
FT                   /id="PRO_5000140333"
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"
FT   CONFLICT        204..206
FT                   /note="DDL -> NDF (in Ref. 2; AAZ75602)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="P -> A (in Ref. 2; AAZ75602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   238 AA;  26415 MW;  345712EFA8B0C8BB CRC64;
     MIAFIVLLSL AAVLQQSSGT VDFASESSNK KDYRKEIVDK HNDLRRSVKP TARNMLQMKW
     NSRAAQNAKR WANRCTFAHS PPYTRTVGKL RCGENIFMSS QPFAWSGVVQ AWYDEVKKFV
     YGIGAKPPSS VIGHYTQVVW YKSHLLGCAS AKCSSTKYLY VCQYCPAGNI IGSIATPYKS
     GPPCGDCPSA CDNGLCTNPC KHNDDLSNCK PLAKKSKCQT EWIKSKCPAT CFCRTEII