PDYN_RAT
ID PDYN_RAT Reviewed; 248 AA.
AC P06300; Q63193;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Proenkephalin-B;
DE AltName: Full=Beta-neoendorphin-dynorphin;
DE AltName: Full=Preprodynorphin;
DE Contains:
DE RecName: Full=Alpha-neoendorphin;
DE Contains:
DE RecName: Full=Beta-neoendorphin;
DE Contains:
DE RecName: Full=Big dynorphin;
DE Short=Big Dyn;
DE Contains:
DE RecName: Full=Dynorphin A(1-17);
DE Short=Dyn-A17;
DE Short=Dynorphin A;
DE Contains:
DE RecName: Full=Dynorphin A(1-13);
DE Contains:
DE RecName: Full=Dynorphin A(1-8);
DE Contains:
DE RecName: Full=Leu-enkephalin;
DE Contains:
DE RecName: Full=Rimorphin;
DE AltName: Full=Dynorphin B;
DE Short=Dyn-B;
DE AltName: Full=Dynorphin B(1-13);
DE Contains:
DE RecName: Full=Leumorphin;
DE AltName: Full=Dynorphin B-29;
DE Flags: Precursor;
GN Name=Pdyn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2628741; DOI=10.1210/mend-3-12-2070;
RA Douglass J., McMurray C.T., Garrett J.E., Adelman J.P., Calavetta L.;
RT "Characterization of the rat prodynorphin gene.";
RL Mol. Endocrinol. 3:2070-2078(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-248.
RC TISSUE=Hypothalamus;
RX PubMed=3858883; DOI=10.1073/pnas.82.12.4291;
RA Civelli O., Douglass J., Goldstein A., Herbert E.;
RT "Sequence and expression of the rat prodynorphin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4291-4295(1985).
RN [3]
RP PROTEIN SEQUENCE OF 235-248.
RX PubMed=8276115; DOI=10.1016/0014-5793(94)80630-6;
RA Dupuy A., Lindberg I., Zhou Y., Akil H., Lazure C., Chretien M.,
RA Seidah N.G., Day R.;
RT "Processing of prodynorphin by the prohormone convertase PC1 results in
RT high molecular weight intermediate forms. Cleavage at a single arginine
RT residue.";
RL FEBS Lett. 337:60-65(1994).
RN [4]
RP IDENTIFICATION OF RIMORPHIN.
RX PubMed=2874472; DOI=10.1016/0024-3205(86)90020-2;
RA Wolter H.J.;
RT "Identification of the tridecapeptide dynorphin B (rimorphin) within
RT perikarya of rat duodenum.";
RL Life Sci. 39:727-730(1986).
RN [5]
RP CONVERSION OF LEUMORPHIN TO RIMORPHIN.
RX PubMed=2862869; DOI=10.1016/0006-291x(85)91738-3;
RA Devi L., Goldstein A.;
RT "Neuropeptide processing by single-step cleavage: conversion of leumorphin
RT (dynorphin B-29) to dynorphin B.";
RL Biochem. Biophys. Res. Commun. 130:1168-1176(1985).
RN [6]
RP IDENTIFICATION OF BRIDGE PEPTIDE.
RX PubMed=2893267;
RA Day R., Akil H.;
RT "Bridge peptide is a cleavage product of pro-dynorphin processing in the
RT rat anterior pituitary.";
RL NIDA Res. Monogr. 75:244-246(1986).
RN [7]
RP FUNCTION OF LEUMORPHIN.
RX PubMed=16181412; DOI=10.1111/j.1471-4159.2005.03339.x;
RA Lee B.D., Kim S., Hur E.M., Park Y.S., Kim Y.H., Lee T.G., Kim K.T.,
RA Suh P.G., Ryu S.H.;
RT "Leumorphin has an anti-apoptotic effect by activating epidermal growth
RT factor receptor kinase in rat pheochromocytoma PC12 cells.";
RL J. Neurochem. 95:56-67(2005).
