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CRVP_DEMVE
ID   CRVP_DEMVE              Reviewed;         238 AA.
AC   A6MFK9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Cysteine-rich venom protein;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein;
DE            Short=CRISP;
DE   Flags: Precursor;
OS   Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX   NCBI_TaxID=412038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17608513; DOI=10.1021/pr0701613;
RA   St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA   de Jersey J., Masci P.P., Lavin M.F.;
RT   "Diversity of toxic components from the venom of the evolutionarily
RT   distinct black whip snake, Demansia vestigiata.";
RL   J. Proteome Res. 6:3093-3107(2007).
CC   -!- FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) cyclic
CC       nucleotide-gated (CNG) ion channel currents. Does not inhibit retinal
CC       (CNGA3) currents. It forms high-affinity contacts with the pore turret
CC       region and most likely inhibits CNG channel current by blocking the
CC       external entrance to the transmembrane pore. Does not affect neither
CC       depolarization- nor caffeine-induced contraction arterial smooth muscle
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; DQ917520; ABK63549.1; -; mRNA.
DR   AlphaFoldDB; A6MFK9; -.
DR   SMR; A6MFK9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion 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   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380669"
FT   CHAIN           28..238
FT                   /note="Cysteine-rich venom protein"
FT                   /id="PRO_5000254113"
FT   DOMAIN          39..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;  26470 MW;  DE3ECA461D23D41F CRC64;
     MIAFIVLLSL AAVLQQSSGT VDFASESSNK GENQKQIVKK HNALRRSVKP PARNMLQMEW
     NSRAAQNAKR WAERCSFTHS PPSLRTVGKL RCGENLLQSS QPLPWSKVVQ AWYDENKNFV
     YGIGAKPPGS VVGHYTQVVW YKSRLLGCAS VKCSPTKYLY VCQYCPAGNI IGSQATPYKS
     GPRCADCPSA CVKGLCTNPC KREDDYSNCK SLAEKNKCME EWMKSKCPAS CFCHNKII
 
 
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