P05421 (DEM2_PHYSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Dermorphin-2 Cleaved into the following chain: 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	198 AA.
Sequence status	Fragment.
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.2
Subcellular location	Secreted.
Tissue specificity	Expressed by the skin glands.
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.2. Source: UniProtKB
Cellular component	extracellular region Inferred from direct assay Ref.2. Source: UniProtKB
Molecular function	opioid peptide activity Inferred from direct assay Ref.2. 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_0000010244
	Peptide	48 – 54	7	Dermorphin Ref.1 Ref.2		PRO_0000010245
	Propeptide	56 – 80	25			PRO_0000010246
	Peptide	83 – 89	7	Dermorphin Ref.1		PRO_0000010247
	Propeptide	91 – 115	25			PRO_0000010248
	Peptide	118 – 124	7	Dermorphin Ref.1		PRO_0000010249
	Propeptide	126 – 150	25			PRO_0000010250
	Peptide	153 – 159	7	Dermorphin		PRO_0000010251
	Propeptide	161 – 185	25			PRO_0000010252
	Peptide	188 – 194	7	Dermorphin		PRO_0000010253
	Propeptide	196 – 198	3			PRO_0000010254
Amino acid modifications
	Modified residue	49	1	D-alanine (Ala) Ref.2
	Modified residue	54	1	Serine amide Ref.1 Ref.2
	Modified residue	84	1	D-alanine (Ala) Ref.1
	Modified residue	89	1	Serine amide Ref.1
	Modified residue	119	1	D-alanine (Ala) Ref.1
	Modified residue	124	1	Serine amide Ref.1
	Modified residue	154	1	D-alanine (Ala)
	Modified residue	159	1	Serine amide
	Modified residue	189	1	D-alanine (Ala)
	Modified residue	194	1	Serine amide
Experimental info
	Non-terminal residue	198	1

Sequences

	Sequence		Length	Mass (Da)
	P05421 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 6E3EDB2B56BDC4EA	FASTA	198	23,138
	10 20 30 40 50 60 MSFLKKSLLL ILFLGLVSLS VCKEEKRVSE EENENEENHE EGSEMKRYAF GYPSGEAKKI 70 80 90 100 110 120 KRESEEEKEI EENHEEGSEM KRYAFGYPSG EAKKIKRESE EENENEENHE EGSEMKRYAF 130 140 150 160 170 180 GYPSGEAKKI KRESEEEKEI EENHEEGSEM KRYAFGYPSG EAKKIKRESE EENENEENHE 190 EGSEMKRYAF GYPSGEAK

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]	"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 48-54, D-AMINO ACID AT ALA-49, AMIDATION AT SER-54, FUNCTION. Tissue: Skin secretion.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M18030 mRNA. Translation: AAA49452.1.
PIR	B27784.
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

DEM2_PHYSA

Accession

Primary (citable) accession number: P05421

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	March 2, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program