ID   THMAC_THETS             Reviewed;          97 AA.
AC   Q6T6C2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Theromacin;
DE   Flags: Precursor;
OS   Theromyzon tessulatum (Duck leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Rhynchobdellida; Glossiphoniidae; Theromyzon.
OX   NCBI_TaxID=13286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-52, DISULFIDE BONDS,
RP   SUBCELLULAR LOCATION, FUNCTION, INDUCTION, AND MASS SPECTROMETRY.
RX   PubMed=15102860; DOI=10.1074/jbc.m312156200;
RA   Tasiemski A., Vandenbulcke F., Mitta G., Lemoine J., Lefebvre C.,
RA   Sautiere P.-E., Salzet M.;
RT   "Molecular characterization of two novel antibacterial peptides inducible
RT   upon bacterial challenge in an annelid, the leech Theromyzon tessulatum.";
RL   J. Biol. Chem. 279:30973-30982(2004).
CC   -!- FUNCTION: Has a bactericidal activity. Active against M.luteus. No
CC       activity toward E.coli and F.oxysporum. {ECO:0000269|PubMed:15102860}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15102860}.
CC   -!- TISSUE SPECIFICITY: Coelomic liquid (at protein level). Expressed in
CC       large fat cells in contact with coelomic cavities, in intestinal
CC       epithelia and at the epidermis level.
CC   -!- INDUCTION: After blood meal ingestion and upon bacterial challenge.
CC       {ECO:0000269|PubMed:15102860}.
CC   -!- MASS SPECTROMETRY: Mass=8517.98; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15102860};
CC   -!- SIMILARITY: Belongs to the macin family. {ECO:0000305}.
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DR   EMBL; AY434032; AAR12065.1; -; mRNA.
DR   AlphaFoldDB; Q6T6C2; -.
DR   SMR; Q6T6C2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   Gene3D; 3.30.30.100; -; 1.
DR   InterPro; IPR029230; Macin.
DR   InterPro; IPR038456; Macin_sf.
DR   Pfam; PF14865; Macin; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15102860"
FT   CHAIN           23..97
FT                   /note="Theromacin"
FT                   /id="PRO_0000342176"
FT   DISULFID        24..31
FT                   /evidence="ECO:0000269|PubMed:15102860"
FT   DISULFID        46..50
FT                   /evidence="ECO:0000269|PubMed:15102860"
FT   DISULFID        53..95
FT                   /evidence="ECO:0000269|PubMed:15102860"
FT   DISULFID        61..69
FT                   /evidence="ECO:0000269|PubMed:15102860"
FT   DISULFID        79..81
FT                   /evidence="ECO:0000269|PubMed:15102860"
SQ   SEQUENCE   97 AA;  10818 MW;  70C17007940593F4 CRC64;
     MELKSGLSIL LCFGICIAVI NAGCFEDWSR CSPSTSRGTG VLWRDCDSYC KVCFKADRGE
     CFDSPSLNCP QRLPNNKQCR CINARTAKDN RNPTCWA