SPN1A_OXYTA
ID SPN1A_OXYTA Reviewed; 166 AA.
AC P86716; S4TYR3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Spiderine-1a {ECO:0000303|PubMed:24118933};
DE AltName: Full=OtTx1a {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], PROTEIN SEQUENCE OF 59-93, FUNCTION,
RP SUBCELLULAR LOCATION, MASS SPECTROMETRY, DOMAIN, AND TOXIC DOSE.
RC TISSUE=Venom, and 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).
RN [2]
RP STRUCTURE BY NMR OF 59-99 AND 108-166, AND DISULFIDE BOND.
RX PubMed=27997708; DOI=10.1002/pro.3101;
RA Nadezhdin K.D., Romanovskaia D.D., Sachkova M.Y., Oparin P.B.,
RA Kovalchuk S.I., Grishin E.V., Arseniev A.S., Vassilevski A.A.;
RT "Modular toxin from the lynx spider Oxyopes takobius: Structure of
RT spiderine domains in solution and membrane-mimicking environment.";
RL Protein Sci. 26:611-616(2017).
CC -!- FUNCTION: Has antimicrobial, insecticidal, cytolytic and cytotoxic
CC activity. Active against E.coli DH5alpha, E.faecalis VKM B 871,
CC B.subtilis VKM B 501, A.globiformis VKM Ac 1112, P.aeruginosa PAO1 and
CC S.aureus 209P in submicromolar or low micromolar ranges. Lyses human
CC erythrocytes. Kills HeLA and A549 cells. {ECO:0000269|PubMed:24118933}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24118933}.
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:0000269|PubMed:27997708}.
CC -!- DOMAIN: The N-terminal part of the mature protein (59-100) forms an
CC alpha-helix which acts as a membrane-active peptide. It is necessary
CC and sufficient for the toxin's antimicrobial, insecticidal, cytolytic
CC and cytotoxic activity. {ECO:0000269|PubMed:24118933,
CC ECO:0000269|PubMed:27997708}.
CC -!- MASS SPECTROMETRY: Mass=12030; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:24118933};
CC -!- TOXIC DOSE: LD(50) is 75 ug/g on flesh fly larvae (S.carnaria).
CC {ECO:0000269|PubMed:24118933}.
CC -!- TOXIC DOSE: PD(50) is 75 ug/g on M.sexta first instar larvae.
CC {ECO:0000269|PubMed:24118933}.
CC -!- SIMILARITY: Belongs to the spiderine family. Cationic/spiderine
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX134895; AGG39774.1; -; mRNA.
DR PDB; 2N85; NMR; -; A=59-99.
DR PDB; 2N86; NMR; -; A=108-166.
DR PDBsum; 2N85; -.
DR PDBsum; 2N86; -.
DR AlphaFoldDB; P86716; -.
DR SMR; P86716; -.
DR TCDB; 8.B.12.1.6; the spider toxin (stx2) family.
DR ArachnoServer; AS001675; M-oxotoxin-Ot3a.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Knottin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..58
FT /evidence="ECO:0000269|PubMed:24118933"
FT /id="PRO_0000425692"
FT CHAIN 59..166
FT /note="Spiderine-1a"
FT /evidence="ECO:0000269|PubMed:24118933"
FT /id="PRO_0000425693"
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:0000305"
FT DISULFID 116..130
FT /evidence="ECO:0000269|PubMed:27997708,
FT ECO:0000312|PDB:2N86"
FT DISULFID 123..135
FT /evidence="ECO:0000269|PubMed:27997708,
FT ECO:0000312|PDB:2N86"
FT DISULFID 127..162
FT /evidence="ECO:0000269|PubMed:27997708,
FT ECO:0000312|PDB:2N86"
FT DISULFID 129..151
FT /evidence="ECO:0000269|PubMed:27997708,
FT ECO:0000312|PDB:2N86"
FT DISULFID 137..149
FT /evidence="ECO:0000269|PubMed:27997708,
FT ECO:0000312|PDB:2N86"
FT HELIX 62..81
FT /evidence="ECO:0007829|PDB:2N85"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:2N85"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2N86"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2N86"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2N86"
SQ SEQUENCE 166 AA; 18421 MW; E5605259C728CEBA CRC64;
MKFALVLLGV CAFYLVNATG DLETELEASE LQELQEALDL IGETPLESLE AEELEEARKF
KWGKLFSTAK KLYKKGKKLS KNKNFKKALK FGKQLAKNLQ AGEEHEPGTP VGNNKCWAIG
TTCSDDCDCC PEHHCHCPAG KWLPGLFRCT CQVTESDKVN KCPPAE
