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TXF2A_SCOMU
ID   TXF2A_SCOMU             Reviewed;          78 AA.
AC   V5N6J4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=U-scoloptoxin(15)-Ssm2a {ECO:0000305};
DE            Short=U-SLPTX(15)-Ssm2a {ECO:0000305};
DE   AltName: Full=Scolotoxin-Ssm2a {ECO:0000312|EMBL:AHA82508.1};
DE   Flags: Precursor;
OS   Scolopendra mutilans (Chinese red-headed centipede) (Scolopendra
OS   subspinipes mutilans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=2836329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Hua W.J.;
RT   "Insecticidal activity of recombinant centipede neurotoxin, rScolotoxin-
RT   Ssm2a on four species in Lepidoptera and Orthoptera.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta). Since the toxin contains
CC       only 2 disulfide bonds, it is called 2ds-CSalpha/beta.
CC       {ECO:0000250|UniProtKB:A0A2L0ART2}.
CC   -!- SIMILARITY: Belongs to the SLPTX(15) family. {ECO:0000305}.
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DR   EMBL; KF555483; AHA82508.1; -; mRNA.
DR   AlphaFoldDB; V5N6J4; -.
DR   SMR; V5N6J4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..78
FT                   /note="U-scoloptoxin(15)-Ssm2a"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5004740274"
FT   REGION          34..37
FT                   /note="Important for inhibition of KCNQ4"
FT                   /evidence="ECO:0000250|UniProtKB:A0A2L0ART2"
FT   SITE            69
FT                   /note="Important for inhibition of KCNQ4"
FT                   /evidence="ECO:0000250|UniProtKB:A0A2L0ART2"
FT   DISULFID        44..70
FT                   /evidence="ECO:0000250|UniProtKB:A0A2L0ART2"
FT   DISULFID        48..72
FT                   /evidence="ECO:0000250|UniProtKB:A0A2L0ART2"
SQ   SEQUENCE   78 AA;  9068 MW;  C005B0B5EE1A3558 CRC64;
     MEKKIIFLCF FVSLLTLPEF ISSQVLVEDD VPFPEKKFAD RGECIRACAA KFTDGDLSKI
     KDVLPRYYKC VCWYYPTS
 
 
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