ID   MCU11_RANGE             Reviewed;          21 AA.
AC   P82066;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Maculatin-1.1;
DE   Contains:
DE     RecName: Full=Maculatin-1.1.1;
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 PHE-21, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
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: Maculatin-1.1 shows significant antibacterial activity
CC       against Gram-positive bacteria, less against Gram-negative bacteria.
CC       Maculatin-1.1.1 is inactive.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- MASS SPECTROMETRY: [Maculatin-1.1]: Mass=2145; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:9620615};
CC   -!- MASS SPECTROMETRY: [Maculatin-1.1.1]: Mass=1975; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:9620615};
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DR   PDB; 2MMJ; NMR; -; A=1-21.
DR   PDB; 2MN8; NMR; -; A=1-21.
DR   PDB; 2MN9; NMR; -; A=1-21.
DR   PDBsum; 2MMJ; -.
DR   PDBsum; 2MN8; -.
DR   PDBsum; 2MN9; -.
DR   AlphaFoldDB; P82066; -.
DR   SMR; P82066; -.
DR   TCDB; 1.C.76.1.1; the pore-forming maculatin peptide (maculatin) family.
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   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..21
FT                   /note="Maculatin-1.1"
FT                   /id="PRO_0000010300"
FT   PEPTIDE         3..21
FT                   /note="Maculatin-1.1.1"
FT                   /id="PRO_0000010301"
FT   MOD_RES         21
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:9620615"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:2MMJ"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:2MMJ"
FT   HELIX           13..20
FT                   /evidence="ECO:0007829|PDB:2MMJ"
SQ   SEQUENCE   21 AA;  2147 MW;  E0975D60AE176029 CRC64;
     GLFGVLAKVA AHVVPAIAEH F