ID   TY01_PITAZ              Reviewed;          61 AA.
AC   Q0VKG8; P84945;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Tryptophyllin-T1 {ECO:0000303|PubMed:17696382};
DE            Short=Pha-T1 {ECO:0000303|PubMed:17696382};
DE   AltName: Full=Tryptophyllin-5 {ECO:0000303|PubMed:17696382};
DE   AltName: Full=Tryptophyllin-HA5 {ECO:0000303|PubMed:17696382};
DE   Flags: Precursor;
GN   Name=trp-Pha-T1 {ECO:0000303|PubMed:17696382};
OS   Pithecopus azureus (Orange-legged monkey tree frog) (Phyllomedusa azurea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Pithecopus.
OX   NCBI_TaxID=2034991;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAL23475.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-61, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND HYDROXYLATION AT
RP   PRO-56.
RC   TISSUE=Skin, and Skin secretion {ECO:0000269|PubMed:17696382};
RX   PubMed=17696382; DOI=10.1021/pr0702666;
RA   Thompson A.H., Bjourson A.J., Orr D.F., Shaw C., McClean S.;
RT   "Amphibian skin secretomics: application of parallel quadrupole time-of-
RT   flight mass spectrometry and peptide precursor cDNA cloning to rapidly
RT   characterize the skin secretory peptidome of Phyllomedusa hypochondrialis
RT   azurea: discovery of a novel peptide family, the hyposins.";
RL   J. Proteome Res. 6:3604-3613(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17696382}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:17696382}.
CC   -!- MASS SPECTROMETRY: Mass=979.60; Method=MALDI; Note=Without
CC       hydroxylation at Pro-56.; Evidence={ECO:0000269|PubMed:17696382};
CC   -!- MASS SPECTROMETRY: Mass=995.64; Method=MALDI; Note=With hydroxylation
CC       at Pro-56.; Evidence={ECO:0000269|PubMed:17696382};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Tryptophillin subfamily. {ECO:0000255}.
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DR   EMBL; AM292542; CAL23475.1; -; mRNA.
DR   AlphaFoldDB; Q0VKG8; -.
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   Amphibian defense peptide; Direct protein sequencing; Hydroxylation;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..53
FT                   /evidence="ECO:0000269|PubMed:17696382"
FT                   /id="PRO_0000250602"
FT   PEPTIDE         54..61
FT                   /note="Tryptophyllin-T1"
FT                   /evidence="ECO:0000269|PubMed:17696382"
FT                   /id="PRO_0000250603"
FT   REGION          25..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:17696382"
SQ   SEQUENCE   61 AA;  7290 MW;  C1B3566BABE1CB77 CRC64;
     MDFLKKSLFL VLFLGLVSIS LCDEEKRQDD DEASEREEKK EIHEEGNQEE RRDRPPSWIP
     K