ID   TPFY_AGADC              Reviewed;          62 AA.
AC   P83455; Q8AXT9;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Tryptophyllin-1;
DE   AltName: Full=PdT-1;
DE   Flags: Precursor;
OS   Agalychnis dacnicolor (Giant mexican leaf frog) (Pachymedusa dacnicolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=75988 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-60, MASS SPECTROMETRY,
RP   HYDROXYLATION AT PRO-56, AND AMIDATION AT PRO-60.
RC   TISSUE=Skin {ECO:0000269|PubMed:14687697}, and
RC   Skin secretion {ECO:0000269|PubMed:14687697};
RX   PubMed=14687697; DOI=10.1016/j.regpep.2003.08.004;
RA   Chen T.B., Orr D.F., O'Rourke M., McLynn C., Bjourson A.J., McClean S.,
RA   Hirst D., Rao P., Shaw C.;
RT   "Pachymedusa dacnicolor tryptophyllin-1: structural characterization,
RT   pharmacological activity and cloning of precursor cDNA.";
RL   Regul. Pept. 117:25-32(2004).
CC   -!- FUNCTION: Myoactive. Has selective relaxing activity on vascular smooth
CC       muscle. {ECO:0000269|PubMed:14687697}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14687697}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:14687697}.
CC   -!- MASS SPECTROMETRY: Mass=809.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14687697};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Tryptophillin subfamily. {ECO:0000255}.
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DR   EMBL; AJ507318; CAD45365.1; -; mRNA.
DR   AlphaFoldDB; P83455; -.
DR   TCDB; 1.C.52.1.8; the dermaseptin (dermaseptin) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; 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; Direct protein sequencing;
KW   Hydroxylation; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..53
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:14687697"
FT                   /id="PRO_5000068813"
FT   PEPTIDE         54..60
FT                   /note="Tryptophyllin-1"
FT                   /evidence="ECO:0000269|PubMed:14687697"
FT                   /id="PRO_0000043845"
FT   REGION          25..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:14687697"
FT   MOD_RES         60
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:14687697"
SQ   SEQUENCE   62 AA;  7346 MW;  DAE56084D89E248F CRC64;
     MNFLKKSLFL VLFLGFVSIS FCDEEKRQDD DEGNEREEKK EIQEDGNQEE RRDKPPAWVP
     GK