ID   CR119_RANGR             Reviewed;          25 AA.
AC   P0C2A8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Caerin-1.19;
DE   Contains:
DE     RecName: Full=Caerin-1.19.1;
DE   Contains:
DE     RecName: Full=Caerin-1.19.2;
DE   Contains:
DE     RecName: Full=Caerin-1.19.3;
OS   Ranoidea gracilenta (Dainty green tree frog) (Litoria gracilenta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=95133;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-25, FUNCTION, MASS SPECTROMETRY, AND
RP   SYNTHESIS OF 1-25.
RC   TISSUE=Skin secretion;
RX   PubMed=16554081; DOI=10.1016/j.toxicon.2006.01.019;
RA   Maclean M.J., Brinkworth C.S., Bilusich D., Bowie J.H., Doyle J.R.,
RA   Llewellyn L.E., Tyler M.J.;
RT   "New caerin antibiotic peptides from the skin secretion of the dainty green
RT   tree frog Litoria gracilenta. Identification using positive and negative
RT   ion electrospray mass spectrometry.";
RL   Toxicon 47:664-675(2006).
CC   -!- FUNCTION: Caerin-1.19 shows significant activity against Gram-positive
CC       organisms, but is less effective against Gram-negative organisms.
CC       {ECO:0000269|PubMed:16554081}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- MASS SPECTROMETRY: [Caerin-1.19]: Mass=2648; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16554081};
CC   -!- MASS SPECTROMETRY: [Caerin-1.19.1]: Mass=2478; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16554081};
CC   -!- MASS SPECTROMETRY: [Caerin-1.19.2]: Mass=2331; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16554081};
CC   -!- MASS SPECTROMETRY: [Caerin-1.19.3]: Mass=1992; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16554081};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C2A8; -.
DR   SMR; P0C2A8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; 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   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Caerin-1.19"
FT                   /id="PRO_0000271470"
FT   PEPTIDE         3..25
FT                   /note="Caerin-1.19.1"
FT                   /id="PRO_0000271471"
FT   PEPTIDE         4..25
FT                   /note="Caerin-1.19.2"
FT                   /id="PRO_0000271472"
FT   PEPTIDE         7..25
FT                   /note="Caerin-1.19.3"
FT                   /id="PRO_0000271473"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:16554081"
SQ   SEQUENCE   25 AA;  2651 MW;  99A77460A7FD4FF2 CRC64;
     GLFKVLGSVA KHLLPHVAPI IAEKL