ID   CRVP1_NAJKA             Reviewed;         239 AA.
AC   P84805; B5THG8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Cysteine-rich venom protein kaouthin-1;
DE   AltName: Full=Cysteine-rich venom protein 25;
DE            Short=CRVP-25k;
DE   Flags: Precursor;
OS   Naja kaouthia (Monocled cobra) (Naja siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-64; 175-180 AND
RP   207-237.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19106157; DOI=10.1093/jb/mvn174;
RA   Matsunaga Y., Yamazaki Y., Hyodo F., Sugiyama Y., Nozaki M., Morita T.;
RT   "Structural divergence of cysteine-rich secretory proteins in snake
RT   venoms.";
RL   J. Biochem. 145:365-375(2009).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 19-43, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:15670767};
RX   PubMed=15670767; DOI=10.1016/j.bbrc.2004.12.154;
RA   Osipov A.V., Levashov M.Y., Tsetlin V.I., Utkin Y.N.;
RT   "Cobra venom contains a pool of cysteine-rich secretory proteins.";
RL   Biochem. Biophys. Res. Commun. 328:177-182(2005).
CC   -!- FUNCTION: Inhibits calcium-activated potassium channels (KCa), voltage-
CC       gated potassium channel (Kv), and the calcium release channel/ryanodine
CC       receptor (RyR). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15670767}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15670767}.
CC   -!- MASS SPECTROMETRY: Mass=24953; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15670767};
CC   -!- MISCELLANEOUS: Not toxic when administered to cockroaches and mice at
CC       doses up to 5 nmol/g. {ECO:0000269|PubMed:15670767}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000255}.
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DR   EMBL; EU938339; ACH73167.1; -; mRNA.
DR   AlphaFoldDB; P84805; -.
DR   SMR; P84805; -.
DR   PRIDE; P84805; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
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   Calcium channel impairing toxin;
KW   Calcium-activated potassium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin;
KW   Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW   Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:15670767,
FT                   ECO:0000269|PubMed:19106157"
FT   CHAIN           19..239
FT                   /note="Cysteine-rich venom protein kaouthin-1"
FT                   /id="PRO_5000399104"
FT   DOMAIN          37..165
FT                   /note="SCP"
FT   DOMAIN          201..234
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        74..152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        91..166
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        147..163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        185..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        201..234
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        210..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        219..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   239 AA;  26846 MW;  CACB1E01F2A04554 CRC64;
     MIAFSLLCLA AVLRQSFGNV DFNSESTRRK KKQKEIVDLH NSLRRRVSPT ASNMLKMEWY
     PEAASNAERW ANTCSLNHSP DNLRVLEGIQ CGESIYMSSN ARTWTEIIHL WHDEYKNFVY
     GVGANPPGSV TGHYTQIVWY QTYRAGCAVS YCPSSAWSYF YVCQYCPSGN FQGKTATPYK
     LGPPCGDCPS ACDNGLCTNP CTIYNKLTNC DSLLKQGSCQ DDWIKSNCPA SCFCRNKII