PDYN_BOVIN
ID PDYN_BOVIN Reviewed; 258 AA.
AC Q95104;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9074507; DOI=10.1016/s0378-1119(96)00721-4;
RA Jiang H., Weesner G.D., Malven P.V.;
RT "cDNA sequence and expression of bovine prodynorphin.";
RL Gene 186:279-283(1997).
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; U58500; AAC48706.1; -; mRNA.
DR PIR; JC6318; JC6318.
DR RefSeq; NP_776564.1; NM_174139.2.
DR AlphaFoldDB; Q95104; -.
DR STRING; 9913.ENSBTAP00000055430; -.
DR PaxDb; Q95104; -.
DR GeneID; 281385; -.
DR KEGG; bta:281385; -.
DR CTD; 5173; -.
DR eggNOG; ENOG502RXT4; Eukaryota.
DR InParanoid; Q95104; -.
DR OrthoDB; 1410356at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Endorphin;
KW Neuropeptide; Neurotransmitter; Opioid peptide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..172
FT /id="PRO_0000008162"
FT PEPTIDE 175..184
FT /note="Alpha-neoendorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306335"
FT PEPTIDE 175..183
FT /note="Beta-neoendorphin"
FT /id="PRO_0000008163"
FT PEPTIDE 175..179
FT /note="Leu-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306336"
FT PROPEP 186..208
FT /id="PRO_0000008164"
FT PEPTIDE 211..242
FT /note="Big dynorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306337"
FT PEPTIDE 211..227
FT /note="Dynorphin A(1-17)"
FT /id="PRO_0000008165"
FT PEPTIDE 211..223
FT /note="Dynorphin A(1-13)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306338"
FT PEPTIDE 211..218
FT /note="Dynorphin A(1-8)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306339"
FT PEPTIDE 211..215
FT /note="Leu-enkephalin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000306340"
FT PEPTIDE 230..258
FT /note="Leumorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008166"
FT PEPTIDE 230..242
FT /note="Rimorphin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000008167"
FT PEPTIDE 230..234
FT /note="Leu-enkephalin"
FT /id="PRO_0000008168"
SQ SEQUENCE 258 AA; 28790 MW; AA51C34022F18046 CRC64;
MVWQGLVLAA CLLALPSVTA DCLAQCSLCA VKTQDGPQPI NPLVCSLECQ AALQPAQEWE
RCQGLLSFLT PFTVGLNGKE DLKSKTVLEE SSSEPAKHIR PYLKELEKNR FLLSTPAEKN
ALSSSLVEKL RGLSGRLGED AESELMGDAQ LNDGALEAEA RDSNEEEPKE QVKRYGGFLR
KYPKRSSEVT GKEAGEGEGG EVGHEDLYKR YGGFLRRIRP KLKWDNQKRY GGFLRRQFKV
VTRSQEDPSA YYEELFDV
