ID   CR16_RANCH              Reviewed;          25 AA.
AC   P62547; P56231; P81249;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 2.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Caerin-1.6 {ECO:0000303|PubMed:9516047};
DE   Contains:
DE     RecName: Full=Caerin-1.6.1 {ECO:0000303|PubMed:9516047};
OS   Ranoidea chloris (Red-eyed tree frog) (Litoria chloris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=86064;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-25, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=9516047; DOI=10.1111/j.1399-3011.1998.tb00629.x;
RA   Steinborner S.T., Currie G.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "New antibiotic caerin 1 peptides from the skin secretion of the Australian
RT   tree frog Litoria chloris. Comparison of the activities of the caerin 1
RT   peptides from the genus Litoria.";
RL   J. Pept. Res. 51:121-126(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=11784303; DOI=10.1046/j.0014-2956.2002.02630.x;
RA   Doyle J., Llewellyn L.E., Brinkworth C.S., Bowie J.H., Wegener K.L.,
RA   Rozek T., Wabnitz P.A., Wallace J.C., Tyler M.J.;
RT   "Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation
RT   of lesuerin from the skin secretion of the Australian stony creek frog
RT   Litoria lesueuri.";
RL   Eur. J. Biochem. 269:100-109(2002).
CC   -!- FUNCTION: [Caerin-1.6]: Antimicrobial peptide (PubMed:9516047). Adopts
CC       an alpha helical conformation which can disrupt bacterial membranes
CC       (PubMed:9516047). Strongly inhibits the formation of NO by neuronal
CC       nitric oxide synthase (nNOS) at micromolar concentrations
CC       (PubMed:11784303). Acts by a non-competitive mechanism, probably by
CC       binding to calcium/calmodulin and as a consequence blocking calmodulin
CC       attachment to nNOS (By similarity). {ECO:0000250|UniProtKB:P81252,
CC       ECO:0000269|PubMed:11784303, ECO:0000269|PubMed:9516047}.
CC   -!- FUNCTION: [Caerin-1.6.1]: Does not show antimicrobial activity.
CC       {ECO:0000269|PubMed:9516047}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9516047}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000305|PubMed:9516047}.
CC   -!- DOMAIN: Contains two amphipathic alpha helix regions separated by a
CC       region of less-defined helicity and greater flexibility. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P62547; -.
DR   SMR; P62547; -.
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:0045087; P:innate immune response; 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; Immunity; Innate immunity; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Caerin-1.6"
FT                   /evidence="ECO:0000269|PubMed:9516047"
FT                   /id="PRO_0000010178"
FT   PEPTIDE         3..25
FT                   /note="Caerin-1.6.1"
FT                   /evidence="ECO:0000269|PubMed:9516047"
FT                   /id="PRO_0000010179"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:9516047"
SQ   SEQUENCE   25 AA;  2594 MW;  82B97580BB0EB36D CRC64;
     GLFSVLGAVA KHVLPHVVPV IAEKL