ID   TOAP1_TITOB             Reviewed;          74 AA.
AC   A0A1D3IXR7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Antimicrobial peptide ToAp1 {ECO:0000303|PubMed:27917162};
DE   Flags: Precursor;
OS   Tityus obscurus (Amazonian scorpion) (Tityus cambridgei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=1221240;
RN   [1] {ECO:0000312|EMBL:JAT91105.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA   de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA   Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA   Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT   "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT   obscurus and T. serrulatus scorpions.";
RL   PLoS ONE 13:e0193739-e0193739(2018).
RN   [2] {ECO:0000312|EMBL:SBQ16530.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 23-39, AND PROBABLE AMIDATION AT
RP   LYS-39.
RC   TISSUE=Venom gland;
RX   PubMed=27917162; DOI=10.3389/fmicb.2016.01844;
RA   Guilhelmelli F., Vilela N., Smidt K.S., de Oliveira M.A.,
RA   da Cunha Morales Alvares A., Rigonatto M.C., da Silva Costa P.H.,
RA   Tavares A.H., de Freitas S.M., Nicola A.M., Franco O.L., Derengowski L.D.,
RA   Schwartz E.F., Mortari M.R., Bocca A.L., Albuquerque P., Silva-Pereira I.;
RT   "Activity of scorpion venom-derived antifungal peptides against planktonic
RT   cells of Candida spp. and Cryptococcus neoformans and Candida albicans
RT   biofilms.";
RL   Front. Microbiol. 7:1844-1844(2016).
CC   -!- FUNCTION: Antimicrobial peptide. Is able to kill Mycobacterium
CC       abscessus subsp. massiliense in a dose-dependent manner (By
CC       similarity). Has antifungal activity against Candida spp. and one
CC       Cryptococcus neoformans strains with MICs values ranging from 12.5 to
CC       200 uM (PubMed:27917162). Shows also an inhibitory activity on
CC       C.albicans biofilms at high concentrations (PubMed:27917162). Shows low
CC       cytotoxic activity and has weak hemolytic activity on human
CC       erythrocytes (PubMed:27917162). Shows anti-inflammatory activities,
CC       since it decreases release of pro-inflammatory cytokines, and increases
CC       release of anti-inflammatory cytokines (By similarity). Acts by
CC       blocking the Toll-like receptor 4 (TLR4) (By similarity). In addition,
CC       decreases the expression of costimulatory molecules such as CD80 and
CC       CD86 in LPS-stimulated cells (By similarity). In vivo, does not induce
CC       immuce cell migration (By similarity). Helical wheel projections
CC       predict an amphipathic peptide with distinct hydrophobic and
CC       hydrophilic faces (Probable). {ECO:0000250|UniProtKB:P0DQT2,
CC       ECO:0000269|PubMed:27917162, ECO:0000305|PubMed:27917162}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27917162}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:27917162}.
CC   -!- MISCELLANEOUS: Does not show antifungal activity against Candida
CC       glabrata (ATCC90030) (MIC>400 uM). {ECO:0000269|PubMed:27917162}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Short antimicrobial peptide (group 4) family.
CC       {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; GEMQ01000084; JAT91105.1; -; Transcribed_RNA.
DR   EMBL; GEMQ01000031; JAT91158.1; -; Transcribed_RNA.
DR   EMBL; GEMQ01000022; JAT91167.1; -; Transcribed_RNA.
DR   EMBL; LT576029; SBQ16530.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Fungicide; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..39
FT                   /note="Antimicrobial peptide ToAp1"
FT                   /evidence="ECO:0000305|PubMed:27917162"
FT                   /id="PRO_5013493957"
FT   PROPEP          40..74
FT                   /evidence="ECO:0000305|PubMed:27917162"
FT                   /id="PRO_0000454900"
FT   MOD_RES         39
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000305|PubMed:27917162"
SQ   SEQUENCE   74 AA;  8487 MW;  8F77727272863762 CRC64;
     MQMKYLIPIF FLVLIVADHC HAFIGMIPGL IGGLISAFKG RRKRDITAQI EQYRNIQKRE
     AAELEELLAN LPVY