ID   DEM_PITAZ               Reviewed;           7 AA.
AC   P85887;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 13.
DE   RecName: Full=Dermorphin {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]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, HYDROXYLATION AT PRO-6, AMIDATION AT
RP   SER-7, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
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   -!- FUNCTION: Dermorphin has a very potent opiate-like activity. It has
CC       high affinity and selectivity for mu-type opioid receptors (By
CC       similarity). {ECO:0000250|UniProtKB:P05422}.
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=818.38; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17696382};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermorphin subfamily. {ECO:0000255}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Direct protein sequencing; Endorphin;
KW   Hydroxylation; Opioid peptide; Secreted.
FT   PEPTIDE         1..7
FT                   /note="Dermorphin"
FT                   /evidence="ECO:0000269|PubMed:17696382"
FT                   /id="PRO_0000345631"
FT   MOD_RES         6
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17696382"
FT   MOD_RES         7
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:17696382"
SQ   SEQUENCE   7 AA;  804 MW;  75A77B5879CDCB30 CRC64;
     YAFGYPS