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Reviewed, UniProtKB/Swiss-Prot P30926 (ACHB4_HUMAN)

Last modified February 9, 2010. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Neuronal acetylcholine receptor subunit beta-4
Gene names
Name: CHRNB4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-4 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.9

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the ligand-gated ionic channel (TC 1.A.9) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 498477Neuronal acetylcholine receptor subunit beta-4
PRO_0000000389

Regions

Topological domain22 – 236215Extracellular Potential
Transmembrane237 – 25721 Potential
Topological domain258 – 2658Cytoplasmic Potential
Transmembrane266 – 28621 Potential
Topological domain287 – 29812Extracellular Potential
Transmembrane299 – 31921 Potential
Topological domain320 – 460141Cytoplasmic Potential
Transmembrane461 – 48121 Potential
Topological domain482 – 49817Extracellular Potential

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Disulfide bond153 ↔ 167 By similarity

Natural variations

Natural variant911T → I: dbSNP rs12914008.
VAR_048174
Natural variant1361R → W
VAR_013241
Natural variant1401S → G: dbSNP rs56218866. Ref.5
VAR_013242
Natural variant4671M → V
VAR_013243

Experimental info

Sequence conflict72 – 732EQ → DE in CAA48336. Ref.8
Sequence conflict1211Missing in CAC34819. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P30926-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 0D48AB203F3FD03E

FASTA49856,380
        10         20         30         40         50         60 
MRRAPSLVLF FLVALCGRGN CRVANAEEKL MDDLLNKTRY NNLIRPATSS SQLISIKLQL 

        70         80         90        100        110        120 
SLAQLISVNE REQIMTTNVW LKQEWTDYRL TWNSSRYEGV NILRIPAKRI WLPDIVLYNN 

       130        140        150        160        170        180 
ADGTYEVSVY TNLIVRSNGS VLWLPPAIYK SACKIEVKYF PFDQQNCTLK FRSWTYDHTE 

       190        200        210        220        230        240 
IDMVLMTPTA SMDDFTPSGE WDIVALPGRR TVNPQDPSYV DVTYDFIIKR KPLFYTINLI 

       250        260        270        280        290        300 
IPCVLTTLLA ILVFYLPSDC GEKMTLCISV LLALTFFLLL ISKIVPPTSL DVPLIGKYLM 

       310        320        330        340        350        360 
FTMVLVTFSI VTSVCVLNVH HRSPSTHTMA PWVKRCFLHK LPTFLFMKRP GPDSSPARAF 

       370        380        390        400        410        420 
PPSKSCVTKP EATATSTSPS NFYGNSMYFV NPASAASKSP AGSTPVAIPR DFWLRSSGRF 

       430        440        450        460        470        480 
RQDVQEALEG VSFIAQHMKN DDEDQSVVED WKYVAMVVDR LFLWVFMFVC VLGTVGLFLP 

       490 
PLFQTHAASE GPYAAQRD 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"'Orphan' alpha6 nicotinic AChR subunit can form a functional heteromeric acetylcholine receptor."
Gerzanich V., Kuryatov A., Anand R., Lindstrom J.
Mol. Pharmacol. 51:320-327(1997) [PubMed: 9203638] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[4]"Characterization of the genomic structure of human nicotinic acetylcholine receptor CHRNA5/A3/B4 gene cluster: identification of two novel introns in the 3' untranslated region of CHRNA3 and of a tail-to-tail overlap between CHRNA3 and CHRNA5."
Duga S., Solda G., Asselta R., Bonati M.T., Dalpra L., Malcovati M., Tenchini M.L.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Characterization of the human beta4 nAChR gene and polymorphisms in CHRNA3 and CHRNB4."
Lev-Lehman E., Bercovich D., Xu W., Stockton D.W., Beaudet A.L.
J. Hum. Genet. 46:362-366(2001) [PubMed: 11450844] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-136; GLY-140 AND VAL-467.
[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].
[7]"Transcription factors NF-Y and Sp1 are important determinants of the promoter activity of the bovine and human neuronal nicotinic receptor beta 4 subunit genes."
Valor L.M., Campos-Caro A., Carrasco-Serrano C., Ortiz J.A., Ballesta J.J., Criado M.
J. Biol. Chem. 277:8866-8876(2002) [PubMed: 11742001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
[8]"Neuronal-type nicotinic receptors in human neuroblastoma and small-cell lung carcinoma cell lines."
Tarroni P., Rubboli F., Chini B., Zwart R., Oortgiesen M., Sher E., Clementi F.
FEBS Lett. 312:66-70(1992) [PubMed: 1330682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-498.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62439 mRNA. Translation: AAB40117.1.
U48861 mRNA. Translation: AAA92123.1.
Y08416 mRNA. Translation: CAA69693.1.
AJ306454 expand/collapse EMBL AC list , AJ306455, AJ306456, AJ306457, AJ306458, AJ306459 Genomic DNA. Translation: CAC34819.1.
AF306329 expand/collapse EMBL AC list , AF306325, AF306326, AF306327, AF306328 Genomic DNA. Translation: AAL02062.1.
BC096080 mRNA. Translation: AAH96080.1.
BC096082 mRNA. Translation: AAH96082.1.
AF453877 Genomic DNA. Translation: AAL57840.1.
X68275 mRNA. Translation: CAA48336.1.
IPIIPI00028080.
PIRG02421.
RefSeqNP_000741.1.
UniGeneHs.624178

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASGmodel-B/D/E262-284[»]
SMRP30926. Positions 25-484.
ModBaseSearch...

Protein-protein interaction databases

STRINGP30926.

Proteomic databases

PRIDEP30926.

Genome annotation databases

EnsemblENST00000261751; ENSP00000261751; ENSG00000117971; Homo sapiens. [Genome view]
GeneID1143.
KEGGhsa:1143.
UCSCuc002bed.1. human.

Organism-specific databases

CTD1143.
GeneCardsGC15M076703.
H-InvDBHIX0038160.
HGNCHGNC:1964. CHRNB4.
MIM118509. gene.
PharmGKBPA26496.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10228.
HOGENOMHBG387619.
HOVERGENP30926.
InParanoidP30926.
OMAMTPTASM.
PhylomeDBP30926.

Gene expression databases

ArrayExpressP30926.
BgeeP30926.
CleanExHS_CHRNB4.
GenevestigatorP30926.
GermOnlineENSG00000117971. Homo sapiens.

Family and domain databases

InterProIPR006202. Neur_chan_lig_bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt_N.
[Graphical view]
Gene3DG3DSA:2.70.170.10. Neur_chan_lig_bd. 1 hit.
PANTHERPTHR18945. Neur_channel. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio4756.
SOURCESearch...

Entry information

Entry nameACHB4_HUMAN
AccessionPrimary (citable) accession number: P30926
Secondary accession number(s): Q16607 expand/collapse secondary AC list , Q4VBA5, Q8WXC8, Q9BQR4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

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Human chromosome 15: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents