ID   CR11_RANGI              Reviewed;          25 AA.
AC   P62569; P56226;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Caerin-1.1;
DE   Contains:
DE     RecName: Full=Caerin-1.1.1;
DE   Contains:
DE     RecName: Full=Caerin-1.1.3;
DE   Contains:
DE     RecName: Full=Caerin-1.1.5;
DE   Contains:
DE     RecName: Full=Caerin-1.1.6;
DE   Contains:
DE     RecName: Full=Caerin-1.1.7;
DE   Contains:
DE     RecName: Full=Caerin-1.1.8;
OS   Ranoidea gilleni (Centralian tree frog) (Litoria gilleni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=39405;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-25, AND MASS SPECTROMETRY.
RC   TISSUE=Parotoid gland;
RA   Waugh R.J., Stone D.J.M., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "Peptides from Australian frogs. The structures of the caerins and
RT   caeridins from Litoria gilleni.";
RL   J. Chem. Res. 139:937-961(1993).
CC   -!- FUNCTION: Antibacterial and antiviral peptides that adopt an alpha
CC       helical conformation which can disrupt bacterial membranes. Each caerin
CC       displays a different antimicrobial specificity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands.
CC   -!- DOMAIN: Contains two amphipathic alpha helix regions separated by a
CC       region of less-defined helicity and greater flexibility.
CC   -!- PTM: The major product is Caerin-1.1; in addition, different peptides
CC       are produced that are missing some amino acid residues at the N-
CC       terminus or C-terminus. Caerin-1.1.1 is inactive.
CC   -!- MASS SPECTROMETRY: [Caerin-1.1]: Mass=2582; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.1]: Mass=2412; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.3]: Mass=1421; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.5]: Mass=1626; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.6]: Mass=1489; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.7]: Mass=1180; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.8]: Mass=915; Method=FAB;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P62569; -.
DR   SMR; P62569; -.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR010000; Caerin_1.
DR   Pfam; PF07440; Caerin_1; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Antiviral defense; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Caerin-1.1"
FT                   /id="PRO_0000010164"
FT   PEPTIDE         1..16
FT                   /note="Caerin-1.1.5"
FT                   /id="PRO_0000010165"
FT   PEPTIDE         1..15
FT                   /note="Caerin-1.1.6"
FT                   /id="PRO_0000010166"
FT   PEPTIDE         1..12
FT                   /note="Caerin-1.1.7"
FT                   /id="PRO_0000010167"
FT   PEPTIDE         1..10
FT                   /note="Caerin-1.1.8"
FT                   /id="PRO_0000010168"
FT   PEPTIDE         3..25
FT                   /note="Caerin-1.1.1"
FT                   /id="PRO_0000010169"
FT   PEPTIDE         13..25
FT                   /note="Caerin-1.1.3"
FT                   /id="PRO_0000010170"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   25 AA;  2585 MW;  D8A5A460BB0EBE00 CRC64;
     GLLSVLGSVA KHVLPHVVPV IAEHL