ID PENKB_XENLA Reviewed; 216 AA. AC P07194; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=Proenkephalin-A-B; DE Contains: DE RecName: Full=Synenkephalin; DE Contains: DE RecName: Full=Met-enkephalin; DE AltName: Full=Opioid growth factor; DE Short=OGF; DE Contains: DE RecName: Full=Met-enkephalin-Arg-Gly-Tyr; DE Contains: DE RecName: Full=Met-enkephalin-Arg-Phe; DE Flags: Precursor; Fragment; GN Name=penk-b; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6547769; DOI=10.1038/310251a0; RA Martens G.J.M., Herbert E.; RT "Polymorphism and absence of Leu-enkephalin sequences in proenkephalin RT genes in Xenopus laevis."; RL Nature 310:251-254(1984). CC -!- FUNCTION: Enkephalin neuropeptides compete with and mimic the effects CC of opiate drugs. They play a role in a number of physiologic functions, CC including pain perception and responses to stress. CC {ECO:0000250|UniProtKB:P01210}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01210}. CC -!- PTM: The N-terminal domain contains 6 conserved cysteines thought to be CC involved in disulfide bonding and/or processing. CC {ECO:0000250|UniProtKB:P01210}. 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; X00853; CAA25406.1; -; Genomic_DNA. DR AlphaFoldDB; P07194; -. DR AGR; Xenbase:XB-GENE-942765; -. DR Xenbase; XB-GENE-942765; penk.L. DR Proteomes; UP000186698; Genome assembly. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW. DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR006024; Opioid_neupept. DR InterPro; IPR000703; Proenkphlin_A. DR PANTHER; PTHR11438; PROENKEPHALIN; 1. DR PANTHER; PTHR11438:SF3; PROENKEPHALIN-A; 1. DR Pfam; PF01160; Opiods_neuropep; 1. DR PRINTS; PR01028; OPIOIDPRCRSR. DR PRINTS; PR01029; PENKAPRCRSR. PE 3: Inferred from homology; KW Cleavage on pair of basic residues; Disulfide bond; Endorphin; KW Neuropeptide; Opioid peptide; Reference proteome; Secreted. FT PEPTIDE <1..47 FT /note="Synenkephalin" FT /id="PRO_0000008307" FT PEPTIDE 50..54 FT /note="Met-enkephalin" FT /id="PRO_0000008308" FT PEPTIDE 57..61 FT /note="Met-enkephalin" FT /id="PRO_0000008309" FT PROPEP 64..85 FT /id="PRO_0000008310" FT PEPTIDE 86..90 FT /note="Met-enkephalin" FT /id="PRO_0000008311" FT PROPEP 93..131 FT /id="PRO_0000008312" FT PEPTIDE 134..141 FT /note="Met-enkephalin-Arg-Gly-Tyr" FT /id="PRO_0000008313" FT PROPEP 144..155 FT /id="PRO_0000008314" FT PEPTIDE 158..162 FT /note="Met-enkephalin" FT /id="PRO_0000008315" FT PROPEP 165..175 FT /id="PRO_0000008316" FT PEPTIDE 178..182 FT /note="Met-enkephalin" FT /id="PRO_0000008317" FT PROPEP 183..207 FT /id="PRO_0000008318" FT PEPTIDE 210..216 FT /note="Met-enkephalin-Arg-Phe" FT /id="PRO_0000008319" FT REGION 114..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 SQ SEQUENCE 216 AA; 24979 MW; BB48865419AC4131 CRC64; ACTLECEGKL PSAKAWGTCK ELLQLTKLDG VQDGEKYQDN NDSHYIAKKY GGFMKRYGGF MKKMDELYHA EPEEDDAGGE ILAKNYGGFM KKEYDSNRDA SDLLRELLAT SGDPESAIYH DNNSETPGEM NKRYGGFMRG YRRSTDLEDE TRGIQKRYGG FMRRVGRPEW WQDYQKRYGG FMTRFTDSFL PSDEDGESYS KENPDMEKRY GGFMRF //