ID   CRVP1_NAJNA             Reviewed;          33 AA.
AC   P86543;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cysteine-rich venom protein;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein 1 {ECO:0000303|PubMed:20203422};
DE            Short=CRISP1 {ECO:0000303|PubMed:20203422};
DE   AltName: Full=Cysteine-rich secretory protein 2 {ECO:0000303|PubMed:20203422};
DE            Short=CRISP2 {ECO:0000303|PubMed:20203422};
DE   AltName: Full=Najanajin;
DE   Flags: Fragment;
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom {ECO:0000269|PubMed:20203422};
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12.
RC   TISSUE=Venom;
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).
CC   -!- FUNCTION: Blocks contraction of smooth muscle elicited by high
CC       potassium-induced depolarization, but does not block caffeine-
CC       stimulated contraction. May target voltage-gated calcium channels on
CC       smooth muscle (Cav) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20203422}.
CC   -!- PTM: Contains 8 disulfide bonds. {ECO:0000250|UniProtKB:P84808}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000255}.
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DR   AlphaFoldDB; P86543; -.
DR   SMR; P86543; -.
DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Reference proteome; Secreted;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   CHAIN           1..>33
FT                   /note="Cysteine-rich venom protein"
FT                   /id="PRO_0000394691"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        1
FT                   /note="N -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         33
FT                   /evidence="ECO:0000303|PubMed:20203422"
SQ   SEQUENCE   33 AA;  3910 MW;  6A8662439E399A54 CRC64;
     NVDFNSESTR RKKKQKEIVD LHNSLRRRVS PTA