SPN1B_OXYTA
ID SPN1B_OXYTA Reviewed; 166 AA.
AC P86717; S4TZ61;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Spiderine-1b {ECO:0000303|PubMed:24118933};
DE AltName: Full=M-oxotoxin-Ot3b {ECO:0000305};
DE Short=M-OXTX-Ot3b {ECO:0000305};
DE AltName: Full=OtTx1b {ECO:0000303|PubMed:24118933};
DE Flags: Precursor;
OS Oxyopes takobius (Lynx spider) (Oxyopes foliiformis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Lycosoidea; Oxyopidae; Oxyopes.
OX NCBI_TaxID=666126;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=24118933; DOI=10.1111/febs.12547;
RA Vassilevski A.A., Sachkova M.Y., Ignatova A.A., Kozlov S.A., Feofanov A.V.,
RA Grishin E.V.;
RT "Spider toxins comprising disulfide-rich and linear amphipathic domains: A
RT new class of molecules identified in the lynx spider Oxyopes takobius.";
RL FEBS J. 280:6247-6261(2013).
CC -!- FUNCTION: Has antimicrobial, insecticidal, cytolytic and cytotoxic
CC activity. {ECO:0000250|UniProtKB:P86716}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86716}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24118933}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000250|UniProtKB:P86716}.
CC -!- DOMAIN: The N-terminal part of the mature protein (59-100) probably
CC forms an alpha-helix which acts as a membrane-active peptide. It is
CC necessary and sufficient for the toxin's antimicrobial, insecticidal,
CC cytolytic and cytotoxic activity. {ECO:0000250|UniProtKB:P86716}.
CC -!- SIMILARITY: Belongs to the spiderine family. Cationic/spiderine
CC subfamily. {ECO:0000305}.
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DR EMBL; JX134894; AGG39773.1; -; mRNA.
DR AlphaFoldDB; P86717; -.
DR SMR; P86717; -.
DR ArachnoServer; AS001939; M-oxotoxin-Ot3b.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR044061; OXYTX_ICK.
DR PROSITE; PS51861; OXYTX_ICK; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Cytolysis; Disulfide bond; Knottin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..58
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT /id="PRO_0000425694"
FT CHAIN 59..166
FT /note="Spiderine-1b"
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT /id="PRO_0000425695"
FT DOMAIN 113..166
FT /note="Oxytoxin-type inhibitor cystine knot (ICK)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01208"
FT REGION 59..99
FT /note="Linear cationic cytotoxin domain"
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 116..130
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 123..135
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 127..162
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 129..151
FT /evidence="ECO:0000250|UniProtKB:P86716"
FT DISULFID 137..149
FT /evidence="ECO:0000250|UniProtKB:P86716"
SQ SEQUENCE 166 AA; 18395 MW; 8FE08C499C47DFB5 CRC64;
MKFALVLLGI CAFYLVNATG DLETELEASE LQELQEALDL IGETSLESLE AEELEEARKF
KWGKLFSAAK KLYKKGKKLS KNKNFKKALK FGKQLAKNLQ AGEEHEPGTP VGNNKCWAIG
TTCSDDCDCC PEHHCHCPAG KWLPGLFRCT CQVTESDKVN KCPPAE
