CRVP_PHIOL
ID CRVP_PHIOL Reviewed; 239 AA.
AC Q09GJ9; Q2XXP7; Q2XXP8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Cysteine-rich venom protein;
DE Short=CRVP;
DE AltName: Full=CRISP-PHI1;
DE AltName: Full=CRISP-PHI2;
DE AltName: Full=Cysteine-rich secretory protein;
DE Flags: Precursor;
OS Philodryas olfersii (Green snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX NCBI_TaxID=120305;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABI74696.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland {ECO:0000269|PubMed:16857193};
RX PubMed=16857193; DOI=10.1016/j.febslet.2006.07.010;
RA Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RT "Some aspects of the venom proteome of the Colubridae snake Philodryas
RT olfersii revealed from a Duvernoy's (venom) gland transcriptome.";
RL FEBS Lett. 580:4417-4422(2006).
RN [2]
RP ERRATUM OF PUBMED:16857193.
RA Ching A.T.C., Rocha M.M.T., Paes Leme A.F., Pimenta D.C., Furtado M.F.D.,
RA Serrano S.M.T., Ho P.L., Junqueira-de-Azevedo I.L.M.;
RL FEBS Lett. 580:5122-5123(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAZ75603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-236.
RC TISSUE=Venom gland {ECO:0000312|EMBL:AAZ75603.1};
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|UniProtKB:Q8JI40}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16857193}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16857193}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000255}.
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DR EMBL; DQ912659; ABI74696.1; -; mRNA.
DR EMBL; DQ139897; AAZ75603.1; -; mRNA.
DR EMBL; DQ139898; AAZ75604.1; -; mRNA.
DR AlphaFoldDB; Q09GJ9; -.
DR SMR; Q09GJ9; -.
DR PRIDE; Q09GJ9; -.
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 InterPro; IPR002413; V5_allergen-like.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF08562; Crisp; 1.
DR PRINTS; PR00838; V5ALLERGEN.
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..239
FT /note="Cysteine-rich venom protein"
FT /id="PRO_0000315898"
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:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 91..166
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 147..163
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 185..192
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 188..197
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 201..234
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 210..228
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..232
FT /evidence="ECO:0000250|UniProtKB:Q7T1K6,
FT ECO:0000255|PROSITE-ProRule:PRU01005"
FT CONFLICT 10
FT /note="A -> V (in Ref. 3; AAZ75603)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> V (in Ref. 3; AAZ75603)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="E -> K (in Ref. 3; AAZ75603)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="N -> I (in Ref. 3; AAZ75604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26968 MW; A835CB372EAD7569 CRC64;
MIVFILLSLA AVLQQSFGLV DFNSESPRRP EIQRVIVDTH NSYRRTVSPT ASNMLRMEWY
AEAAANAERW ASLCAYDHSQ NSDRVLDGIQ CGENIYMSSN PRSWTEIMQS WYDEYKNFDF
GYGANPPGSV IGHYTQIVWY KSYRIGCAAY YCPSSLYNYF YVCQYCPAGN FAGRTATPYN
SGPTCGDCPS ACDNGLCTNP CSEKNEFTNC NELVQQSSCQ DDWIKSNCAA TCFCKNKII
