CRVP1_HYDHA
ID CRVP1_HYDHA Reviewed; 238 AA.
AC Q8UW25;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Cysteine-rich venom protein 1;
DE Short=CRVP;
DE Flags: Precursor;
OS Hydrophis hardwickii (Hardwick's spine-bellied seasnake) (Lapemis
OS hardwickii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX NCBI_TaxID=8781;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Wei J., Zhong X., Yang W., Zhao G., Xu A.;
RT "A novel cysteine-rich venom protein precursor (CRVP) mRNA from sea snake
RT (Lapemis hardwickii).";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL54896.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF159541; AAL54896.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q8UW25; -.
DR SMR; Q8UW25; -.
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 2: Evidence at transcript level;
KW Calcium channel impairing toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..238
FT /note="Cysteine-rich venom protein 1"
FT /id="PRO_0000006276"
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; 26294 MW; 7EC0587E5CA9C4F1 CRC64;
MIAFIVLLSL AAVLQQSSGT VDFASESSNK KDYRREIVDK HNALRRSVKP TARNMLQMKW
NSRAAQNAKR SADRCTFAHS PEHTRTVGKF RCGENIFMSS QPFAWSGVVQ DWYDEIKNVV
DGIGAKPPGS VIGHYTQIVW YKSHLLGCAS AKCSSTKYLY VCQYCPAGNI SSSIATPYKS
GPSCGDCPSA CVNGLCTNPC EYEDTFSNCK ALAKKTKCKT EWIKSKCPAT CFCHNKII