DEM2_PHYSA
ID DEM2_PHYSA Reviewed; 198 AA.
AC P05421;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Dermorphin-2;
DE Contains:
DE RecName: Full=Dermorphin;
DE Flags: Precursor; Fragment;
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; 83-89; 118-124; 153-159 AND 188-194, D-AMINO
RP ACID AT ALA-49; ALA-84; ALA-119; ALA-154 AND ALA-189, AMIDATION AT SER-54;
RP SER-89; SER-124; SER-159 AND SER-194, AND FUNCTION.
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 {ECO:0000269|PubMed:7287299}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermorphin subfamily. {ECO:0000305}.
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DR EMBL; M18030; AAA49452.1; -; mRNA.
DR PIR; B27784; B27784.
DR AlphaFoldDB; P05421; -.
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_0000010244"
FT PEPTIDE 48..54
FT /note="Dermorphin"
FT /evidence="ECO:0000269|PubMed:3659910"
FT /id="PRO_0000010245"
FT PROPEP 56..80
FT /id="PRO_0000010246"
FT PEPTIDE 83..89
FT /note="Dermorphin"
FT /evidence="ECO:0000269|PubMed:3659910"
FT /id="PRO_0000010247"
FT PROPEP 91..115
FT /id="PRO_0000010248"
FT PEPTIDE 118..124
FT /note="Dermorphin"
FT /evidence="ECO:0000269|PubMed:3659910"
FT /id="PRO_0000010249"
FT PROPEP 126..150
FT /id="PRO_0000010250"
FT PEPTIDE 153..159
FT /note="Dermorphin"
FT /id="PRO_0000010251"
FT PROPEP 161..185
FT /id="PRO_0000010252"
FT PEPTIDE 188..194
FT /note="Dermorphin"
FT /id="PRO_0000010253"
FT PROPEP 196..198
FT /id="PRO_0000010254"
FT REGION 24..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 54
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:3659910,
FT ECO:0000269|PubMed:7287299"
FT MOD_RES 84
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:3659910,
FT ECO:0000269|PubMed:7287299"
FT MOD_RES 89
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:3659910,
FT ECO:0000269|PubMed:7287299"
FT MOD_RES 119
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:3659910,
FT ECO:0000269|PubMed:7287299"
FT MOD_RES 124
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:3659910,
FT ECO:0000269|PubMed:7287299"
FT MOD_RES 154
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 159
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 189
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:7287299"
FT MOD_RES 194
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:7287299"
FT NON_TER 198
SQ 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
