Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01190
Entry Name
UniProt Accession
Theoretical PI
6.67
Molecular Weight
70192.69
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Neuronal acetylcholine receptor subunit alpha-4
Protein Synonyms/Alias
Gene Name
Chrna4
Gene Synonyms/Alias
Acra4;
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
273
Canonical
VFYLPSECGEKVTLC
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Amici SA, McKay SB, Wells GB, Robson JI, Nasir M, Ponath G, Anand R. A highly conserved cytoplasmic cysteine residue in the α4 nicotinic acetylcholine receptoris palmitoylated and regulates protein expression. J Biol Chem. 2012 Jun29;287(27):23119-27. doi: 10.1074/jbc.M111.328294. Epub 2012 May 16.[PMID:22593584]
Functional Description
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 permeable to sodium ions.
Sequence Annotation
Topological domain: 32 249 Extracellular.
Transmembrane: 250 270 Helical.
Transmembrane: 279 299 Helical.
Transmembrane: 313 333 Helical.
Topological domain: 334 604 Cytoplasmic.
Transmembrane: 605 625 Helical.
Protein Length
630 AA.
Protein Sequence
(Canonical)
MANSGTGAPP PLLLLPLLLL LGTGLLPASS HIETRAHAEE RLLKRLFSGY NKWSRPVANI  60
SDVVLVRFGL SIAQLIDVDE KNQMMTTNVW VKQEWHDYKL RWDPGDYENV TSIRIPSELI  120
WRPDIVLYNN ADGDFAVTHL TKAHLFYDGR VQWTPPAIYK SSCSIDVTFF PFDQQNCTMK  180
FGSWTYDKAK IDLVSMHSRV DQLDFWESGE WVIVDAVGTY NTRKYECCAE IYPDITYAFI  240
IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SECGEKVTLC ISVLLSLTVF LLLITEIIPS  300
PTSLVIPLIG EYLLFTMIFV TLSIVITVFV LNVHHRSPRT HTMPAWVRRV FLDIVPRLLF  360
MKRPSVVKDN CRRLIESMHK MANAPRFWPE PVGEPGILSD ICNQGLSPAP TFCNPTDTAV  420
ETQPTCRSPP LEVPDLKTSE VEKASPCPSP GSCPPPKSSS GAPMLIKARS LSVQHVPSSQ  480
EAAEDGIRCR SRSIQYCVSQ DGAASLADSK PTSSPTSLKA RPSQLPVSDQ ASPCKCTCKE  540
PSPVSPVTVL KAGGTKAPPQ HLPLSPALTR AVEGVQYIAD HLKAEDTDFS VKEDWKYVAM  600
VIDRIFLWMF IIVCLLGTVG LFLPPWLAAC                                   630
FASTA
(Canonical)
>LipidDB-10116-01190|P09483
MANSGTGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANI
SDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELI
WRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMK
FGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFI
IRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPS
PTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLF
MKRPSVVKDNCRRLIESMHKMANAPRFWPEPVGEPGILSDICNQGLSPAPTFCNPTDTAV
ETQPTCRSPPLEVPDLKTSEVEKASPCPSPGSCPPPKSSSGAPMLIKARSLSVQHVPSSQ
EAAEDGIRCRSRSIQYCVSQDGAASLADSKPTSSPTSLKARPSQLPVSDQASPCKCTCKE
PSPVSPVTVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAM
VIDRIFLWMFIIVCLLGTVGLFLPPWLAAC
Gene Ontology
GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0030425; C:dendrite; IDA:RGD
GO:0016020; C:membrane; IDA:RGD
GO:0043025; C:neuronal cell body; IDA:RGD
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0042166; F:acetylcholine binding; IDA:RGD
GO:0004889; F:acetylcholine-activated cation-selective channel activity; IDA:RGD
GO:0008144; F:drug binding; IDA:RGD
GO:0046982; F:protein heterodimerization activity; IDA:RGD
GO:0098655; P:cation transmembrane transport; IDA:GOC
GO:0006812; P:cation transport; IDA:GOC
GO:0033603; P:positive regulation of dopamine secretion; IDA:RGD
GO:0051291; P:protein heterooligomerization; IDA:RGD
GO:0007271; P:synaptic transmission, cholinergic; IMP:RGD
Interpro
InterPro; IPR027361; Acetylcholine_rcpt_TM
InterPro; IPR006202; Neur_chan_lig-bd
InterPro; IPR006201; Neur_channel
InterPro; IPR006029; Neurotrans-gated_channel_TM
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt
Pfam
Pfam; PF02931; Neur_chan_LBD;
Pfam; PF02932; Neur_chan_memb;
SMART
PROSITE
PROSITE; PS00236; NEUROTR_ION_CHANNEL;
PRINTS
PRINTS; PR00254; NICOTINICR;
PRINTS; PR00252; NRIONCHANNEL;