P17787 (ACHB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuronal acetylcholine receptor subunit beta-2

Gene names

Name:

CHRNB2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subunit structure	Neuronal AChR is composed of two different types of subunits: alpha and beta. Beta-2 subunit can be combined to alpha-2, alpha-3 or alpha-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Ref.7
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Involvement in disease	Defects in CHRNB2 are the cause of nocturnal frontal lobe epilepsy type 3 (ENFL3) [MIM:605375]. ENFL3 is an autosomal dominant epilepsy characterized by nocturnal seizures with hyperkinetic automatisms and poorly organized stereotyped movements. Ref.8 Ref.9
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-2/CHRNB2 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Polymorphism
Disease	Disease mutation Epilepsy
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ionic channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	B cell activation Inferred from sequence or structural similarity. Source: UniProtKB behavioral response to nicotine Inferred from mutant phenotype. Source: UniProtKB calcium ion transport Inferred from sequence or structural similarity. Source: UniProtKB central nervous system projection neuron axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB lateral geniculate nucleus development Inferred from sequence or structural similarity. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB membrane depolarization Inferred from sequence or structural similarity. Source: UniProtKB memory Inferred from mutant phenotype. Source: UniProtKB negative regulation of action potential Inferred from sequence or structural similarity. Source: UniProtKB optic nerve morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of B cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of dopamine secretion Inferred from sequence or structural similarity. Source: UniProtKB regulation of circadian sleep/wake cycle, REM sleep Inferred from sequence or structural similarity. Source: UniProtKB regulation of dendrite morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of dopamine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB response to cocaine Inferred from sequence or structural similarity. Source: UniProtKB response to ethanol Inferred from sequence or structural similarity. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB sensory perception of pain Inferred from sequence or structural similarity. Source: UniProtKB sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB smooth muscle contraction Inferred from sequence or structural similarity. Source: UniProtKB social behavior Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission involved in micturition Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission, cholinergic Inferred from sequence or structural similarity. Source: UniProtKB vestibulocochlear nerve development Inferred from sequence or structural similarity. Source: UniProtKB visual learning Inferred from mutant phenotype. Source: UniProtKB visual perception Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	acetylcholine-gated channel complex Inferred from direct assay Ref.2. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW external side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylcholine binding Inferred from mutant phenotype. Source: UniProtKB acetylcholine receptor activity Inferred from direct assay Ref.2. Source: UniProtKB acetylcholine-activated cation-selective channel activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

By similarity

Chain

26 – 502

477

Neuronal acetylcholine receptor subunit beta-2

PRO_0000000379

Regions

Topological domain

26 – 233

208

Extracellular Potential

Transmembrane

234 – 258

25

Helical; Potential

Transmembrane

266 – 284

19

Helical; Potential

Transmembrane

300 – 321

22

Helical; Potential

Topological domain

322 – 458

137

Cytoplasmic Potential

Transmembrane

459 – 478

20

Helical; Potential

Amino acid modifications

Glycosylation

51

1

N-linked (GlcNAc...) Potential

Glycosylation

168

1

N-linked (GlcNAc...) Potential

Glycosylation

485

1

N-linked (GlcNAc...) Potential

Disulfide bond

155 ↔ 169

By similarity

Natural variations

Natural variant

287

1

V → L in ENFL3. Ref.8

VAR_012714

Natural variant

287

1

V → M in ENFL3; approximately 10-fold increase in acetylcholine sensitivity. Ref.9

VAR_012715

Natural variant

397

1

Q → H. Ref.10
Corresponds to variant rs55685423 [ dbSNP | Ensembl ].

VAR_021564

Experimental info

Sequence conflict

26

1

T → A in CAA05108. Ref.4

Sequence conflict

426

1

E → A in CAA05108. Ref.4

Sequence conflict

446

1

S → SVR in CAA05108. Ref.4

Secondary structure

1

.

.

.

.

.

502

Helix Strand Turn

Details...

