TX1B_CHEPU
ID TX1B_CHEPU Reviewed; 183 AA.
AC C0HKG8; 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 16.
DE RecName: Full=DELTA-miturgitoxin-Cp1b {ECO:0000305};
DE Short=DELTA-MGTX-Cp1b {ECO:0000305};
DE AltName: Full=Toxin CpTx1 {ECO:0000303|PubMed:20657014};
DE AltName: Full=Toxin CpTx1b {ECO:0000303|PubMed:20657014, ECO:0000312|EMBL:CBH50809.1};
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:CBH50809.1}
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:CBH50809.1};
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; FN594515; CBH50809.1; -; mRNA.
DR EMBL; FN594516; CBH50810.1; -; mRNA.
DR AlphaFoldDB; C0HKG8; -.
DR SMR; C0HKG8; -.
DR TCDB; 8.B.19.2.7; the sea anemone k+ channel blocker toxin, bcstx3 (bcstx3) family.
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_0000440154"
FT CHAIN 48..181
FT /note="DELTA-miturgitoxin-Cp1b"
FT /evidence="ECO:0000269|PubMed:20657014"
FT /id="PRO_0000440155"
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; 20819 MW; 30650AF8CBCB6C0F CRC64;
MKFSLFFSVF FLAVLHACLS ESEIDLEDEE HFMSSDSFLS EIQDESRGKT CIERNKECTN
DRHGCCRGKI FKDKCTCVKN GKTEKCVCTQ KKWAKIIESY IGDIPALPKP VDDKCVPKHA
DCSKRKDECC KGGIFKYQCK CYDMYDDDGE KTDLCGCVSP VEHQAIEGAL RIAKKLIGDR
WGR
