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P20420 (ACHA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit alpha-5
Gene names
Name:Chrna5
Synonyms:Acra5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 seems to be composed of two different types of subunits: alpha and non-alpha (beta).

Subcellular location

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

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-5/CHRNA5 sub-subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 452425Neuronal acetylcholine receptor subunit alpha-5
PRO_0000000358

Regions

Topological domain28 – 239212Extracellular Potential
Transmembrane240 – 26021Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane302 – 32221Helical; Potential
Topological domain323 – 41492Cytoplasmic Potential
Transmembrane415 – 43521Helical; Potential
Topological domain436 – 45217Extracellular Potential

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Disulfide bond155 ↔ 169 By similarity
Disulfide bond219 ↔ 220Associated with receptor activation By similarity

Sequences

Sequence LengthMass (Da)Tools
P20420 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 7CEB24553936B2E7

FASTA45251,874
        10         20         30         40         50         60 
MVQLLAGRWR PTGARRGTRG GLPELSSAAK HEDSLFRDLF EDYERWVRPV EHLSDKIKIK 

        70         80         90        100        110        120 
FGLAISQLVD VDEKNQLMTT NVWLKQEWID VKLRWNPDDY GGIKIIRVPS DSLWIPDIVL 

       130        140        150        160        170        180 
FDNADGRFEG ASTKTVVRYN GTVTWTQPAN YKSSCTIDVT FFPFDLQNCS MKFGSWTYDG 

       190        200        210        220        230        240 
SQVDIILEDQ DVDRTDFFDN GEWEIMSAMG SKGNRTDSCC WYPYITYSFV IKRLPLFYTL 

       250        260        270        280        290        300 
FLIIPCIGLS FLTVVVFYLP SNEGEKISLC TSVLVSLTVF LLVIEEIIPS SSKVIPLIGE 

       310        320        330        340        350        360 
YLVFTMIFVT LSIMVTVFAI NIHHRSSSTH NAMAPWVRKI FLHKLPKLLC MRSHADRYFT 

       370        380        390        400        410        420 
QREEAESGAG PKSRNTLEAA LDCIRYITRH VVKENDVREV VEDWKFIAQV LDRMFLWTFL 

       430        440        450 
LVSIIGTLGL FVPVIYKWAN IIVPVHIGNT IK 

« Hide

References

[1]"Alpha 3, alpha 5, and beta 4: three members of the rat neuronal nicotinic acetylcholine receptor-related gene family form a gene cluster."
Boulter J., O'Shea-Greenfield A., Duvoisin R.M., Connolly J.G., Wada E., Jensen A., Gardner P.D., Ballivet M., Deneris E.S., McKinnon D., Heinemann S.F., Patrick J.
J. Biol. Chem. 265:4472-4482(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05231 mRNA. Translation: AAA74475.1.
IPIIPI00325218.
PIRA35721.
UniGeneRn.40125.

3D structure databases

ProteinModelPortalP20420.
SMRP20420. Positions 235-327.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000062227.

Proteomic databases

PRIDEP20420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2347. rat.

Organism-specific databases

RGD2347. Chrna5.

Phylogenomic databases

eggNOGNOG267611.
HOGENOMHOG000006756.
HOVERGENHBG003756.
InParanoidP20420.
OrthoDBEOG41JZC6.

Gene expression databases

ArrayExpressP20420.
GenevestigatorP20420.
GermOnlineENSRNOG00000013610. Rattus norvegicus.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP20420.
ChEMBLCHEMBL4960.

Entry information

Entry nameACHA5_RAT
AccessionPrimary (citable) accession number: P20420
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families