ID   TERN_PSEUS              Reviewed;          36 AA.
AC   P82321;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Termicin;
OS   Pseudacanthotermes spiniger.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termitidae; Macrotermitinae; Pseudacanthotermes.
OX   NCBI_TaxID=115113;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY,
RP   AMIDATION AT GLY-36, AND DISULFIDE BONDS.
RC   TISSUE=Blood, and Salivary gland;
RX   PubMed=11053427; DOI=10.1074/jbc.m002998200;
RA   Lamberty M., Zachary D., Lanot R., Bordereau C., Robert A., Hoffmann J.A.,
RA   Bulet P.;
RT   "Insect immunity. Constitutive expression of a cysteine-rich antifungal and
RT   a linear antibacterial peptide in a termite insect.";
RL   J. Biol. Chem. 276:4085-4092(2001).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=12592014; DOI=10.1110/ps.0228303;
RA   Da Silva P., Jouvensal L., Lamberty M., Bulet P., Caille A., Vovelle F.;
RT   "Solution structure of termicin, an antimicrobial peptide from the termite
RT   Pseudacanthotermes spiniger.";
RL   Protein Sci. 12:438-446(2003).
CC   -!- FUNCTION: Weak activity against Gram-positive bacteria B.megaterium,
CC       S.pyogenes and M.luteus, strong activity against yeasts C.albicans,
CC       C.neoformans and S.cerevisiae and filamentous fungi F.oxysporum,
CC       F.culmorum, N.crassa and N.hematococca. Less active against filamentous
CC       fungus T.viride. Inactive against Gram-positive bacteria A.viridans and
CC       S.aureus, filamentous fungi A.fumigatus and B.bassiana and yeast
CC       C.glabrata. {ECO:0000269|PubMed:11053427}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands and hemocytes.
CC       {ECO:0000269|PubMed:11053427}.
CC   -!- INDUCTION: By bacterial infection.
CC   -!- MASS SPECTROMETRY: Mass=4216.05; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11053427};
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DR   PDB; 1MM0; NMR; -; A=1-36.
DR   PDBsum; 1MM0; -.
DR   AlphaFoldDB; P82321; -.
DR   SMR; P82321; -.
DR   EvolutionaryTrace; P82321; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR024723; Termicin.
DR   Pfam; PF11415; Toxin_37; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Secreted.
FT   PEPTIDE         1..36
FT                   /note="Termicin"
FT                   /id="PRO_0000044688"
FT   MOD_RES         36
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:11053427"
FT   DISULFID        2..24
FT                   /evidence="ECO:0000269|PubMed:11053427"
FT   DISULFID        7..29
FT                   /evidence="ECO:0000269|PubMed:11053427"
FT   DISULFID        11..31
FT                   /evidence="ECO:0000269|PubMed:11053427"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:1MM0"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:1MM0"
FT   STRAND          28..33
FT                   /evidence="ECO:0007829|PDB:1MM0"
SQ   SEQUENCE   36 AA;  4222 MW;  1CA862900D9C3529 CRC64;
     ACNFQSCWAT CQAQHSIYFR RAFCDRSQCK CVFVRG