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Dermorphin-2 [Cleaved into: Dermorphin] (Fragment)

 DEM2_PHYSA              Reviewed;         198 AA.
P05421;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
20-JAN-2016, entry version 58.
RecName: Full=Dermorphin-2;
Contains:
RecName: Full=Dermorphin;
Flags: Precursor; Fragment;
Phyllomedusa sauvagei (Sauvage's leaf frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae;
Phyllomedusinae; Phyllomedusa.
NCBI_TaxID=8395;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
PubMed=3659910; DOI=10.1126/science.3659910;
Richter K., Egger R., Kreil G.;
"D-alanine in the frog skin peptide dermorphin is derived from L-
alanine in the precursor.";
Science 238:200-202(1987).
[2]
PROTEIN SEQUENCE OF 48-54; 83-89; 118-124; 153-159 AND 188-194,
D-AMINO ACID AT ALA-49; ALA-84; ALA-119; ALA-154 AND ALA-189,
AMIDATION AT SER-54; SER-89; SER-124; SER-159 AND SER-194, AND
FUNCTION.
TISSUE=Skin secretion;
PubMed=7287299;
Montecucchi P.C., de Castiglione R., Piani S., Gozzini L.,
Erspamer V.;
"Amino acid composition and sequence of dermorphin, a novel opiate-
like peptide from the skin of Phyllomedusa sauvagei.";
Int. J. Pept. Protein Res. 17:275-283(1981).
-!- FUNCTION: Dermorphin has a very potent opiate-like activity. It
has high affinity and selectivity for mu-type opioid receptors.
{ECO:0000269|PubMed:7287299}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- 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; M18030; AAA49452.1; -; mRNA.
PIR; B27784; B27784.
HOVERGEN; HBG005448; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0001515; F:opioid peptide activity; IDA:UniProtKB.
GO; GO:0006952; P:defense response; IDA:UniProtKB.
GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
InterPro; IPR004275; Frog_antimicrobial_propeptide.
Pfam; PF03032; FSAP_sig_propep; 1.
1: Evidence at protein level;
Amidation; Amphibian defense peptide;
Cleavage on pair of basic residues; D-amino acid;
Direct protein sequencing; Endorphin; Opioid peptide; Repeat;
Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 45
/FTId=PRO_0000010244.
PEPTIDE 48 54 Dermorphin. {ECO:0000269|PubMed:3659910}.
/FTId=PRO_0000010245.
PROPEP 56 80
/FTId=PRO_0000010246.
PEPTIDE 83 89 Dermorphin. {ECO:0000269|PubMed:3659910}.
/FTId=PRO_0000010247.
PROPEP 91 115
/FTId=PRO_0000010248.
PEPTIDE 118 124 Dermorphin. {ECO:0000269|PubMed:3659910}.
/FTId=PRO_0000010249.
PROPEP 126 150
/FTId=PRO_0000010250.
PEPTIDE 153 159 Dermorphin.
/FTId=PRO_0000010251.
PROPEP 161 185
/FTId=PRO_0000010252.
PEPTIDE 188 194 Dermorphin.
/FTId=PRO_0000010253.
PROPEP 196 198
/FTId=PRO_0000010254.
MOD_RES 49 49 D-alanine (Ala).
{ECO:0000269|PubMed:7287299}.
MOD_RES 54 54 Serine amide.
{ECO:0000269|PubMed:3659910,
ECO:0000269|PubMed:7287299}.
MOD_RES 84 84 D-alanine (Ala).
{ECO:0000269|PubMed:3659910,
ECO:0000269|PubMed:7287299}.
MOD_RES 89 89 Serine amide.
{ECO:0000269|PubMed:3659910,
ECO:0000269|PubMed:7287299}.
MOD_RES 119 119 D-alanine (Ala).
{ECO:0000269|PubMed:3659910,
ECO:0000269|PubMed:7287299}.
MOD_RES 124 124 Serine amide.
{ECO:0000269|PubMed:3659910,
ECO:0000269|PubMed:7287299}.
MOD_RES 154 154 D-alanine (Ala).
{ECO:0000269|PubMed:7287299}.
MOD_RES 159 159 Serine amide.
{ECO:0000269|PubMed:7287299}.
MOD_RES 189 189 D-alanine (Ala).
{ECO:0000269|PubMed:7287299}.
MOD_RES 194 194 Serine amide.
{ECO:0000269|PubMed:7287299}.
NON_TER 198 198
SEQUENCE 198 AA; 23138 MW; 6E3EDB2B56BDC4EA CRC64;
MSFLKKSLLL ILFLGLVSLS VCKEEKRVSE EENENEENHE EGSEMKRYAF GYPSGEAKKI
KRESEEEKEI EENHEEGSEM KRYAFGYPSG EAKKIKRESE EENENEENHE EGSEMKRYAF
GYPSGEAKKI KRESEEEKEI EENHEEGSEM KRYAFGYPSG EAKKIKRESE EENENEENHE
EGSEMKRYAF GYPSGEAK


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