ACHA3_BOVIN
ID ACHA3_BOVIN Reviewed; 495 AA.
AC Q07263;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=CHRNA3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1620271; DOI=10.1007/bf00966671;
RA Criado M., Alamo L., Navarro A.;
RT "Primary structure of an agonist binding subunit of the nicotinic
RT acetylcholine receptor from bovine adrenal chromaffin cells.";
RL Neurochem. Res. 17:281-287(1992).
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 -!- SUBUNIT: Neuronal AChR is composed of two different types of subunits:
CC alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to
CC give rise to functional receptors. Interacts with RIC3; which is
CC required for proper folding and assembly. Interacts with LYPD6. The
CC heteropentamer alpha-3-beta-2 interacts with alpha-conotoxins ImI,
CC ImII, PnIA, GID and MII. The heteropentamer composed of alpha-3 and
CC beta-4 subunits interacts with the alpha-conotoxin ImI.
CC {ECO:0000250|UniProtKB:P04757, ECO:0000250|UniProtKB:P32297}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X57032; CAA40348.1; -; mRNA.
DR PIR; S60589; S60589.
DR RefSeq; NP_777144.1; NM_174719.2.
DR AlphaFoldDB; Q07263; -.
DR SMR; Q07263; -.
DR STRING; 9913.ENSBTAP00000004070; -.
DR ChEMBL; CHEMBL5317; -.
DR PaxDb; Q07263; -.
DR PRIDE; Q07263; -.
DR GeneID; 282702; -.
DR KEGG; bta:282702; -.
DR CTD; 1136; -.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; Q07263; -.
DR OrthoDB; 381858at2759; -.
DR PRO; PR:Q07263; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISS:UniProtKB.
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:0043005; C:neuron projection; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; ISS:UniProtKB.
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:0035095; P:behavioral response to nicotine; ISS:UniProtKB.
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:0007399; P:nervous system development; ISS:UniProtKB.
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:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0060084; P:synaptic transmission involved in micturition; 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; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..495
FT /note="Neuronal acetylcholine receptor subunit alpha-3"
FT /id="PRO_0000000345"
FT TOPO_DOM 22..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 468..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04757"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 149..163
FT /evidence="ECO:0000250"
FT DISULFID 213..214
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 495 AA; 56914 MW; 322825629821EA07 CRC64;
MARRSRLRRL LLLLLLPVAS TSDAEHRLFE RLFEDYNEII RPVANVSDPV IIQFEVSMSQ
LVKVDEVNQI METNLWLKQI WNDYKLKWNP SDYDGAEFMR VPAEKIWKPD IVLYNNAVGD
FQVDDKTKAL LKYTGEVTWI PPAIFKSSCK IDVTYFPFDY QNCTMKFGSW SYDKAKIDLV
LIGSSMNLKD YWESGEWAII KAPGYKHDIK YNCCEEIYPD ITYSLYIRRL PLFYTINLII
PCLLISFLTV LVFYLPSDCG EKVTLCISVL LSLTVFLLVI TETIPSTSLV IPLIGEYLLF
TMIFVTLSIV ITVFVLNVHY RTPTTHTMPA WVKTIFLNLL PRVMFMTRPA SNEGNTQRPR
PFYSAELSNL NCFSRIESKV CKEGYPCQDG LCGYCHHRRA KISNFSANLT RSSSSESVDA
VLSLSALSPE IKEAIQSVKY IAENMKAQNE AKEIQDDWKY VAMVIDRIFL WVFILVCILG
TAGLFLQPLM TRDDA