CC -!- FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate
CC drugs. They play a role in a number of physiologic functions, including
CC pain perception and responses to stress (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Dynorphin peptides differentially regulate the kappa opioid
CC receptor. Dynorphin A(1-13) has a typical opiod activity, it is 700
CC times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Leumorphin has a typical opiod activity and may have anti-
CC apoptotic effect. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The N-terminal domain contains 6 conserved cysteines thought to be
CC involved in disulfide bonding and/or processing.
CC -!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
CC {ECO:0000305}.
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DR EMBL; M32784; AAA41117.1; -; Genomic_DNA.
DR EMBL; M32783; AAA41117.1; JOINED; Genomic_DNA.
DR EMBL; M10088; AAA41118.1; -; Genomic_DNA.
DR PIR; A41395; DFRTP.
DR AlphaFoldDB; P06300; -.
DR BMRB; P06300; -.
DR ELM; P06300; -.
DR STRING; 10116.ENSRNOP00000038921; -.
DR PaxDb; P06300; -.
DR PRIDE; P06300; -.
DR UCSC; RGD:62054; rat.
DR RGD; 62054; Pdyn.
DR eggNOG; ENOG502RXT4; Eukaryota.
DR InParanoid; P06300; -.
DR PhylomeDB; P06300; -.
DR Reactome; R-RNO-111885; Opioid Signalling.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P06300; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0099013; C:neuronal dense core vesicle lumen; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
DR GO; GO:0031628; F:opioid receptor binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; TAS:RGD.
DR GO; GO:0007600; P:sensory perception; IBA:GO_Central.
DR InterPro; IPR006024; Opioid_neupept.
DR InterPro; IPR000750; Proenkphlin_B.
DR PANTHER; PTHR11438; PTHR11438; 1.
DR PANTHER; PTHR11438:SF4; PTHR11438:SF4; 1.
DR Pfam; PF01160; Opiods_neuropep; 1.
DR PRINTS; PR01028; OPIOIDPRCRSR.
DR PRINTS; PR01030; PENKBPRCRSR.
DR PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Endorphin; Neuropeptide; Neurotransmitter; Opioid peptide;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..163
FT /id="PRO_0000008198"
FT PEPTIDE 166..175
FT /note="Alpha-neoendorphin"
FT /id="PRO_0000306365"
FT PEPTIDE 166..174
FT /note="Beta-neoendorphin"
FT /id="PRO_0000008199"
FT PEPTIDE 166..170
FT /note="Leu-enkephalin"
FT /id="PRO_0000008200"
FT PROPEP 177..199
FT /id="PRO_0000008201"
FT PEPTIDE 202..233
FT /note="Big dynorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306366"
FT PEPTIDE 202..218
FT /note="Dynorphin A(1-17)"
FT /id="PRO_0000008202"
FT PEPTIDE 202..214
FT /note="Dynorphin A(1-13)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306367"
FT PEPTIDE 202..209
FT /note="Dynorphin A(1-8)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306368"
FT PEPTIDE 202..206
FT /note="Leu-enkephalin"
FT /id="PRO_0000008203"
FT PEPTIDE 221..248
FT /note="Leumorphin"
FT /id="PRO_0000008204"
FT PEPTIDE 221..233
FT /note="Rimorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306369"
FT PEPTIDE 221..225
FT /note="Leu-enkephalin"
FT /id="PRO_0000008205"
FT REGION 174..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 181
FT /note="T -> A (in Ref. 2; AAA41118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 28079 MW; 899F1B24CA3D1E91 CRC64;
MAWSRLMLAA CLLVIPSEVA ADCLSLCSLC AVRTQDGPHP INPLICSLEC QDLVPPSEEW
ETCRGFWSFL TLTASGLHGK DDLENEVALE EGYTALTKLL EPLLKELEKG QLLTSVSEEK
LRGLSSRFGN GRESELLGTD LMNDEAAQAG TLHFNEEDLR KQAKRYGGFL RKYPKRSSEM
TGDEDRGQDG DQVGHEDLYK RYGGFLRRIR PKLKWDNQKR YGGFLRRQFK VVTRSQENPN
TYSEDLDV
