CRVP_OPHHA
ID CRVP_OPHHA Reviewed; 239 AA.
AC Q7ZT98; Q7T1R6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cysteine-rich venom protein ophanin;
DE Short=CRVP;
DE AltName: Full=Opharin;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-58; 60-66; 117-141;
RP 181-225 AND 228-237, CHARACTERIZATION, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=12646276; DOI=10.1016/s0003-9861(03)00028-6;
RA Yamazaki Y., Hyodo F., Morita T.;
RT "Wide distribution of cysteine-rich secretory proteins in snake venoms:
RT isolation and cloning of novel snake venom cysteine-rich secretory
RT proteins.";
RL Arch. Biochem. Biophys. 412:133-141(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Pung Y.F., Kumar P.P., Kini R.M.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Weakly 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. {ECO:0000269|PubMed:12646276}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=25037.4; Mass_error=67.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12646276};
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; AY181984; AAO62996.1; -; mRNA.
DR EMBL; AY299475; AAP81292.1; -; mRNA.
DR AlphaFoldDB; Q7ZT98; -.
DR SMR; Q7ZT98; -.
DR PRIDE; Q7ZT98; -.
DR TopDownProteomics; Q7ZT98; -.
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..18
FT /evidence="ECO:0000269|PubMed:12646276"
FT CHAIN 19..239
FT /note="Cysteine-rich venom protein ophanin"
FT /id="PRO_0000006281"
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"
FT CONFLICT 90
FT /note="E -> Q (in Ref. 2; AAP81292)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="S -> N (in Ref. 2; AAP81292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26869 MW; 9B9D779FA8DA265D CRC64;
MIAFTLLSLA AVLQQSFGNV DFNSESTRRQ KKQKEIVDLH NSLRRSVSPT ASNMLKMQWY
PEAASNAERW ASNCNLGHSP DYSRVLEGIE CGENIYMSSN PRAWTEIIQL WHDEYKNFVY
GVGANPPGSV TGHYTQIVWY KTYRIGCAVN YCPSSEYSYF YVCQYCPSGN MRGSTATPYK
SGPTCGDCPS ACDNGLCTNP CTLYNEYTNC DSLVKQSSCQ DEWIKSKCPA SCFCHNKII
