ID   CT11_RANCI              Reviewed;          16 AA.
AC   P81835; P81836; P81837;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Citropin-1.1 {ECO:0000303|PubMed:10504394};
DE   Contains:
DE     RecName: Full=Citropin-1.1.1 {ECO:0000303|PubMed:10504394};
DE   Contains:
DE     RecName: Full=Citropin-1.1.2 {ECO:0000303|PubMed:10504394};
OS   Ranoidea citropa (Australian Blue Mountains tree frog) (Litoria citropa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=94770;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AMIDATION AT LEU-16, SUBCELLULAR LOCATION, AND
RP   STRUCTURE BY NMR.
RC   TISSUE=Skin secretion;
RX   PubMed=10504394; DOI=10.1046/j.1432-1327.1999.00750.x;
RA   Wegener K.L., Wabnitz P.A., Carver J.A., Bowie J.H., Chia B.C.S.,
RA   Wallace J.C., Tyler M.J.;
RT   "Host defence peptides from the skin glands of the Australian blue
RT   mountains tree-frog Litoria citropa. Solution structure of the
RT   antibacterial peptide citropin 1.1.";
RL   Eur. J. Biochem. 265:627-637(1999).
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: Bacteriostatic action for Gram-positive bacteria
CC       (PubMed:10504394). 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 (PubMed:11784303). {ECO:0000269|PubMed:10504394,
CC       ECO:0000269|PubMed:11784303}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10504394}.
CC   -!- TISSUE SPECIFICITY: Expressed by the dorsal and submental skin glands.
CC       {ECO:0000305|PubMed:10504394}.
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DR   AlphaFoldDB; P81835; -.
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; IPR013157; Aurein_antimicrobial_peptide.
DR   Pfam; PF08256; Antimicrobial20; 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..16
FT                   /note="Citropin-1.1"
FT                   /evidence="ECO:0000269|PubMed:10504394"
FT                   /id="PRO_0000010190"
FT   PEPTIDE         3..16
FT                   /note="Citropin-1.1.1"
FT                   /evidence="ECO:0000269|PubMed:10504394"
FT                   /id="PRO_0000010191"
FT   PEPTIDE         4..16
FT                   /note="Citropin-1.1.2"
FT                   /evidence="ECO:0000269|PubMed:10504394"
FT                   /id="PRO_0000010192"
FT   MOD_RES         16
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:10504394"
SQ   SEQUENCE   16 AA;  1616 MW;  1D87851F98D73DE9 CRC64;
     GLFDVIKKVA SVIGGL