ID   DEM_AGAAN               Reviewed;          86 AA.
AC   O93227;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Dermorphin peptides;
DE   Contains:
DE     RecName: Full=Dermorphin;
DE   Flags: Precursor; Fragment;
OS   Agalychnis annae (Blue-sided leaf frog) (Phyllomedusa annae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=75990 {ECO:0000312|EMBL:CAA06547.1};
RN   [1] {ECO:0000312|EMBL:CAA06547.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin {ECO:0000269|PubMed:9657380};
RX   PubMed=9657380; DOI=10.1016/s0014-5793(98)00545-6;
RA   Wechselberger C., Severini C., Kreil G., Negri L.;
RT   "A new opioid peptide predicted from cloned cDNAs from skin of Pachymedusa
RT   dacnicolor and Agalychnis annae.";
RL   FEBS Lett. 429:41-43(1998).
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:P05421}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9657380}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermorphin subfamily. {ECO:0000305}.
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DR   EMBL; AJ005444; CAA06547.1; -; mRNA.
DR   AlphaFoldDB; O93227; -.
DR   PRIDE; O93227; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0001515; F:opioid peptide activity; ISS:UniProtKB.
DR   GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   D-amino acid; Endorphin; Opioid peptide; Repeat; Secreted.
FT   PROPEP          1..24
FT                   /id="PRO_0000010217"
FT   PEPTIDE         27..33
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010218"
FT   PROPEP          35..61
FT                   /id="PRO_0000010219"
FT   PEPTIDE         64..70
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010220"
FT   PROPEP          72..86
FT                   /id="PRO_0000010221"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         28
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         65
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAA06547.1"
SQ   SEQUENCE   86 AA;  10443 MW;  E2DA64B6A5CC7ACF CRC64;
     KKIKRETEED ENENEEERNE RSEMKRYAFG YPSGEEKKIK RETEEDENEN EEERNEEGSE
     MKRYAFGYPS GEAKRMKRKP AEEETE