ID   DEM_AGADC               Reviewed;         201 AA.
AC   O93456;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Dermorphin peptides;
DE   Contains:
DE     RecName: Full=[Ile2]-deltorphin;
DE   Contains:
DE     RecName: Full=Dermorphin;
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:0000312|EMBL:CAA06546.1};
RN   [1] {ECO:0000312|EMBL:CAA06546.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], D-AMINO ACID AT ILE-190, AND SYNTHESIS OF
RP   189-195.
RC   TISSUE=Skin {ECO:0000305};
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:P05422}.
CC   -!- FUNCTION: Deltorphin has a very potent opiate-like activity. It has
CC       high affinity and selectivity for delta-type opioid receptors (By
CC       similarity). {ECO:0000250|UniProtKB:P05422}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; AJ005443; CAA06546.1; -; mRNA.
DR   AlphaFoldDB; O93456; -.
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.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   D-amino acid; Endorphin; Opioid peptide; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000010222"
FT   PEPTIDE         49..55
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010223"
FT   PROPEP          57..82
FT                   /id="PRO_0000010224"
FT   PEPTIDE         85..91
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010225"
FT   PROPEP          93..118
FT                   /id="PRO_0000010226"
FT   PEPTIDE         121..127
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010227"
FT   PROPEP          129..154
FT                   /id="PRO_0000010228"
FT   PEPTIDE         157..163
FT                   /note="Dermorphin"
FT                   /id="PRO_0000010229"
FT   PROPEP          165..186
FT                   /id="PRO_0000010230"
FT   PEPTIDE         189..195
FT                   /note="[Ile2]-deltorphin"
FT                   /id="PRO_0000010231"
FT   PROPEP          196..201
FT                   /id="PRO_0000010232"
FT   REGION          26..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         55
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         86
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         91
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         122
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         127
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         158
FT                   /note="D-alanine (Ala)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         163
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="D-allo-isoleucine"
FT                   /evidence="ECO:0000269|PubMed:9657380"
SQ   SEQUENCE   201 AA;  23887 MW;  2F324D6701CDDA31 CRC64;
     MSFLKKSLLL ILFLGLVSLS ICEEQKREIE EDENENEEER NEASEMKRYA FGYPSGEEKK
     IKRETEEDEN ENEEERNEAS EMKRYAFGYP SGEEKKIKRE TEEDENENEE ERNEASEMKR
     YAFGYPSGEE KKIKRETEED ENENEEERNE GSEMKRYAFG YPSGGAKRMK RKPVEEEENH
     VAGSKMKRYI FHLMDGEVKK I