DA2D_PHYBI
ID DA2D_PHYBI Reviewed; 227 AA.
AC P21850;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=[D-Ala2]-deltorphins;
DE Contains:
DE RecName: Full=[D-Ala2]-dermorphin-like 1;
DE Contains:
DE RecName: Full=[D-Ala2]-dermorphin-like 2;
DE Contains:
DE RecName: Full=[D-Ala2]-deltorphin-2;
DE AltName: Full=[D-Ala2]-deltorphin II;
DE Contains:
DE RecName: Full=[D-Ala2]-deltorphin-1;
DE AltName: Full=[D-Ala2]-deltorphin I;
DE Flags: Precursor;
OS Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], D-AMINO ACID AT ALA-50; ALA-79; ALA-108;
RP ALA-144; ALA-180 AND ALA-216, AND AMIDATION AT GLY-113; GLY-149; GLY-185
RP AND GLY-221.
RC TISSUE=Skin;
RX PubMed=2352951; DOI=10.1073/pnas.87.12.4836;
RA Richter K., Egger R., Negri L., Corsi R., Severini C., Kreil G.;
RT "cDNAs encoding [D-Ala2]deltorphin precursors from skin of Phyllomedusa
RT bicolor also contain genetic information for three dermorphin-related
RT opioid peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4836-4839(1990).
CC -!- FUNCTION: Deltorphin is a heptapeptide with a very potent opiate-like
CC activity. Has high affinity and selectivity for delta-type opioid
CC receptors. The two dermorphin-like peptides have a similar affinity and
CC selectivity for the mu opioid receptor as dermorphin.
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; M34560; AAA49451.1; -; mRNA.
DR PIR; A35514; A35514.
DR PIR; S21230; S21230.
DR PIR; S36662; S36662.
DR AlphaFoldDB; P21850; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
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; Endorphin; Opioid peptide; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..46
FT /id="PRO_0000010204"
FT PEPTIDE 49..55
FT /note="[D-Ala2]-dermorphin-like 1"
FT /id="PRO_0000010205"
FT PROPEP 57..75
FT /id="PRO_0000010206"
FT PEPTIDE 78..83
FT /note="[D-Ala2]-dermorphin-like 2"
FT /id="PRO_0000010207"
FT PROPEP 86..104
FT /id="PRO_0000010208"
FT PEPTIDE 107..113
FT /note="[D-Ala2]-deltorphin-2"
FT /id="PRO_0000010209"
FT PROPEP 115..140
FT /id="PRO_0000010210"
FT PEPTIDE 143..149
FT /note="[D-Ala2]-deltorphin-1"
FT /id="PRO_0000010211"
FT PROPEP 151..176
FT /id="PRO_0000010212"
FT PEPTIDE 179..185
FT /note="[D-Ala2]-deltorphin-1"
FT /id="PRO_0000010213"
FT PROPEP 187..212
FT /id="PRO_0000010214"
FT PEPTIDE 215..221
FT /note="[D-Ala2]-deltorphin-1"
FT /id="PRO_0000010215"
FT PROPEP 223..227
FT /id="PRO_0000010216"
FT REGION 22..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 79
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 108
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 113
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 144
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 149
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 180
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 185
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 216
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:2352951"
FT MOD_RES 221
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:2352951"
FT VARIANT 53..54
FT /note="Missing (in clone AD3)"
FT VARIANT 120..227
FT /note="Missing (in clone AD7)"
FT VARIANT 156..227
FT /note="Missing (in clone AD8)"
SQ SEQUENCE 227 AA; 26934 MW; 08CE573BAE362130 CRC64;
MSFLKKSLLL VLFLGLVSHS VCKEEKRETE EENENEEENH EVGSEMKRYA FWYPNRDTEE
KNENEEENQE EGSEMKRYAF GYPKREPEEE NENEEENHEE GSEMKRYAFE VVGGEAKKMK
REPEEENENE EENHEEGSEM KRYAFDVVGG EAKKMKREPE EENENEEENH EEGSEMKRYA
FDVVGGEAKK MKREPEEENE NEEENHEEGS EMKRYAFDVV GGEAKKM
