ID   CRVP_TELDH              Reviewed;         210 AA.
AC   Q2XXP5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Cysteine-rich venom protein TEL1;
DE            Short=CRVP;
DE   AltName: Full=Cysteine-rich secretory protein TEL1;
DE            Short=CRISP-TEL1;
DE   Flags: Precursor; Fragment;
OS   Telescopus dhara (Egyptian catsnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Telescopus.
OX   NCBI_TaxID=338837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16292255; DOI=10.1038/nature04328;
RA   Fry B.G., Vidal N., Norman J.A., Vonk F.J., Scheib H., Ramjan S.F.R.,
RA   Kuruppu S., Fung K., Blair Hedges S., Richardson M.K., Hodgson W.C.,
RA   Ignjatovic V., Summerhayes R., Kochva E.;
RT   "Early evolution of the venom system in lizards and snakes.";
RL   Nature 439:584-588(2006).
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 {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; DQ139900; AAZ75606.1; -; mRNA.
DR   AlphaFoldDB; Q2XXP5; -.
DR   SMR; Q2XXP5; -.
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; 3.40.33.10; -; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
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..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..>210
FT                   /note="Cysteine-rich venom protein TEL1"
FT                   /id="PRO_0000380647"
FT   DOMAIN          37..165
FT                   /note="SCP"
FT   DOMAIN          201..210
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   NON_TER         210
SQ   SEQUENCE   210 AA;  23926 MW;  20268CBE54C074E0 CRC64;
     MIVFILLSLA AVLQQSFGNV DFNSESPRRK NKQKEIVDMH NSLRRSVKPT ASNMLRMEWY
     SEAASNAERW AYRCILNHSP ESSRILGGIK CGENIYMSSN PRKWTEVIQL WYDEYKNFVY
     GIGANPRGSV IGHYTQIVWY KSYRIGCAAY YCPSSSYNYF YVCQYCPTGN WNGLTATPYK
     SGPTCGDCPS ACDNGLCTNP CLHENKFTNC