ID   CR11_RANCA              Reviewed;          75 AA.
AC   Q800R2; P56226;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Caerin-1.1 {ECO:0000303|PubMed:12709067};
DE   Contains:
DE     RecName: Full=Caerin-1.1.1 {ECO:0000303|Ref.2};
DE   Contains:
DE     RecName: Full=Caerin-1.1.2 {ECO:0000303|Ref.2};
DE   Contains:
DE     RecName: Full=Caerin-1.1.4 {ECO:0000303|Ref.2};
DE   Flags: Precursor;
OS   Ranoidea caerulea (Green tree frog) (Litoria caerulea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=30344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=12709067; DOI=10.1046/j.1432-1033.2003.03584.x;
RA   Vanhoye D., Bruston F., Nicolas P., Amiche M.;
RT   "Antimicrobial peptides from hylid and ranin frogs originated from a 150-
RT   million-year-old ancestral precursor with a conserved signal peptide but a
RT   hypermutable antimicrobial domain.";
RL   Eur. J. Biochem. 270:2068-2081(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-74, AMIDATION AT LEU-74, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Parotoid gland;
RA   Stone D.J.M., Waugh R.J., Bowie J.H., Wallace J.C., Tyler M.J.;
RT   "Peptides from Australian frogs. The structures of the caerins from Litoria
RT   caerula.";
RL   J. Chem. Res. 138:910-936(1993).
CC   -!- FUNCTION: [Caerin-1.1]: Antimicrobial peptide with antibacterial and
CC       antiviral activities (By similarity). Adopts an alpha helical
CC       conformation which can disrupt bacterial membranes (By similarity).
CC       Inhibits the formation of NO by neuronal nitric oxide synthase (nNOS)
CC       at micromolar concentrations (By similarity). Acts by a non-competitive
CC       mechanism, probably by binding to calcium/calmodulin and as a
CC       consequence blocking calmodulin attachment to nNOS (By similarity).
CC       {ECO:0000250|UniProtKB:P62568, ECO:0000250|UniProtKB:P81252}.
CC   -!- FUNCTION: [Caerin-1.1.1]: Is inactive. {ECO:0000250|UniProtKB:P62568}.
CC   -!- FUNCTION: [Caerin-1.1.4]: Is inactive. {ECO:0000250|UniProtKB:P62568}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin parotoid and/or rostral
CC       glands. {ECO:0000305|Ref.2}.
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 and Caerin-1.1.4 are inactive.
CC   -!- MASS SPECTROMETRY: [Caerin-1.1]: Mass=2582; Method=FAB;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.1]: Mass=2412; Method=FAB;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.2]: Mass=2299; Method=FAB;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MASS SPECTROMETRY: [Caerin-1.1.4]: Mass=2333; Method=FAB;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   EMBL; AY218785; AAO62960.1; -; mRNA.
DR   AlphaFoldDB; Q800R2; -.
DR   TCDB; 1.C.52.1.9; the dermaseptin (dermaseptin) family.
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   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR010000; Caerin_1.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF07440; Caerin_1; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Antiviral defense; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|Ref.2"
FT                   /id="PRO_0000010159"
FT   PEPTIDE         50..74
FT                   /note="Caerin-1.1"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000010160"
FT   PEPTIDE         50..72
FT                   /note="Caerin-1.1.4"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000010161"
FT   PEPTIDE         52..74
FT                   /note="Caerin-1.1.1"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000010162"
FT   PEPTIDE         53..74
FT                   /note="Caerin-1.1.2"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000010163"
FT   REGION          24..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   75 AA;  8281 MW;  D4A852F80031299D CRC64;
     MASLKKSLFL VLLLGFVSVS ICEEEKRQED EDEHEEEGES QEEGSEEKRG LLSVLGSVAK
     HVLPHVVPVI AEHLG