ID   MCU31_RANGE             Reviewed;          26 AA.
AC   P82069;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Maculatin-3.1;
OS   Ranoidea genimaculata (Brown-spotted tree frog) (Litoria genimaculata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=95132;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT ALA-26, AND MASS SPECTROMETRY.
RX   PubMed=9620615;
RX   DOI=10.1002/(sici)1099-1387(199804)4:2<111::aid-psc134>3.0.co;2-8;
RA   Rozek T., Waugh R.J., Steinborner S.T., Bowie J.H., Tyler M.J.,
RA   Wallace J.C.;
RT   "The maculatin peptides from the skin glands of the tree frog Litoria
RT   genimaculata. A comparison of the structures and antibacterial activities
RT   of maculatin 1.1 and caerin 1.1.";
RL   J. Pept. Sci. 4:111-115(1998).
CC   -!- FUNCTION: Shows antibacterial activity against S.uberis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- MASS SPECTROMETRY: Mass=2395; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:9620615};
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DR   AlphaFoldDB; P82069; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..26
FT                   /note="Maculatin-3.1"
FT                   /id="PRO_0000043813"
FT   MOD_RES         26
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000269|PubMed:9620615"
SQ   SEQUENCE   26 AA;  2726 MW;  169A29554C4D66DD CRC64;
     GLLQTIKEKL ESLESLAKGI VSGIQA