ACHA5_RAT
ID ACHA5_RAT Reviewed; 452 AA.
AC P20420;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-5;
DE Flags: Precursor;
GN Name=Chrna5; Synonyms=Acra5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1689727; DOI=10.1016/s0021-9258(19)39588-2;
RA Boulter J., O'Shea-Greenfield A., Duvoisin R.M., Connolly J.G., Wada E.,
RA Jensen A., Gardner P.D., Ballivet M., Deneris E.S., McKinnon D.,
RA Heinemann S.F., Patrick J.;
RT "Alpha 3, alpha 5, and beta 4: three members of the rat neuronal nicotinic
RT acetylcholine receptor-related gene family form a gene cluster.";
RL J. Biol. Chem. 265:4472-4482(1990).
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 seems to be composed of two different types of
CC subunits: alpha and non-alpha (beta). Interacts with LYPD6.
CC {ECO:0000250|UniProtKB:P30532}.
CC -!- INTERACTION:
CC P20420; P09483: Chrna4; NbExp=6; IntAct=EBI-10828372, EBI-7842410;
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-5/CHRNA5 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; J05231; AAA74475.1; -; mRNA.
DR PIR; A35721; A35721.
DR AlphaFoldDB; P20420; -.
DR SMR; P20420; -.
DR ComplexPortal; CPX-190; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2.
DR ComplexPortal; CPX-208; Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4.
DR ComplexPortal; CPX-215; Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2.
DR IntAct; P20420; 5.
DR STRING; 10116.ENSRNOP00000062227; -.
DR BindingDB; P20420; -.
DR ChEMBL; CHEMBL4106146; -.
DR DrugCentral; P20420; -.
DR GlyGen; P20420; 3 sites.
DR PaxDb; P20420; -.
DR PRIDE; P20420; -.
DR UCSC; RGD:2347; rat.
DR RGD; 2347; Chrna5.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P20420; -.
DR PhylomeDB; P20420; -.
DR Reactome; R-RNO-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-RNO-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR PRO; PR:P20420; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
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:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
DR GO; GO:0015464; F:acetylcholine receptor activity; ISO:RGD.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IMP:RGD.
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:0044877; F:protein-containing complex binding; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0071316; P:cellular response to nicotine; IMP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
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:0098908; P:regulation of neuronal action potential; IMP:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; ISO:RGD.
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; 2.
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 1: Evidence at protein 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..452
FT /note="Neuronal acetylcholine receptor subunit alpha-5"
FT /id="PRO_0000000358"
FT TOPO_DOM 28..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..169
FT /evidence="ECO:0000250"
FT DISULFID 219..220
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 51874 MW; 7CEB24553936B2E7 CRC64;
MVQLLAGRWR PTGARRGTRG GLPELSSAAK HEDSLFRDLF EDYERWVRPV EHLSDKIKIK
FGLAISQLVD VDEKNQLMTT NVWLKQEWID VKLRWNPDDY GGIKIIRVPS DSLWIPDIVL
FDNADGRFEG ASTKTVVRYN GTVTWTQPAN YKSSCTIDVT FFPFDLQNCS MKFGSWTYDG
SQVDIILEDQ DVDRTDFFDN GEWEIMSAMG SKGNRTDSCC WYPYITYSFV IKRLPLFYTL
FLIIPCIGLS FLTVVVFYLP SNEGEKISLC TSVLVSLTVF LLVIEEIIPS SSKVIPLIGE
YLVFTMIFVT LSIMVTVFAI NIHHRSSSTH NAMAPWVRKI FLHKLPKLLC MRSHADRYFT
QREEAESGAG PKSRNTLEAA LDCIRYITRH VVKENDVREV VEDWKFIAQV LDRMFLWTFL
LVSIIGTLGL FVPVIYKWAN IIVPVHIGNT IK
