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   27-MAR-2024, entry version 131.
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 opioid activity, it is 700
CC       times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Leumorphin has a typical opioid 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   PhosphoSitePlus; P06300; -.
DR   PaxDb; 10116-ENSRNOP00000038921; -.
DR   UCSC; RGD:62054; rat.
DR   AGR; RGD:62054; -.
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; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0031045; C:dense core granule; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0098992; C:neuronal dense core vesicle; ISO: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:0035902; P:response to immobilization stress; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   GO; GO:0007600; P:sensory perception; IBA:GO_Central.
DR   InterPro; IPR006024; Opioid_neupept.
DR   InterPro; IPR000750; Proenkphlin_B.
DR   PANTHER; PTHR11438; PROENKEPHALIN; 1.
DR   PANTHER; PTHR11438:SF4; PROENKEPHALIN-B; 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
//