3NB_OXYFU
ID 3NB_OXYFU Reviewed; 74 AA.
AC C0HJD3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Fulgimotoxin {ECO:0000303|PubMed:23851011};
DE Short=FTx {ECO:0000303|PubMed:23851011};
OS Oxybelis fulgidus (Green vine snake) (Coluber fulgidus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Colubrinae; Oxybelis.
OX NCBI_TaxID=121355;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, AND PYROGLUTAMATE FORMATION AT
RP GLN-1.
RC TISSUE=Venom;
RX PubMed=23851011; DOI=10.1016/j.biochi.2013.06.025;
RA Heyborne W.H., Mackessy S.P.;
RT "Identification and characterization of a taxon-specific three-finger toxin
RT from the venom of the Green Vinesnake (Oxybelis fulgidus; family
RT Colubridae).";
RL Biochimie 95:1923-1932(2013).
CC -!- FUNCTION: Reptile-specific three-finger toxin that is lethal at low
CC doses for lizards, but not for mice. Probably acts as a neurotoxin.
CC {ECO:0000269|PubMed:23851011}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23851011}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23851011}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23851011}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:23851011}.
CC -!- PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:23851011}.
CC -!- MASS SPECTROMETRY: Mass=8146.06; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23851011};
CC -!- TOXIC DOSE: LD(50) is 0.28 ug/g by intraperitoneal injection in
CC A.carolinensis and 0.6 ug/g in H.frenatus.
CC {ECO:0000269|PubMed:23851011}.
CC -!- MISCELLANEOUS: Not toxic to neonate mice by intraperitoneal injection
CC at doses up to 5 ug/g. {ECO:0000269|PubMed:23851011}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Boigatoxin sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJD3; -.
DR SMR; C0HJD3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Neurotoxin;
KW Pyrrolidone carboxylic acid; Secreted; Toxin.
FT CHAIN 1..74
FT /note="Fulgimotoxin"
FT /evidence="ECO:0000269|PubMed:23851011"
FT /id="PRO_0000424698"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:23851011"
FT DISULFID 10..34
FT /evidence="ECO:0000250|UniProtKB:A0S865"
FT DISULFID 13..21
FT /evidence="ECO:0000250|UniProtKB:A0S865"
FT DISULFID 27..51
FT /evidence="ECO:0000250|UniProtKB:A0S865"
FT DISULFID 55..66
FT /evidence="ECO:0000250|UniProtKB:A0S865"
FT DISULFID 67..72
FT /evidence="ECO:0000250|UniProtKB:A0S865"
SQ SEQUENCE 74 AA; 8141 MW; BBA0532B5BA5DA6B CRC64;
QAIGPPFGLC FQCNQKTSSD CFNAKRCPPF HRTCYTLYKP DGGEEWAVKG CAKGCPTAGP
DERVKCCHTP RCNN