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GOME_ACAGO
ID   GOME_ACAGO              Reviewed;          84 AA.
AC   P82358; Q86RA2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Gomesin;
DE   Flags: Precursor;
OS   Acanthoscurria gomesiana (Tarantula spider) (Phormictopus pheopygus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Acanthoscurria.
OX   NCBI_TaxID=115339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PYROGLUTAMATE FORMATION AT
RP   GLN-24, AND AMIDATION AT ARG-41.
RC   TISSUE=Hemocyte;
RX   PubMed=14505694; DOI=10.1016/s0965-1748(03)00115-2;
RA   Lorenzini D.M., Fukuzawa A.H., da Silva P.I. Jr., Machado-Santelli G.,
RA   Bijovsky A.T., Daffre S.;
RT   "Molecular cloning, expression analysis and cellular localization of
RT   gomesin, an anti-microbial peptide from hemocytes of the spider
RT   Acanthoscurria gomesiana.";
RL   Insect Biochem. Mol. Biol. 33:1011-1016(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-41, CHARACTERIZATION, MASS SPECTROMETRY, FUNCTION,
RP   TISSUE SPECIFICITY, PYROGLUTAMATE FORMATION AT GLN-24, AMIDATION AT ARG-41,
RP   AND DISULFIDE BONDS.
RC   TISSUE=Hemocyte;
RX   PubMed=10942757; DOI=10.1074/jbc.m001491200;
RA   Silva P.I. Jr., Daffre S., Bulet P.;
RT   "Isolation and characterization of gomesin, an 18-residue cysteine-rich
RT   defense peptide from the spider Acanthoscurria gomesiana hemocytes with
RT   sequence similarities to horseshoe crab antimicrobial peptides of the
RT   tachyplesin family.";
RL   J. Biol. Chem. 275:33464-33470(2000).
RN   [3]
RP   STRUCTURE BY NMR OF 24-41.
RX   PubMed=11856345; DOI=10.1046/j.0014-2956.2002.02760.x;
RA   Mandard N., Bulet P., Caille A., Daffre S., Vovelle F.;
RT   "The solution structure of gomesin, an antimicrobial cysteine-rich peptide
RT   from the spider.";
RL   Eur. J. Biochem. 269:1190-1198(2002).
CC   -!- FUNCTION: Active against several Gram-positive bacteria such as
CC       Bacillus spp, Staphylococcus spp and E.faecalis, several Gram-negative
CC       bacteria such as E.coli, K.pneumoniae, P.aeruginosa and Salmonella spp,
CC       filamentous fungi such as N.crassa, T.viridae and yeasts such as
CC       C.albicans. It is active against the parasite L.amazonensis as well. It
CC       shows hemolytic activity. {ECO:0000269|PubMed:10942757}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: In hemocytes only, but not in all hemocytes
CC       observed. {ECO:0000269|PubMed:10942757, ECO:0000269|PubMed:14505694}.
CC   -!- MASS SPECTROMETRY: Mass=2270.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10942757};
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DR   EMBL; AJ544540; CAD67587.1; -; mRNA.
DR   PDB; 1KFP; NMR; -; A=24-41.
DR   PDB; 6MY1; NMR; -; A=24-41.
DR   PDB; 6MY2; NMR; -; A=24-41.
DR   PDB; 6MY3; NMR; -; A=24-41.
DR   PDBsum; 1KFP; -.
DR   PDBsum; 6MY1; -.
DR   PDBsum; 6MY2; -.
DR   PDBsum; 6MY3; -.
DR   AlphaFoldDB; P82358; -.
DR   BMRB; P82358; -.
DR   SMR; P82358; -.
DR   TCDB; 1.C.34.3.1; the tachyplesin (tachyplesin) family.
DR   EvolutionaryTrace; P82358; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Hemolysis; Pyrrolidone carboxylic acid;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:10942757"
FT   PEPTIDE         24..41
FT                   /note="Gomesin"
FT                   /id="PRO_0000021338"
FT   PROPEP          42..84
FT                   /id="PRO_0000021339"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:10942757,
FT                   ECO:0000269|PubMed:14505694"
FT   MOD_RES         41
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:10942757,
FT                   ECO:0000269|PubMed:14505694"
FT   DISULFID        25..38
FT                   /evidence="ECO:0000269|PubMed:10942757"
FT   DISULFID        29..34
FT                   /evidence="ECO:0000269|PubMed:10942757"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:1KFP"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:1KFP"
SQ   SEQUENCE   84 AA;  9688 MW;  2B346C21A41F516E CRC64;
     MNRTRLFACL LLAVLILVHE SNAQCRRLCY KQRCVTYCRG RGKRSLDETN VGTSDVEKRA
     FDDSNVPSLV EERELEDEGS FIFD
 
 
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