ID   TX2A_CHEPU              Reviewed;         179 AA.
AC   A0A059T2H4; C0HJD4;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=DELTA-miturgitoxin-Cp2a {ECO:0000305};
DE            Short=DELTA-MGTX-Cp2a {ECO:0000305};
DE   AltName: Full=Toxin CpTx-2a {ECO:0000303|PubMed:24717175};
DE   AltName: Full=Toxin CpTx1-2a {ECO:0000305};
DE   Flags: Precursor;
OS   Cheiracanthium punctorium (Yellow sac spider) (Aranea punctoria).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Entelegynae incertae sedis; Cheiracanthiidae;
OC   Cheiracanthium.
OX   NCBI_TaxID=682790 {ECO:0000312|EMBL:AHH30791.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-67, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION
RP   BY MASS SPECTROMETRY, PQM MOTIF, TOXIC DOSE, AND AMIDATION AT VAL-178.
RC   TISSUE=Venom {ECO:0000303|PubMed:24717175}, and
RC   Venom gland {ECO:0000303|PubMed:24717175};
RX   PubMed=24717175; DOI=10.1111/imb.12097;
RA   Sachkova M.Y., Slavokhotova A.A., Grishin E.V., Vassilevski A.A.;
RT   "Structure of the yellow sac spider Cheiracanthium punctorium genes
RT   provides clues to evolution of insecticidal two-domain knottin toxins.";
RL   Insect Mol. Biol. 23:527-538(2014).
CC   -!- FUNCTION: Spider venom toxin that exhibits cytolytic activity by
CC       forming an alpha-helix across the membrane (By similarity). Lethal to
CC       insect larvae (PubMed:24717175). {ECO:0000250|UniProtKB:C0HKG7,
CC       ECO:0000269|PubMed:24717175}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24717175}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:24717175}.
CC   -!- DOMAIN: The presence of 'disulfide through disulfide knots'
CC       structurally defines this protein as a knottin. This toxin contains 2
CC       'disulfide through disulfide knots'. {ECO:0000305}.
CC   -!- PTM: Cleavage of the propeptide depends on the processing quadruplet
CC       motif (XXXR, with at least one of X being E).
CC       {ECO:0000303|PubMed:24717175}.
CC   -!- MASS SPECTROMETRY: Mass=14970; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24717175};
CC   -!- TOXIC DOSE: LD(50) is >50 ug/g in S.carnaria larvae.
CC       {ECO:0000269|PubMed:24717175}.
CC   -!- TOXIC DOSE: PD(50) is 33-50 ug/g in S.carnaria larvae.
CC       {ECO:0000269|PubMed:24717175}.
CC   -!- SIMILARITY: Belongs to the spider toxin CSTX family. Double-CSTX
CC       subfamily. {ECO:0000255}.
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DR   EMBL; KF155273; AHH30791.1; -; mRNA.
DR   AlphaFoldDB; A0A059T2H4; -.
DR   SMR; A0A059T2H4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019553; Spider_toxin_CSTX_knottin.
DR   InterPro; IPR011142; Spider_toxin_CSTX_Knottin_CS.
DR   Pfam; PF10530; Toxin_35; 2.
DR   PROSITE; PS60029; SPIDER_CSTX; 2.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Knottin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000305|PubMed:24717175"
FT                   /id="PRO_0000440158"
FT   CHAIN           48..178
FT                   /note="DELTA-miturgitoxin-Cp2a"
FT                   /evidence="ECO:0000305|PubMed:24717175"
FT                   /id="PRO_5001582535"
FT   MOTIF           44..47
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:24717175"
FT   MOD_RES         178
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:24717175"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        58..75
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        65..88
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        77..86
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        115..130
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        122..139
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        129..158
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        141..156
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
SQ   SEQUENCE   179 AA;  20501 MW;  94ED2CA1FD1B8B55 CRC64;
     MKFSLFFGVL FLAILHSCLS ESEKDLTDED HFRSSDSFLS EIQEESRGKK CIERNKECTN
     DRHGCCRGKI FKDKCECVGS GGKERCVCKQ KKWAKIIESY IGDIPTLPKP EDDKCVPKHE
     DCSERKNDCC KSGLFTLKCK CYDMQDDEDG KKTELCGCVQ PFEHKAIEQA LRFGKWMVG