ACHA2_PANTR
ID ACHA2_PANTR Reviewed; 529 AA.
AC Q5IS52;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-2;
DE Flags: Precursor;
GN Name=CHRNA2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 {ECO:0000250}.
CC -!- SUBUNIT: Neuronal AChR seems to be composed of two different types of
CC subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined
CC to beta-2 or beta-4 to give rise to functional receptors. The alpha-
CC 2:beta-2 nAChR complex is proposed to be a heteropentamer with two
CC subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and
CC HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3
CC stoichiometry; the subtypes differ in their subunit binding interfaces
CC which are involved in ligand binding (By similarity).
CC {ECO:0000250|UniProtKB:Q15822}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Multi-pass 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-2/CHRNA2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AY665276; AAV74314.1; -; mRNA.
DR RefSeq; NP_001029107.1; NM_001033935.1.
DR RefSeq; XP_009453308.1; XM_009455033.2.
DR AlphaFoldDB; Q5IS52; -.
DR SMR; Q5IS52; -.
DR STRING; 9598.ENSPTRP00000034420; -.
DR PaxDb; Q5IS52; -.
DR Ensembl; ENSPTRT00000037245; ENSPTRP00000034420; ENSPTRG00000020105.
DR GeneID; 472725; -.
DR KEGG; ptr:472725; -.
DR CTD; 1135; -.
DR VGNC; VGNC:7589; CHRNA2.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158299; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q5IS52; -.
DR OMA; QHAKNKD; -.
DR OrthoDB; 381858at2759; -.
DR TreeFam; TF315605; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000020105; Expressed in superior frontal gyrus and 4 other tissues.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; IEA:Ensembl.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0035094; P:response to nicotine; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
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; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..529
FT /note="Neuronal acetylcholine receptor subunit alpha-2"
FT /id="PRO_0000000342"
FT TOPO_DOM 27..264
FT /note="Extracellular"
FT TRANSMEM 265..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..502
FT /note="Cytoplasmic"
FT TRANSMEM 503..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 27..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250"
FT DISULFID 247..248
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 59773 MW; DCE98F58DC06EDDC CRC64;
MGPSCPVFLS FTKLSLWWLL LTPAGGEEAK RPPPRAPGDP LSSPSPTALP QGGSHTETED
RLFKHLFRGY NRWARPVPNT SDVVIVRFGL SIAQLIDVDE KNQMMTTNVW LKQEWSDYKL
RWNPADFGNI TSLRVPSEMI WIPDIVLYNN ADGEFAVTHM TKAHLFSTGT VHWVPPAIYK
SSCSIDVTFF PFDQQNCKMK FGSWTYDKAK IDLEQMEQTV DLKDYWESGE WAIVNATGTY
NSKKYDCCAE IYPDVTYAFI IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SNCGEKITLC
ISVLLSLTVF LLLITEIIPS TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPSTH
TMPHWVRGTL LGCVPRWLLM NRPPPPLELC HPLHLKLSPS YHWLESNVDA EEREVVVEEE
DRWACAGHVA PSVGTLCSHG HLHSGASGPK AEALLQEGEL LLSPHMQKAL EGVHYIADHL
RSEDADSSVK EDWKYVAMVI DRIFLWLFII VCFLGTIGLF LPPFLAGMI
