ID   CR1B_RANCA              Reviewed;          75 AA.
AC   Q800R9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Caerin 1.11 {ECO:0000303|PubMed:12709067};
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], FUNCTION, SYNTHESIS OF 50-74, AND AMIDATION AT
RP   LEU-74.
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).
CC   -!- FUNCTION: Cationic amphipathic alpha-helical antimicrobial peptide with
CC       weak or no activity against both Gram-positive and Gram-negative
CC       bacteria (PubMed:12709067). Is weakly active against E.coli (MIC=25
CC       uM), E.cloacae (MIC=50 uM), K.pneumoniae (MIC=25 uM), and
CC       S.haemolyticus (MIC=50 uM) (PubMed:12709067). Has no activity against
CC       S.typhimurium, S.enteritidis, B.megaterium, and S.aureus (MIC>100 uM)
CC       (PubMed:12709067). {ECO:0000269|PubMed:12709067}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12709067}. Target
CC       cell membrane {ECO:0000305|PubMed:12709067}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:12709067}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Caerin subfamily. {ECO:0000305}.
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DR   EMBL; AY218778; AAO62953.1; -; mRNA.
DR   AlphaFoldDB; Q800R9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Cleavage on pair of basic residues; Immunity; Innate immunity; Membrane;
KW   Secreted; Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:12709067"
FT                   /id="PRO_0000449904"
FT   PEPTIDE         50..74
FT                   /note="Caerin 1.11"
FT                   /evidence="ECO:0000305|PubMed:12709067"
FT                   /id="PRO_5004295650"
FT   REGION          24..48
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:0000305|PubMed:12709067"
SQ   SEQUENCE   75 AA;  8381 MW;  840CA0FAF2CDD39A CRC64;
     MASLKKSLFL VLFLGFVSVS ICEEEKRQED EDEHEEEGEN QEEGSEEKRG LFSVLGSVAK
     HVVPRVVPVI AEHLG