cellular response to transforming growth factor beta stimulus
cellular response to virus
general adaptation syndrome, behavioral process
response to estradiol
response to hypoxia
startle response
locomotory behavior
response to nicotine
human ageing
response to epinephrine
cellular response to vitamin D
behavioral fear response
locomotory exploration behavior
response to calcium ion
response to morphine
response to lipopolysaccharide
osteoblast differentiation
glial cell proliferation
sensory perception of pain
cellular response to oxidative stress
response to radiation
response to ethanol
positive regulation of behavioral fear response
response to toxic substance
cellular response to cAMP
aggressive behavior
signal transduction
sensory perception
neuropeptide signaling pathway
chemical synaptic transmission
post-translational protein modification
regulation of signaling receptor activity
G protein-coupled receptor signaling pathway
response to bacterium
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
5179
18619
Ensembl
ENSG00000181195
ENSMUSG00000045573
UniProt
P01210
P22005
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 Mb
Chr 4: 4.13 – 4.14 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/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]
^ abcGRCh38: Ensembl release 89: ENSG00000181195 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000045573 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ abDonald W. Pfaff (2002). Hormones, brain, and behavior. Elsevier. p. 173. ISBN 978-0-12-532109-9. Retrieved 25 November 2011.
^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.
^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.
^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.
^ abMizuno 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.
^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.
^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.
^Jones BN, Stern AS, Lewis RV, Kimura S, Stein S, Udenfriend S, Shively JE (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.
Proenkephalin (PENK), formerly known as proenkephalin A (since proenkephalin B was renamed prodynorphin), is an endogenous opioid polypeptide hormone which...
Prodynorphin, also known as proenkephalin B, is an opioid polypeptide hormone involved with chemical signal transduction and cell communication. The gene...
and the other containing methionine ("met"). Both are products of the proenkephalin gene. Met-enkephalin is Tyr-Gly-Gly-Phe-Met. Leu-enkephalin is Tyr-Gly-Gly-Phe-Leu...
synthesized from the precursor proopiomelanocortin (POMC), encoded by proenkephalin A, and dynorphins encoded by pre-dynorphin. The word endorphin is derived...
needed] Instead, [Met]enkephalin is produced from its own precursor, proenkephalin A. The production of β-MSH occurs in humans but not in mice or rats...
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