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Dermorphin peptides [Cleaved into: Dermorphin] (Fragment)

 DEM_AGAAN               Reviewed;          86 AA.
O93227;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 40.
RecName: Full=Dermorphin peptides;
Contains:
RecName: Full=Dermorphin;
Flags: Precursor; Fragment;
Agalychnis annae (Blue-sided leaf frog) (Phyllomedusa annae).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae;
Phyllomedusinae; Agalychnis.
NCBI_TaxID=75990 {ECO:0000312|EMBL:CAA06547.1};
[1] {ECO:0000312|EMBL:CAA06547.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin {ECO:0000269|PubMed:9657380};
PubMed=9657380; DOI=10.1016/S0014-5793(98)00545-6;
Wechselberger C., Severini C., Kreil G., Negri L.;
"A new opioid peptide predicted from cloned cDNAs from skin of
Pachymedusa dacnicolor and Agalychnis annae.";
FEBS Lett. 429:41-43(1998).
-!- FUNCTION: Dermorphin has a very potent opiate-like activity. It
has high affinity and selectivity for mu-type opioid receptors (By
similarity). {ECO:0000250|UniProtKB:P05421}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9657380}.
-!- TISSUE SPECIFICITY: Expressed by the skin glands.
-!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
Dermorphin subfamily. {ECO:0000305}.
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EMBL; AJ005444; CAA06547.1; -; mRNA.
PRIDE; O93227; -.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0001515; F:opioid peptide activity; ISS:UniProtKB.
GO; GO:0006952; P:defense response; ISS:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
2: Evidence at transcript level;
Amidation; Amphibian defense peptide;
Cleavage on pair of basic residues; D-amino acid; Endorphin;
Opioid peptide; Repeat; Secreted.
PROPEP 1 24
/FTId=PRO_0000010217.
PEPTIDE 27 33 Dermorphin.
/FTId=PRO_0000010218.
PROPEP 35 61
/FTId=PRO_0000010219.
PEPTIDE 64 70 Dermorphin.
/FTId=PRO_0000010220.
PROPEP 72 86
/FTId=PRO_0000010221.
MOD_RES 28 28 D-alanine (Ala). {ECO:0000250}.
MOD_RES 33 33 Serine amide. {ECO:0000250}.
MOD_RES 65 65 D-alanine (Ala). {ECO:0000250}.
MOD_RES 70 70 Serine amide. {ECO:0000250}.
NON_TER 1 1 {ECO:0000312|EMBL:CAA06547.1}.
SEQUENCE 86 AA; 10443 MW; E2DA64B6A5CC7ACF CRC64;
KKIKRETEED ENENEEERNE RSEMKRYAFG YPSGEEKKIK RETEEDENEN EEERNEEGSE
MKRYAFGYPS GEAKRMKRKP AEEETE


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