ID   CZS1_CRUCA              Reviewed;          70 AA.
AC   A0A193H395;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Cruzioseptin-1 {ECO:0000303|PubMed:27321580};
DE            Short=CZS-1 {ECO:0000303|PubMed:27321580};
DE   Flags: Precursor;
OS   Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Cruziohyla.
OX   NCBI_TaxID=318249 {ECO:0000312|EMBL:ANN87758.1};
RN   [1] {ECO:0000312|EMBL:ANN87758.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS, SUBCELLULAR LOCATION,
RP   AMIDATION AT PHE-65, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000312|EMBL:ANN87758.1};
RX   PubMed=27321580; DOI=10.1016/j.jprot.2016.06.017;
RA   Proano-Bolanos C., Zhou M., Wang L., Coloma L.A., Chen T., Shaw C.;
RT   "Peptidomic approach identifies cruzioseptins, a new family of potent
RT   antimicrobial peptides in the splendid leaf frog, Cruziohyla calcarifer.";
RL   J. Proteomics 146:1-13(2016).
CC   -!- FUNCTION: Has antimicrobial activity against Gram-negative bacterium
CC       E.coli (MIC=15.11 uM), aginst Gram-positive bacterium S.aureus
CC       (MIC=3.77 uM) and against fungus C.albicans (MIC=3.77 uM). At higher
CC       concentrations also has a bactericidal and fungicidal effect. Has
CC       hemagglutinating activity against horse erythrocytes.
CC       {ECO:0000269|PubMed:27321580}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27321580}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:27321580}.
CC   -!- MASS SPECTROMETRY: Mass=2117.26; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:27321580};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Cruzioseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02713";
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DR   EMBL; KX065078; ANN87758.1; -; mRNA.
DR   AlphaFoldDB; A0A193H395; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
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; Fungicide; Hemagglutinin; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /evidence="ECO:0000305|PubMed:27321580"
FT                   /id="PRO_0000439459"
FT   PEPTIDE         45..65
FT                   /note="Cruzioseptin-1"
FT                   /evidence="ECO:0000269|PubMed:27321580"
FT                   /id="PRO_0000439460"
FT   PROPEP          66..70
FT                   /evidence="ECO:0000305|PubMed:27321580"
FT                   /id="PRO_0000439461"
FT   MOD_RES         65
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:27321580"
SQ   SEQUENCE   70 AA;  7935 MW;  F805FE197E26A5CE CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKREEN EEEQDDDEQS EEKRGFLDIV KGVGKVALGA
     VSKLFGQEER