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NTA_CORVA
ID   NTA_CORVA               Reviewed;          31 AA.
AC   P82601;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=U1-theraphotoxin-Cv1a {ECO:0000305};
DE            Short=U1-TRTX-Cv1a {ECO:0000305};
DE   AltName: Full=Covalitoxin-2 {ECO:0000305};
DE   AltName: Full=Covalitoxin-II {ECO:0000303|PubMed:10838086};
DE            Short=CvTx-II {ECO:0000303|PubMed:10838086};
OS   Coremiocnemis valida (Singapore tarantula) (Blue femur tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Coremiocnemis.
OX   NCBI_TaxID=129522;
RN   [1]
RP   PROTEIN SEQUENCE, BIOASSAY, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10838086; DOI=10.1016/s0014-5793(00)01593-3;
RA   Balaji R.A., Sasaki T., Gopalakrishnakone P., Sato K., Kini R.M.,
RA   Bay B.-H.;
RT   "Purification, structure determination and synthesis of covalitoxin-II, a
RT   short insect-specific neurotoxic peptide from the venom of the
RT   Coremiocnemis validus (Singapore tarantula).";
RL   FEBS Lett. 474:208-212(2000).
CC   -!- FUNCTION: Insecticidal toxin that induces reversible paralysis in
CC       crickets but not in cockroaches and mice. Molecular target unknown.
CC       {ECO:0000269|PubMed:10838086}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10838086}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:10838086}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P60590}.
CC   -!- MASS SPECTROMETRY: Mass=3406.91; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10838086};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family.
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DR   AlphaFoldDB; P82601; -.
DR   SMR; P82601; -.
DR   ArachnoServer; AS000422; U1-theraphotoxin-Cv1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Secreted; Toxin.
FT   PEPTIDE         1..31
FT                   /note="U1-theraphotoxin-Cv1a"
FT                   /evidence="ECO:0000269|PubMed:10838086"
FT                   /id="PRO_0000045030"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:P60590"
FT   DISULFID        9..21
FT                   /evidence="ECO:0000250|UniProtKB:P60590"
FT   DISULFID        15..28
FT                   /evidence="ECO:0000250|UniProtKB:P60590"
SQ   SEQUENCE   31 AA;  3413 MW;  FF7EC4BE8C070087 CRC64;
     ACSRAGENCY KSGRCCDGLY CKAYVVTCYK P
 
 
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