ACHA4_MUSPF
ID ACHA4_MUSPF Reviewed; 627 AA.
AC Q19AE6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-4;
DE Flags: Precursor;
GN Name=CHRNA4;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16569710; DOI=10.1124/mol.105.020198;
RA Briggs C.A., Gubbins E.J., Marks M.J., Putman C.B., Thimmapaya R.,
RA Meyer M.D., Surowy C.S.;
RT "Untranslated region-dependent exclusive expression of high-sensitivity
RT subforms of alpha4beta2 and alpha3beta2 nicotinic acetylcholine
RT receptors.";
RL Mol. Pharmacol. 70:227-240(2006).
CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC extensive change in conformation that affects all subunits and leads to
CC opening of an ion-conducting channel across the plasma membrane
CC permeable to sodium ions. {ECO:0000250}.
CC -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC alpha and beta. Alpha-4 subunit can be combined to beta-2 or beta-4 to
CC give rise to functional receptors, complexes with beta-2 may be
CC heteropentamers. Interacts with RIC3; which is required for proper
CC folding and assembly. Interacts with LYPD6. The heteropentamer alpha-4-
CC beta-2 interacts with alpha-conotoxins PnIA, GID and MII (By
CC similarity). {ECO:0000250|UniProtKB:P09483,
CC ECO:0000250|UniProtKB:P43681}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-4/CHRNA4 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ533688; ABF83200.1; -; mRNA.
DR RefSeq; NP_001297126.1; NM_001310197.1.
DR AlphaFoldDB; Q19AE6; -.
DR SMR; Q19AE6; -.
DR STRING; 9669.ENSMPUP00000008135; -.
DR GeneID; 101690282; -.
DR CTD; 1137; -.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_1_1_1; -.
DR InParanoid; Q19AE6; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISS:UniProtKB.
DR GO; GO:0035095; P:behavioral response to nicotine; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR Gene3D; 1.20.58.390; -; 2.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00254; NICOTINICR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..627
FT /note="Neuronal acetylcholine receptor subunit alpha-4"
FT /id="PRO_0000310947"
FT TOPO_DOM 32..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 384..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09483"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70174"
FT LIPID 273
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..177
FT /evidence="ECO:0000250"
FT DISULFID 227..228
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 69381 MW; 850B48FF9358B63E CRC64;
MELGGPGAPP PPLLPPLLLL LGAGFLPASS PVETRAHAEE RLLKTLFSGY NKWSRPVANI
SDVVLVHFGL SIAQLIDVDE KNQMMTTNVW VKQEWYDYKL RWDPADYENV TSIRIPSELI
WRPDIVLYNN ADGDFAITHL TKAHLFHDGR VQWTPPAIYK SSCSIDVTFF PFDQQNCTMK
FGSWTYDKAK IDLVSMQSHV DQLGLWESGE WVIVDAAGTY NTRKYECCAE VYPDITYAFV
IRRLPLFYTI NLIVPCLLIS CLTVLVFYLP SDCGEKVTLC ISVLLSLTVF LLLITEIIPS
TSLVIPLIGE YLLFTMVFVT LSIVITVFVL NVHHRSPRTH TMPAWVRRVF LDVVPRLLLM
KRPSVVKDNC RRLIESMHKV ASAPGFWPEP EGEPGVVSGE RSRGPSRSAS FRGPRDEPAE
PQPACASPSD RVPAPQPSEG DPGSPCPLPD SCRPPPSTRA PGLTEARSLS FQHVSSAAER
VEGGVRCRSW SIQGCAPQDE AASVAGGPVT SSPAFPKASA AELLPPDQPS PCRCRCRKEP
SPNAVRKACG TRVPARHLPL SPALARAVEG VQYIADHLKA EDTDFSVKED WKYVAMVIDR
IFLWVFVIVC LLGTAGLFLP PWLAGMI
