ID PDYN_CAVPO Reviewed; 245 AA. AC Q60478; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 24-JAN-2024, entry version 109. 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 Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae; OC Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Hartley; TISSUE=Adrenal gland, and Brain; RX PubMed=8985124; DOI=10.1089/dna.1996.15.1105; RA Yuferov V.P., Laforge K.S., Spangler R., Maggos C.E., Kreek M.J.; RT "Guinea pig preprodynorphin mRNA: primary structure and regional RT quantitation in the brain."; RL DNA Cell Biol. 15:1105-1112(1996). RN [2] RP IDENTIFICATION OF DYNORPHIN A(1-8); DYNORPHIN A(1-17) AND RP ALPHA-NEOENDORPHIN. RX PubMed=2565558; DOI=10.1016/0143-4179(89)90094-2; RA Steele P.A., Turner C.A., Murphy R.; RT "Measurement and chromatographic characterization of prodynorphin-derived RT peptides in the guinea-pig ileum."; RL Neuropeptides 13:207-213(1989). 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; U38912; AAC18427.1; -; mRNA. DR PIR; A60410; A60410. DR RefSeq; NP_001166468.1; NM_001172997.1. DR AlphaFoldDB; Q60478; -. DR BMRB; Q60478; -. DR STRING; 10141.ENSCPOP00000019436; -. DR Ensembl; ENSCPOT00000022266.2; ENSCPOP00000019436.1; ENSCPOG00000024291.2. DR GeneID; 100135596; -. DR KEGG; cpoc:100135596; -. DR CTD; 5173; -. DR VEuPathDB; HostDB:ENSCPOG00000024291; -. DR eggNOG; ENOG502RXT4; Eukaryota. DR GeneTree; ENSGT00950000183149; -. DR HOGENOM; CLU_070973_1_0_1; -. DR InParanoid; Q60478; -. DR OMA; CSMCAVQ; -. DR OrthoDB; 5318835at2759; -. DR TreeFam; TF332620; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000024291; Expressed in hypothalamus and 4 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl. DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW. DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW. DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW. 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..161 FT /id="PRO_0000008169" FT PEPTIDE 164..173 FT /note="Alpha-neoendorphin" FT /id="PRO_0000306341" FT PEPTIDE 164..172 FT /note="Beta-neoendorphin" FT /id="PRO_0000008170" FT PEPTIDE 164..168 FT /note="Leu-enkephalin" FT /evidence="ECO:0000250" FT /id="PRO_0000306342" FT PROPEP 175..195 FT /id="PRO_0000008171" FT PEPTIDE 198..229 FT /note="Big dynorphin" FT /evidence="ECO:0000250" FT /id="PRO_0000306343" FT PEPTIDE 198..214 FT /note="Dynorphin A(1-17)" FT /id="PRO_0000008172" FT PEPTIDE 198..210 FT /note="Dynorphin A(1-13)" FT /evidence="ECO:0000250" FT /id="PRO_0000306344" FT PEPTIDE 198..205 FT /note="Dynorphin A(1-8)" FT /id="PRO_0000306345" FT PEPTIDE 198..202 FT /note="Leu-enkephalin" FT /evidence="ECO:0000250" FT /id="PRO_0000306346" FT PEPTIDE 217..245 FT /note="Leumorphin" FT /id="PRO_0000008173" FT PEPTIDE 217..229 FT /note="Rimorphin" FT /evidence="ECO:0000250" FT /id="PRO_0000008174" FT PEPTIDE 217..221 FT /note="Leu-enkephalin" FT /id="PRO_0000008175" SQ SEQUENCE 245 AA; 27509 MW; 719B811A3683D19B CRC64; MVWPRLVLAA CLLAMPPAAA ECLSQCSLCA VRTQDGPKPI NPLICSLECQ ETLLPSEEWE RCQGILSFFP SALRLRDQSG LDSRAALEEV YGELAKRARP FLQELEKSRF LPSTPAEDKF RGLLGGLGEG LGSEAMGAPQ LNSGAVEAAA LDFDEDPKEQ VKRYGGFLRK YPKRSSEVAR EGDRDGDNAG HEDLYKRYGG FLRRIRPKLK WDNQKRYGGF LRRQFKVVTR SQEDPNAYSE EFFDV //