P05422 (DEM1_PHYSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Dermorphin-1 Cleaved into the following 2 chains: Deltorphin Alternative name(s): Dermenkephalin Dermorphin
Organism	Phyllomedusa sauvagei (Sauvage's leaf frog)
Taxonomic identifier	8395 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Hyloidea › Hylidae › Phyllomedusinae › Phyllomedusa

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dermorphin has a very potent opiate-like activity. It has high affinity and selectivity for mu-type opioid receptors. Ref.3 Ref.4 Deltorphin has a very potent opiate-like activity. It has high affinity and selectivity for delta-type opioid receptors. Ref.3 Ref.4
Subcellular location	Secreted.
Tissue specificity	Expressed by the skin glands. Ref.4
Sequence similarities	Belongs to the frog skin active peptide (FSAP) family. Dermorphin subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Amphibian defense peptide Endorphin Opioid peptide
PTM	Amidation Cleavage on pair of basic residues D-amino acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from electronic annotation. Source: InterPro neuropeptide signaling pathway Inferred from direct assay Ref.4. Source: UniProtKB
Cellular component	extracellular region Inferred from direct assay Ref.4. Source: UniProtKB
Molecular function	opioid peptide activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 45	25			PRO_0000010233
	Peptide	48 – 54	7	Deltorphin Ref.2 Ref.3		PRO_0000010234
	Propeptide	56 – 77	22			PRO_0000010235
	Peptide	80 – 86	7	Dermorphin Ref.4		PRO_0000010236
	Propeptide	88 – 112	25			PRO_0000010237
	Peptide	115 – 121	7	Dermorphin		PRO_0000010238
	Propeptide	123 – 147	25			PRO_0000010239
	Peptide	150 – 156	7	Dermorphin		PRO_0000010240
	Propeptide	158 – 182	25			PRO_0000010241
	Peptide	185 – 191	7	Dermorphin		PRO_0000010242
	Propeptide	193 – 197	5			PRO_0000010243
Amino acid modifications
	Modified residue	49	1	D-methionine
	Modified residue	54	1	Aspartic acid 1-amide
	Modified residue	81	1	D-alanine (Ala) Ref.4
	Modified residue	86	1	Serine amide Ref.4
	Modified residue	116	1	D-alanine (Ala)
	Modified residue	121	1	Serine amide
	Modified residue	151	1	D-alanine (Ala)
	Modified residue	156	1	Serine amide
	Modified residue	186	1	D-alanine (Ala)
	Modified residue	191	1	Serine amide

Sequences

	Sequence		Length	Mass (Da)
	P05422 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 58C6883BC0C9B687	FASTA	197	23,165
	10 20 30 40 50 60 MSFLKKSLLL ILFLGLVSLS VCKEEKRETE EENENEENHE EGSEMKRYMF HLMDGEAKKR 70 80 90 100 110 120 DSEENEIEEN HEEGSEMKRY AFGYPSGEAK KIKRVSEEEN ENEENHEEGS EMKRYAFGYP 130 140 150 160 170 180 SGEAKKIKRE SEEEKEIEEN HEEGSEMKRY AFGYPSGEAK KIKRESEEEN ENEENHEEGS 190 EMKRYAFGYP SGEAKKM

References

[1]	"D-alanine in the frog skin peptide dermorphin is derived from L-alanine in the precursor." Richter K., Egger R., Kreil G. Science 238:200-202(1987) [PubMed: 3659910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skin.
[2]	"Identification of a D-alanine-containing polypeptide precursor for the peptide opioid, dermorphin." Mor A., Delfaour A., Nicolas P. J. Biol. Chem. 266:6264-6270(1991) [PubMed: 2007579] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-54; 99-111 AND 115-126. Tissue: Skin secretion.
[3]	"Deltorphin, a novel amphibian skin peptide with high selectivity and affinity for delta opioid receptors." Kreil G., Barra D., Simmaco M., Erspamer V., Erspamer G.F., Negri L., Severini C., Corsi R., Melchiorri P. Eur. J. Pharmacol. 162:123-128(1989) [PubMed: 2542051] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-54, FUNCTION. Tissue: Skin secretion.
[4]	"Amino acid composition and sequence of dermorphin, a novel opiate-like peptide from the skin of Phyllomedusa sauvagei." Montecucchi P.C., de Castiglione R., Piani S., Gozzini L., Erspamer V. Int. J. Pept. Protein Res. 17:275-283(1981) [PubMed: 7287299] [Abstract] Cited for: PROTEIN SEQUENCE OF 80-86, D-AMINO ACID AT ALA-81, AMIDATION AT SER-86, FUNCTION, TISSUE SPECIFICITY. Tissue: Skin secretion.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M18031 mRNA. Translation: AAA49453.1.
PIR	A27784.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG005448.
Family and domain databases
InterPro	IPR004275. Brevinin. [Graphical view]
Pfam	PF03032. Brevenin. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DEM1_PHYSA

Accession

Primary (citable) accession number: P05422

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	March 2, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program