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 24-JAN-2024, entry version 103. 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 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U58500; AAC48706.1; -; mRNA. DR PIR; JC6318; JC6318. DR RefSeq; NP_776564.1; NM_174139.2. DR AlphaFoldDB; Q95104; -. DR STRING; 9913.ENSBTAP00000068675; -. DR PaxDb; 9913-ENSBTAP00000055430; -. DR GeneID; 281385; -. DR KEGG; bta:281385; -. DR CTD; 5173; -. DR eggNOG; ENOG502RXT4; Eukaryota. DR InParanoid; Q95104; -. 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; 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 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 //