Beta strand

233 – 236

4

Helix

242 – 257

16

Sequences

	Sequence		Length	Mass (Da)
	P17787 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 7EEDEF6ADFDC9F23	FASTA	502	57,019
	10 20 30 40 50 60 MARRCGPVAL LLGFGLLRLC SGVWGTDTEE RLVEHLLDPS RYNKLIRPAT NGSELVTVQL 70 80 90 100 110 120 MVSLAQLISV HEREQIMTTN VWLTQEWEDY RLTWKPEEFD NMKKVRLPSK HIWLPDVVLY 130 140 150 160 170 180 NNADGMYEVS FYSNAVVSYD GSIFWLPPAI YKSACKIEVK HFPFDQQNCT MKFRSWTYDR 190 200 210 220 230 240 TEIDLVLKSE VASLDDFTPS GEWDIVALPG RRNENPDDST YVDITYDFII RRKPLFYTIN 250 260 270 280 290 300 LIIPCVLITS LAILVFYLPS DCGEKMTLCI SVLLALTVFL LLISKIVPPT SLDVPLVGKY 310 320 330 340 350 360 LMFTMVLVTF SIVTSVCVLN VHHRSPTTHT MAPWVKVVFL EKLPALLFMQ QPRHHCARQR 370 380 390 400 410 420 LRLRRRQRER EGAGALFFRE APGADSCTCF VNRASVQGLA GAFGAEPAPV AGPGRSGEPC 430 440 450 460 470 480 GCGLREAVDG VRFIADHMRS EDDDQSVSED WKYVAMVIDR LFLWIFVFVC VFGTIGMFLQ 490 500 PLFQNYTTTT FLHSDHSAPS SK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the human nicotinic acetylcholine receptor beta 2 subunit gene." Anand R., Lindstrom J. Nucleic Acids Res. 18:4272-4272(1990) [PubMed: 2377478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[2]	"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." Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E., Johnson E.C., Velicelebi G., Harpold M.M. J. Mol. Neurosci. 7:217-228(1996) [PubMed: 8906617] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"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." Groot Kormelink P.J., Luyten W.H.M.L. FEBS Lett. 400:309-314(1997) [PubMed: 9009220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Frontal cortex.
[4]	"The structures of the human neuronal nicotinic acetylcholine receptor beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3)." Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K. Hum. Genet. 103:645-653(1998) [PubMed: 9921897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Genomic organization and mapping of the human and mouse neuronal beta2-nicotinic acetylcholine receptor genes." Lueders K.K., Elliott R.W., Marenholz I., Mischke D., DuPree M., Hamer D. Mamm. Genome 10:900-905(1999) [PubMed: 10441742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells." Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S. Mol. Pharmacol. 68:1431-1438(2005) [PubMed: 16120769] [Abstract] Cited for: INTERACTION WITH RIC3.
[8]	"The nicotinic receptor beta-2 subunit is mutant in nocturnal frontal lobe epilepsy." De Fusco M., Becchetti A., Patrignani A., Annesi G., Gambardella A., Quattrone A., Ballabio A., Wanke E., Casari G. Nat. Genet. 26:275-276(2000) [PubMed: 11062464] [Abstract] Cited for: VARIANT ENFL3 LEU-287.
[9]	"CHRNB2 is the second acetylcholine receptor subunit associated with autosomal dominant nocturnal frontal lobe epilepsy." Phillips H.A., Favre I., Kirkpatrick M., Zuberi S.M., Goudie D., Heron S.E., Scheffer I.E., Sutherland G.R., Berkovic S.F., Bertrand D., Mulley J.C. Am. J. Hum. Genet. 68:225-231(2001) [PubMed: 11104662] [Abstract] Cited for: VARIANT ENFL3 MET-287.
[10]	"Genetic and functional analysis of single nucleotide polymorphisms in the beta2-neuronal nicotinic acetylcholine receptor gene (CHRNB2)." Lueders K.K., Hu S., McHugh L., Myakishev M.V., Sirota L.A., Hamer D.H. Nicotine Tob. Res. 4:115-125(2002) [PubMed: 11906688] [Abstract] Cited for: VARIANT HIS-397.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53179 mRNA. Translation: CAA37320.1.
U62437 mRNA. Translation: AAB40115.1.
Y08415 mRNA. Translation: CAA69692.1.
AJ001935 , AJ001936, AJ001937, AJ001938, AJ001939 Genomic DNA. Translation: CAA05108.1.
AF077186 Genomic DNA. Translation: AAD45422.1.
BC075040 mRNA. Translation: AAH75040.1.
BC075041 mRNA. Translation: AAH75041.1.

IPI

IPI00016869.

PIR

S10505.

RefSeq

NP_000739.1. NM_000748.2.

UniGene

Hs.2306.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GVT	model	-	B/D/E	30-233	[»]
2K58	NMR	-	B	231-265	[»]
2K59	NMR	-	B	264-291	[»]
2KSR	NMR	-	A	231-486	[»]

ProteinModelPortal

P17787.

SMR

P17787. Positions 26-486.

ModBase

Search...

Protein-protein interaction databases

STRING

P17787.

Polymorphism databases

DMDM

113105.

Proteomic databases

PRIDE

P17787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368476; ENSP00000357461; ENSG00000160716.

GeneID

1141.

KEGG

hsa:1141.

UCSC

uc001ffg.1. human.

Organism-specific databases

CTD

1141.

GeneCards

GC01P154540.

H-InvDB

HIX0028798.

HGNC

HGNC:1962. CHRNB2.

MIM

118507. gene.
605375. phenotype.

neXtProt

NX_P17787.

Orphanet

98784. Nocturnal frontal lobe epilepsy.

PharmGKB

PA115.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18383.

HOGENOM

HBG387619.

HOVERGEN

HBG003756.

InParanoid

P17787.

OMA

CSCGLRE.

OrthoDB

EOG4HQDJ4.

PhylomeDB

P17787.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

P17787.

Bgee

P17787.

CleanEx

HS_CHRNB2.

Genevestigator

P17787.

GermOnline

ENSG00000160716. Homo sapiens.

Family and domain databases

InterPro

IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]

Gene3D

G3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.

KO

K04813.

PANTHER

PTHR18945. Neur_channel. 1 hit.

Pfam

PF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]

PRINTS

PR00254. NICOTINICR.
PR00252. NRIONCHANNEL.

SUPFAM

SSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.

TIGRFAMs

TIGR00860. LIC. 1 hit.

PROSITE

PS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00184. Nicotine.

NextBio

4748.

SOURCE

Search...

Entry information

Entry name

ACHB2_HUMAN

Accession

Primary (citable) accession number: P17787
Secondary accession number(s): Q9UEH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	January 25, 2012
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.