CRVP1_NAJAT
ID CRVP1_NAJAT Reviewed; 239 AA.
AC Q7T1K6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cysteine-rich venom protein natrin-1;
DE AltName: Full=Cysteine-rich venom protein 1;
DE AltName: Full=NA-CRVP1;
DE AltName: Full=Protein G2a;
DE Flags: Precursor;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J., Teng M., Niu L.;
RT "Purification and cloning of toxins of CRISP family from Naja atra
RT venoms.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 19-60.
RC TISSUE=Venom;
RX PubMed=14529736; DOI=10.1016/s0041-0101(03)00234-4;
RA Jin Y., Lu Q., Zhou X., Zhu S., Li R., Wang W., Xiong Y.;
RT "Purification and cloning of cysteine-rich proteins from Trimeresurus
RT jerdonii and Naja atra venoms.";
RL Toxicon 42:539-547(2003).
RN [3]
RP PROTEIN SEQUENCE OF 19-43, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=15581679; DOI=10.1016/j.toxicon.2004.09.002;
RA Chang L.-S., Liou J.-C., Lin S.-R., Cheng Y.-C.;
RT "Purification and characterization of Taiwan cobra venom proteins with weak
RT toxicity.";
RL Toxicon 45:21-25(2005).
RN [4]
RP PROTEIN SEQUENCE OF 19-38, X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF
RP 19-239, FUNCTION, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=17070778; DOI=10.1016/j.bbrc.2006.10.067;
RA Wang F., Li H., Liu M.N., Song H., Han H.-M., Wang Q.-L., Yin C.-C.,
RA Zhou Y.-C., Qi Z., Shu Y.-Y., Lin Z.-J., Jiang T.;
RT "Structural and functional analysis of natrin, a venom protein that targets
RT various ion channels.";
RL Biochem. Biophys. Res. Commun. 351:443-448(2006).
RN [5]
RP FUNCTION.
RX PubMed=18658224; DOI=10.1529/biophysj.108.137224;
RA Zhou Q., Wang Q.-L., Meng X., Strauss J., Shu Y., Jiang T., Wagenknecht T.,
RA Yin C.-C., Sui S.-F., Liu Z.;
RT "Structural and functional characterization of ryanodine receptor-natrin
RT toxin interaction.";
RL Biophys. J. 95:4289-4299(2008).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 19-239, AND DISULFIDE BONDS.
RX PubMed=15388950; DOI=10.1107/s0907444904019766;
RA Wang Y.-L., Goh K.X., Wu W.G., Chen C.J.;
RT "Purification, crystallization and preliminary X-ray crystallographic
RT analysis of a cysteine-rich secretory protein (CRISP) from Naja atra
RT venom.";
RL Acta Crystallogr. D 60:1912-1915(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 19-239, DISULFIDE BONDS, AND
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=16042391; DOI=10.1021/bi050614m;
RA Wang J., Shen B., Guo M., Lou X., Duan Y., Cheng X.P., Teng M., Niu L.,
RA Liu Q., Huang Q., Hao Q.;
RT "Blocking effect and crystal structure of natrin toxin, a cysteine-rich
RT secretory protein from Naja atra venom that targets the BKCa channel.";
RL Biochemistry 44:10145-10152(2005).
CC -!- FUNCTION: Inhibits calcium-activated potassium channels
CC (KCa1.1/KCNMA1), voltage-gated potassium channel Kv1.3/KCNA3, and the
CC calcium release channel/ryanodine receptor (RyR). Binds specifically to
CC type 1 RyR (RyR1) from skeletal muscle. Inhibit both the binding of
CC ryanodine to RyR1, and RyR1's calcium-channel activity. Inhibits
CC carbachol-induced muscle contraction and weakly blocks muscle
CC contraction evoked by potassium. {ECO:0000269|PubMed:15581679,
CC ECO:0000269|PubMed:16042391, ECO:0000269|PubMed:17070778,
CC ECO:0000269|PubMed:18658224}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=24937; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15581679};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY324325; AAP85301.1; -; mRNA.
DR PDB; 1XTA; X-ray; 1.58 A; A/B=19-239.
DR PDB; 1XX5; X-ray; 2.40 A; A/B/C=19-239.
DR PDB; 2GIZ; X-ray; 1.68 A; A/B=19-239.
DR PDB; 3MZ8; X-ray; 2.70 A; A/B=19-239.
DR PDBsum; 1XTA; -.
DR PDBsum; 1XX5; -.
DR PDBsum; 2GIZ; -.
DR PDBsum; 3MZ8; -.
DR AlphaFoldDB; Q7T1K6; -.
DR SMR; Q7T1K6; -.
DR TCDB; 8.B.9.1.2; the triflin toxin (triflin or crisp) family.
DR PRIDE; Q7T1K6; -.
DR EvolutionaryTrace; Q7T1K6; -.
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:0015459; F:potassium 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 3D-structure; 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:14529736,
FT ECO:0000269|PubMed:15581679, ECO:0000269|PubMed:17070778"
FT CHAIN 19..239
FT /note="Cysteine-rich venom protein natrin-1"
FT /id="PRO_0000006279"
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 DISULFID 91..166
FT DISULFID 147..163
FT DISULFID 185..192
FT DISULFID 188..197
FT DISULFID 201..234
FT DISULFID 210..228
FT DISULFID 219..232
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1XTA"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1XTA"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 155..167
FT /evidence="ECO:0007829|PDB:1XTA"
FT TURN 172..176
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1XTA"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3MZ8"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:1XTA"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:1XTA"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1XTA"
SQ SEQUENCE 239 AA; 26882 MW; 70F34EED0391BF26 CRC64;
MIAFSLLCFA AVLQQSFGNV DFNSESTRRK KKQKEIVDLH NSLRRRVSPT ASNMLKMEWY
PEAASNAERW ANTCSLNHSP DNLRVLEGIQ CGESIYMSSN ARTWTEIIHL WHDEYKNFVY
GVGANPPGSV TGHYTQIVWY QTYRAGCAVS YCPSSAWSYF YVCQYCPSGN FQGKTATPYK
LGPPCGDCPS ACDNGLCTNP CTIYNKLTNC DSLLKQSSCQ DDWIKSNCPA SCFCRNKII
