ID   DRSA_AGACL              Reviewed;          81 AA.
AC   B6HY15;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Adenoregulin-related peptide {ECO:0000303|PubMed:18555027};
DE   AltName: Full=ARP-AC1 {ECO:0000303|PubMed:18555027};
DE   Flags: Precursor;
OS   Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=197464;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-78, FUNCTION,
RP   SUBCELLULAR LOCATION, AMIDATION AT ILE-78, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=18555027; DOI=10.1016/j.biochi.2008.04.016;
RA   Wang L., Zhou M., McClelland A., Reilly A., Chen T., Gagliardo R.,
RA   Walker B., Shaw C.;
RT   "Novel dermaseptin, adenoregulin and caerin homologs from the Central
RT   American red-eyed leaf frog, Agalychnis callidryas, revealed by functional
RT   peptidomics of defensive skin secretion.";
RL   Biochimie 90:1435-1441(2008).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacterium
CC       M.luteus NCT C2665 and against Gram-negative bacterium E.coli K12D31.
CC       {ECO:0000269|PubMed:18555027}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18555027}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:18555027}.
CC   -!- MASS SPECTROMETRY: Mass=3141.65; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18555027};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000305}.
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DR   EMBL; AM944841; CAQ16441.1; -; mRNA.
DR   AlphaFoldDB; B6HY15; -.
DR   SMR; B6HY15; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000305|PubMed:18555027"
FT                   /id="PRO_0000442276"
FT   PEPTIDE         46..78
FT                   /note="Adenoregulin-related peptide"
FT                   /evidence="ECO:0000269|PubMed:18555027"
FT                   /id="PRO_0000442277"
FT   PROPEP          79..81
FT                   /evidence="ECO:0000305|PubMed:18555027"
FT                   /id="PRO_0000442278"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         78
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:18555027"
SQ   SEQUENCE   81 AA;  8770 MW;  DC08F3E9C56E472D CRC64;
     MAFLKKSLLL VLFLGLVSLS ICEEEKRENE DEEEQEDDEQ SEMKRGMWSK IKEAGKAAAK
     AAAKAAGKAA LDVVSGAIGE Q