• channel activity • ion channel activity • extracellular ligand-gated ion channel activity • ligand-gated ion channel activity • acetylcholine-gated cation-selective channel activity • transmembrane signaling receptor activity • acetylcholine binding • acetylcholine receptor activity • drug binding
Cellular component
• integral component of membrane • postsynaptic membrane • membrane • plasma membrane • synapse • cell junction • acetylcholine-gated channel complex • dopaminergic synapse • integral component of plasma membrane • neuron projection
Biological process
• response to nicotine • synaptic transmission, cholinergic • ion transport • neuromuscular synaptic transmission • signal transduction • postsynaptic potential • excitatory postsynaptic potential • cation transmembrane transport • ion transmembrane transport • regulation of synaptic vesicle exocytosis • chemical synaptic transmission • regulation of membrane potential • nervous system process • protein heterooligomerization
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
1142
108043
Ensembl
ENSG00000147432
ENSMUSG00000031492
UniProt
Q05901
Q8BMN3
RefSeq (mRNA)
NM_000749 NM_001347717
NM_027454 NM_173212
RefSeq (protein)
NP_000740 NP_001334646
NP_081730 NP_775304
Location (UCSC)
Chr 8: 42.7 – 42.74 Mb
Chr 8: 27.37 – 27.4 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Neuronal acetylcholine receptor subunit beta-3 is a protein that in humans is encoded by the CHRNB3 gene.[5][6]
Contents
1See also
2References
3Further reading
4External links
See also
Nicotinic acetylcholine receptor
References
^ abcGRCh38: Ensembl release 89: ENSG00000147432 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000031492 - Ensembl, May 2017
Hogg RC, Raggenbass M, Bertrand D (2003). Nicotinic acetylcholine receptors: from structure to brain function. Rev. Physiol. Biochem. Pharmacol. Reviews of Physiology, Biochemistry and Pharmacology. 147. pp. 1–46. doi:10.1007/s10254-003-0005-1. ISBN 978-3-540-01365-5. PMID 12783266.
Willoughby JJ, Ninkina NN, Beech MM, et al. (1993). "Molecular cloning of a human neuronal nicotinic acetylcholine receptor beta 3-like subunit". Neurosci. Lett. 155 (2): 136–9. doi:10.1016/0304-3940(93)90691-D. PMID 7690916.
Koyama K, Sudo K, Nakamura Y (1994). "Mapping of the human nicotinic acetylcholine receptor beta 3 gene (CHRNB3) within chromosome 8p11.2". Genomics. 21 (2): 460–1. doi:10.1006/geno.1994.1300. PMID 8088849.
Elliott KJ, Ellis SB, Berckhan KJ, et al. (1997). "Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits". J. Mol. Neurosci. 7 (3): 217–28. doi:10.1007/BF02736842. PMID 8906617.
Groot Kormelink PJ, Luyten WH (1997). "Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32". FEBS Lett. 400 (3): 309–14. doi:10.1016/S0014-5793(96)01383-X. PMID 9009220.
Navaneetham D, Penn A, Howard J, Conti-Fine BM (1997). "Expression of the alpha 7 subunit of the nicotinic acetylcholine receptor in normal and myasthenic human thymuses". Cell. Mol. Biol. (Noisy-le-grand). 43 (3): 433–42. PMID 9193799.
Groot-Kormelink PJ, Luyten WH, Colquhoun D, Sivilotti LG (1998). "A reporter mutation approach shows incorporation of the "orphan" subunit beta3 into a functional nicotinic receptor". J. Biol. Chem. 273 (25): 15317–20. doi:10.1074/jbc.273.25.15317. PMID 9624109.
Sato KZ, Fujii T, Watanabe Y, et al. (1999). "Diversity of mRNA expression for muscarinic acetylcholine receptor subtypes and neuronal nicotinic acetylcholine receptor subunits in human mononuclear leukocytes and leukemic cell lines". Neurosci. Lett. 266 (1): 17–20. doi:10.1016/S0304-3940(99)00259-1. PMID 10336173.
Boorman JP, Groot-Kormelink PJ, Sivilotti LG (2001). "Stoichiometry of human recombinant neuronal nicotinic receptors containing the β3 subunit expressed in Xenopus oocytes". J. Physiol. 529 Pt 3 (Pt 3): 565–77. doi:10.1111/j.1469-7793.2000.00565.x. PMC 2270211. PMID 11118490.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Boorman JP, Beato M, Groot-Kormelink PJ, et al. (2004). "The effects of beta3 subunit incorporation on the pharmacology and single channel properties of oocyte-expressed human alpha3beta4 neuronal nicotinic receptors". J. Biol. Chem. 278 (45): 44033–40. doi:10.1074/jbc.M211719200. PMID 12912995.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
External links
CHRNB3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
Human CHRNB3 genome location and CHRNB3 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
v
t
e
Ion channel, cell surface receptor: ligand-gated ion channels
Cys-loop receptors
5-HT/serotonin
5-HT3
A
B
C
D
E
GABA
GABAA
α1
α2
α3
α4
α5
α6
β1
β2
β3
γ1
γ2
γ3
δ
ε
π
θ
GABAA-ρ
ρ1
ρ2
ρ3
Glycine
α1
α2
α3
α4
β
Nicotinic acetylcholine
monomers: α1
α2
α3
α4
α5
α6
α7
α9
α10
β1
β2
β3
β4
δ
ε
pentamers: (α3)2(β4)3
(α4)2(β2)3
(α7)5
(α1)2(β4)3 - Ganglion type
(α1)2β1δε - Muscle type
Zinc
Zinc-activated
Ionotropic glutamates
Ligand-gated only
AMPA (1
2
3
4)
Kainate
1
2
3
4
5
Voltage- and ligand-gated
NMDA
1
2A
2B
2C
2D
3A
3B
L1A
L1B
‘Orphan’
GluD
δ1
δ2
ATP-gated channels
Purinergic receptors
P2X
1
2
3
4
5
6
7
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