ID   TOP4A_OXYTA             Reviewed;          77 AA.
AC   F8J4S0; P86350;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Oxyopinin-4a {ECO:0000303|PubMed:21933345};
DE            Short=Oxt-4a {ECO:0000303|PubMed:21933345};
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 48-77, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, DISULFIDE
RP   BOND, AND STRUCTURE BY NMR.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=21933345; DOI=10.1111/j.1742-4658.2011.08361.x;
RA   Dubovskii P.V., Vassilevski A.A., Samsonova O.V., Egorova N.S.,
RA   Kozlov S.A., Feofanov A.V., Arseniev A.S., Grishin E.V.;
RT   "Novel lynx spider toxin shares common molecular architecture with defense
RT   peptides from frog skin.";
RL   FEBS J. 278:4382-4393(2011).
CC   -!- FUNCTION: Disrupts cell membranes through the formation of pores
CC       (Probable). Has antibacterial activity against Gram-positive bacteria
CC       S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-
CC       negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has
CC       hemolytic activity against human erythrocytes (EC(50)=7 uM).
CC       {ECO:0000269|PubMed:21933345, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21933345,
CC       ECO:0000303|PubMed:21933345}. Target cell membrane
CC       {ECO:0000305|PubMed:21933345}. Note=Probably forms a transmembrane
CC       alpha-helix in the target cell membrane. {ECO:0000269|PubMed:21933345,
CC       ECO:0000303|PubMed:21933345}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:21933345}.
CC   -!- MASS SPECTROMETRY: Mass=3612.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21933345};
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DR   EMBL; FN997582; CBQ82558.1; -; mRNA.
DR   PDB; 2L3I; NMR; -; A=48-77.
DR   PDBsum; 2L3I; -.
DR   AlphaFoldDB; F8J4S0; -.
DR   BMRB; F8J4S0; -.
DR   SMR; F8J4S0; -.
DR   ArachnoServer; AS001793; MU-oxotoxin-Ot4a.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Hemolysis; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000269|PubMed:21933345"
FT                   /id="PRO_5000770556"
FT   PEPTIDE         48..77
FT                   /note="Oxyopinin-4a"
FT                   /evidence="ECO:0000269|PubMed:21933345"
FT                   /id="PRO_5000770557"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000269|PubMed:21933345"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:2L3I"
FT   HELIX           59..73
FT                   /evidence="ECO:0007829|PDB:2L3I"
SQ   SEQUENCE   77 AA;  9205 MW;  80760E1A5C99FA57 CRC64;
     MKISQVFIFV FLLMISVAWA NEAYEEESNY LSERFDADVE EITPEFRGIR CPKSWKCKAF
     KQRVLKRLLA MLRQHAF