CRVP2_NAJAT
ID CRVP2_NAJAT Reviewed; 238 AA.
AC Q7ZZN8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cysteine-rich venom protein natrin-2;
DE AltName: Full=Cysteine-rich venom protein 2;
DE AltName: Full=NA-CRVP2;
DE AltName: Full=Protein G2b;
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], AND PROTEIN SEQUENCE OF 20-52.
RC TISSUE=Venom, and Venom gland;
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 [2]
RP PROTEIN SEQUENCE OF 26-45, AMINO-ACID COMPOSITION, 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).
CC -!- FUNCTION: Inhibits carbachol-induced muscle contraction and weakly
CC blocks muscle contraction evoked by potassium.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=23637; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15581679};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY261468; AAP20603.1; -; mRNA.
DR AlphaFoldDB; Q7ZZN8; -.
DR SMR; Q7ZZN8; -.
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.
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; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:14529736"
FT CHAIN 20..238
FT /note="Cysteine-rich venom protein natrin-2"
FT /id="PRO_0000006280"
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; 26246 MW; 5A6DA4EFA227256C CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK RENQKQIVDK HNALRRSVRP TARNMLQMEW
NSNAAQNAKR WADRCSFAHS PPHLRTVGKI GCGENLFMSS QPYAWSRVIQ SWYDENKKFV
YGVGANPPGS VIGHYTQIVW YNSHLLGCGA AKCSSSKYLY VCQYCPTGNI IGSIATPYKS
GPPCGDCPSA CVNGLCTNPC KHHNVFSNCQ SLAKQNACQT EWMKSKCAAS CFCRTEII