DEM1_PHYSA
ID DEM1_PHYSA Reviewed; 197 AA.
AC P05422;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Dermorphin-1;
DE Contains:
DE RecName: Full=Deltorphin;
DE AltName: Full=Dermenkephalin;
DE Contains:
DE RecName: Full=Dermorphin;
DE Flags: Precursor;
OS Phyllomedusa sauvagei (Sauvage's leaf frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8395;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=3659910; DOI=10.1126/science.3659910;
RA Richter K., Egger R., Kreil G.;
RT "D-alanine in the frog skin peptide dermorphin is derived from L-alanine in
RT the precursor.";
RL Science 238:200-202(1987).
RN [2]
RP PROTEIN SEQUENCE OF 48-54; 99-111 AND 115-126, D-AMINO ACID AT MET-49, AND
RP AMIDATION AT ASP-54.
RC TISSUE=Skin secretion;
RX PubMed=2007579; DOI=10.1016/s0021-9258(18)38113-4;
RA Mor A., Delfaour A., Nicolas P.;
RT "Identification of a D-alanine-containing polypeptide precursor for the
RT peptide opioid, dermorphin.";
RL J. Biol. Chem. 266:6264-6270(1991).
RN [3]
RP PROTEIN SEQUENCE OF 48-54, D-AMINO ACID AT MET-49, AMIDATION AT ASP-54, AND
RP FUNCTION.
RC TISSUE=Skin secretion;
RX PubMed=2542051; DOI=10.1016/0014-2999(89)90611-0;
RA Kreil G., Barra D., Simmaco M., Erspamer V., Erspamer G.F., Negri L.,
RA Severini C., Corsi R., Melchiorri P.;
RT "Deltorphin, a novel amphibian skin peptide with high selectivity and
RT affinity for delta opioid receptors.";
RL Eur. J. Pharmacol. 162:123-128(1989).
RN [4]
RP PROTEIN SEQUENCE OF 80-86; 115-121; 150-156 AND 185-191, D-AMINO ACID AT
RP ALA-81; ALA-116; ALA-151 AND ALA-186, AMIDATION AT SER-86; SER-121; SER-156
RP AND SER-191, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Skin secretion;
RX PubMed=7287299; DOI=10.1111/j.1399-3011.1981.tb01993.x;
RA Montecucchi P.C., de Castiglione R., Piani S., Gozzini L., Erspamer V.;
RT "Amino acid composition and sequence of dermorphin, a novel opiate-like
RT peptide from the skin of Phyllomedusa sauvagei.";
RL Int. J. Pept. Protein Res. 17:275-283(1981).
CC -!- FUNCTION: Dermorphin has a very potent opiate-like activity. It has
CC high affinity and selectivity for mu-type opioid receptors.
CC -!- FUNCTION: Deltorphin has a very potent opiate-like activity. It has
CC high affinity and selectivity for delta-type opioid receptors.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:7287299}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermorphin subfamily. {ECO:0000305}.
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DR EMBL; M18031; AAA49453.1; -; mRNA.
DR PIR; A27784; A27784.
DR AlphaFoldDB; P05422; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001515; F:opioid peptide activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW D-amino acid; Direct protein sequencing; Endorphin; Opioid peptide; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..45
FT /id="PRO_0000010233"
FT PEPTIDE 48..54
FT /note="Deltorphin"
FT /id="PRO_0000010234"
FT PROPEP 56..77
FT /id="PRO_0000010235"
FT PEPTIDE 80..86
FT /note="Dermorphin"
FT /id="PRO_0000010236"
FT PROPEP 88..112
FT /id="PRO_0000010237"
FT PEPTIDE 115..121
FT /note="Dermorphin"
FT /id="PRO_0000010238"
FT PROPEP 123..147
FT /id="PRO_0000010239"
FT PEPTIDE 150..156
FT /note="Dermorphin"
FT /id="PRO_0000010240"
FT PROPEP 158..182
FT /id="PRO_0000010241"
FT PEPTIDE 185..191
FT /note="Dermorphin"
FT /id="PRO_0000010242"
FT PROPEP 193..197
FT /id="PRO_0000010243"
FT REGION 24..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="D-methionine"
FT /evidence="ECO:0000269|PubMed:2007579,
FT ECO:0000269|PubMed:2542051"
FT MOD_RES 54
FT /note="Aspartic acid 1-amide"
FT /evidence="ECO:0000269|PubMed:2007579,
FT ECO:0000269|PubMed:2542051"
FT MOD_RES 81
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 86
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 116
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 121
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 151
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 156
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 186
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 191
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
SQ SEQUENCE 197 AA; 23165 MW; 58C6883BC0C9B687 CRC64;
MSFLKKSLLL ILFLGLVSLS VCKEEKRETE EENENEENHE EGSEMKRYMF HLMDGEAKKR
DSEENEIEEN HEEGSEMKRY AFGYPSGEAK KIKRVSEEEN ENEENHEEGS EMKRYAFGYP
SGEAKKIKRE SEEEKEIEEN HEEGSEMKRY AFGYPSGEAK KIKRESEEEN ENEENHEEGS
EMKRYAFGYP SGEAKKM
