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TX1C_CHEPU
ID   TX1C_CHEPU              Reviewed;         183 AA.
AC   C0HKG9; D5GSJ8; D5GSJ9; D7FBA1; D7FBA3; P86381; P86429; P86430;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=DELTA-miturgitoxin-Cp1c {ECO:0000305};
DE            Short=DELTA-MGTX-Cp1c {ECO:0000305};
DE   AltName: Full=Toxin CpTx1 {ECO:0000303|PubMed:20657014};
DE   AltName: Full=Toxin CpTx1c {ECO:0000303|PubMed:20657014, ECO:0000312|EMBL:CBH50811.1};
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;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CBH50811.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-181, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOXIC DOSE, PQM MOTIF, AND
RP   AMIDATION AT TRP-181.
RC   TISSUE=Venom {ECO:0000269|PubMed:20657014}, and
RC   Venom gland {ECO:0000312|EMBL:CBH50811.1};
RX   PubMed=20657014; DOI=10.1074/jbc.m110.104265;
RA   Vassilevski A.A., Fedorova I.M., Maleeva E.E., Korolkova Y.V.,
RA   Efimova S.S., Samsonova O.V., Schagina L.V., Feofanov A.V., Magazanik L.G.,
RA   Grishin E.V.;
RT   "Novel class of spider toxin: active principle from the yellow sac spider
RT   Cheiracanthium punctorium venom is a unique two-domain polypeptide.";
RL   J. Biol. Chem. 285:32293-32302(2010).
RN   [2]
RP   ALPHA-HELICAL REGION.
RX   PubMed=22613721; DOI=10.1074/jbc.m112.339051;
RA   Kuhn-Nentwig L., Fedorova I.M., Luscher B.P., Kopp L.S., Trachsel C.,
RA   Schaller J., Vu X.L., Seebeck T., Streitberger K., Nentwig W., Sigel E.,
RA   Magazanik L.G.;
RT   "A venom-derived neurotoxin, CsTx-1, from the spider Cupiennius salei
RT   exhibits cytolytic activities.";
RL   J. Biol. Chem. 287:25640-25649(2012).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 48-67, IDENTIFICATION BY MASS SPECTROMETRY, AND PQM
RP   MOTIF.
RC   TISSUE=Venom {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 (PubMed:20657014). Lethal to
CC       insect larvae (PubMed:20657014, PubMed:24717175). Causes instant
CC       paralysis and death in the larvae of the flesh fly (S.carnaria) at
CC       doses of 20 ug/g, at doses of less than 10 ug/g causes reversible
CC       paralysis (PubMed:20657014). Has cytolytic activity against insect Sf9
CC       cells (PubMed:20657014). Causes stable and irreversible depolarization
CC       of fly muscle fibers, leading to contracture at higher toxin
CC       concentrations (PubMed:20657014). Destabilizes membranes
CC       (PubMed:20657014). {ECO:0000269|PubMed:20657014,
CC       ECO:0000269|PubMed:24717175}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20657014}. Target
CC       cell membrane {ECO:0000269|PubMed:20657014}. Note=Probably forms a
CC       transmembrane alpha-helix in the target cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20657014}.
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' (By similarity). {ECO:0000250}.
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:20657014, ECO:0000303|PubMed:24717175}.
CC   -!- TOXIC DOSE: LD(50) is 10 ug/g on S.carnaria larvae.
CC       {ECO:0000269|PubMed:20657014}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. Double-CSTX
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Characterization of function and toxicity was performed using
CC       CpTx1, a mixture of DELTA-miturgitoxin-Cp1a, DELTA-miturgitoxin-Cp1b
CC       and DELTA-miturgitoxin-Cp1c. While it is assumed that all three are
CC       active current data cannot prove this. {ECO:0000305|PubMed:20657014}.
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DR   EMBL; FN594517; CBH50811.1; -; mRNA.
DR   AlphaFoldDB; C0HKG9; -.
DR   SMR; C0HKG9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; 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; Cytolysis; Direct protein sequencing; Disulfide bond; Knottin;
KW   Membrane; Neurotoxin; Secreted; Signal; Target cell membrane;
KW   Target membrane; Toxin; Transmembrane.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:20657014"
FT                   /id="PRO_0000440156"
FT   CHAIN           48..181
FT                   /note="DELTA-miturgitoxin-Cp1c"
FT                   /evidence="ECO:0000269|PubMed:20657014"
FT                   /id="PRO_0000440157"
FT   REGION          164..177
FT                   /note="Predicted alpha-helix"
FT   MOTIF           44..47
FT                   /note="Processing quadruplet motif"
FT                   /evidence="ECO:0000303|PubMed:20657014,
FT                   ECO:0000303|PubMed:24717175"
FT   MOD_RES         181
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000269|PubMed:20657014"
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..157
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        141..155
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
SQ   SEQUENCE   183 AA;  20778 MW;  10C781D1695AD51E CRC64;
     MKFSLFFSVF FLAVLHACLS ESEIDLEDEE HFMSSDSFLS EIQDESRGKT CIERNKECTN
     DRHGCCRGKI FKDKCTCVKS GKTEKCVCTQ KKWAKIIESY IGDIPALPKP VDDKCVPKHA
     DCSKRKDDCC KGGIFKYQCK CYDMYDDDGE KTDLCGCVSP VEHQAIEGAL RIAKKLIGDR
     WGR
 
 
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