Proenkephalin

PENK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPENK, proenkephalin, PE, PENK-A
External IDsOMIM: 131330; MGI: 104629; HomoloGene: 4528; GeneCards: PENK; OMA:PENK - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006211
NM_001135690

NM_001002927
NM_001348209

RefSeq (protein)

NP_001129162

NP_001002927
NP_001335138

Location (UCSC)Chr 8: 56.44 – 56.45 MbChr 4: 4.13 – 4.14 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Proenkephalin (PENK), formerly known as proenkephalin A (since proenkephalin B was renamed prodynorphin), is an endogenous opioid polypeptide hormone which, via proteolyic cleavage, produces the enkephalin peptides met-enkephalin, and to a lesser extent, leu-enkephalin.[5] Upon cleavage, each proenkephalin peptide results in the generation of four copies of Met-enkephalin, two extended copies of met-enkephalin, and one copy of leu-enkephalin.[5] Contrarily, Leu-enkephalin] is predominantly synthesized from prodynorphin, which produces three copies of it per cleavage, and no copies of Met-enkephalin. Other endogenous opioid peptides produced by proenkephalin include adrenorphin,[6] amidorphin,[7] BAM-18,[8] BAM-20P,[9] BAM-22P,[9] peptide B,[10] peptide E,[11] and peptide F.[12]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000181195Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000045573Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Donald W. Pfaff (2002). Hormones, brain, and behavior. Elsevier. p. 173. ISBN 978-0-12-532109-9. Retrieved 25 November 2011.
  6. ^ Matsuo H, Miyata A, Mizuno K (1983). "Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour". Nature. 305 (5936): 721–723. Bibcode:1983Natur.305..721M. doi:10.1038/305721a0. PMID 6633641. S2CID 4320171.
  7. ^ Seizinger BR, Liebisch DC, Gramsch C, Herz A, Weber E, Evans CJ, et al. (1985). "Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla". Nature. 313 (5997): 57–59. Bibcode:1985Natur.313...57S. doi:10.1038/313057a0. PMID 3965972. S2CID 4363051.
  8. ^ Hurlbut DE, Evans CJ, Barchas JD, Leslie FM (June 1987). "Pharmacological properties of a proenkephalin A-derived opioid peptide: BAM 18". European Journal of Pharmacology. 138 (3): 359–366. doi:10.1016/0014-2999(87)90474-2. PMID 3040439.
  9. ^ a b Mizuno K, Minamino N, Kangawa K, Matsuo H (December 1980). "A new family of endogenous "big" Met-enkephalins from bovine adrenal medulla: purification and structure of docosa- (BAM-22P) and eicosapeptide (BAM-20P) with very potent opiate activity". Biochemical and Biophysical Research Communications. 97 (4): 1283–1290. doi:10.1016/S0006-291X(80)80005-2. PMID 7213356.
  10. ^ Micanovic R, Kruggel W, Ray P, Lewis RV (1984). "Purification and sequence of a non-opioid peptide derived from ovine proenkephalin: implications for possible species specific processing". Peptides. 5 (5): 853–856. doi:10.1016/0196-9781(84)90105-0. PMID 6504720. S2CID 3869685.
  11. ^ Boarder MR, Evans C, Adams M, Erdelyi E, Barchas JD (December 1987). "Peptide E and its products, BAM 18 and Leu-enkephalin, in bovine adrenal medulla and cultured chromaffin cells: release in response to stimulation". Journal of Neurochemistry. 49 (6): 1824–1832. doi:10.1111/j.1471-4159.1987.tb02443.x. PMID 3681299. S2CID 19919675.
  12. ^ Jones BN, Stern AS, Lewis RV, Kimura S, Stein S, Udenfriend S, et al. (October 1980). "Structure of two adrenal polypeptides containing multiple enkephalin sequences". Archives of Biochemistry and Biophysics. 204 (1): 392–395. doi:10.1016/0003-9861(80)90048-X. PMID 7425644.