DEM_PITHY
ID DEM_PITHY Reviewed; 7 AA.
AC P84523;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 02-DEC-2020, entry version 25.
DE RecName: Full=Dermorphin {ECO:0000303|Ref.1};
DE AltName: Full=Hyp-6 {ECO:0000303|Ref.1};
OS Pithecopus hypochondrialis (Orange-legged leaf frog) (Phyllomedusa
OS hypochondrialis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Pithecopus.
OX NCBI_TaxID=317381;
RN [1]
RP PROTEIN SEQUENCE, HYDROXYLATION AT PRO-6, AMIDATION AT SER-7, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Thompson A.H.;
RT "Bioactive peptides derived from the venom of the South American tree frog,
RT Phyllomedusa hypochondrialis.";
RL Submitted (APR-2005) to UniProtKB.
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|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
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|Ref.1"
FT /id="PRO_0000043783"
FT MOD_RES 6
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 7
FT /note="Serine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 7 AA; 804 MW; 75A77B5879CDCB30 CRC64;
YAFGYPS