ACHG_RAT
ID ACHG_RAT Reviewed; 519 AA.
AC P18916;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Acetylcholine receptor subunit gamma;
DE Flags: Precursor;
GN Name=Chrng; Synonyms=Achrg;
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].
RC TISSUE=Muscle;
RX PubMed=1702709; DOI=10.1111/j.1432-1033.1990.tb15637.x;
RA Witzemann V., Stein E., Barg B., Konno T., Koenen M., Kues W., Criado M.,
RA Hofmann M., Sakmann B.;
RT "Primary structure and functional expression of the alpha-, beta-, gamma-,
RT delta- and epsilon-subunits of the acetylcholine receptor from rat
RT muscle.";
RL Eur. J. Biochem. 194:437-448(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-306.
RX PubMed=3666131; DOI=10.1016/0014-5793(87)80518-5;
RA Witzemann V., Barg B., Nishikawa Y., Sakmann B., Numa S.;
RT "Differential regulation of muscle acetylcholine receptor gamma- and
RT epsilon-subunit mRNAs.";
RL FEBS Lett. 223:104-112(1987).
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: Pentamer of two alpha chains, and one each of the beta, delta,
CC and gamma (in immature muscle) or epsilon (in mature muscle) chains.
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. Gamma/CHRNG sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X74834; CAA52828.1; -; mRNA.
DR EMBL; X06364; CAA29662.1; -; Genomic_DNA.
DR PIR; S13874; S13874.
DR RefSeq; NP_062018.1; NM_019145.1.
DR AlphaFoldDB; P18916; -.
DR SMR; P18916; -.
DR ComplexPortal; CPX-253; Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma.
DR STRING; 10116.ENSRNOP00000026529; -.
DR BindingDB; P18916; -.
DR ChEMBL; CHEMBL4523658; -.
DR GlyGen; P18916; 2 sites.
DR PaxDb; P18916; -.
DR GeneID; 25753; -.
DR KEGG; rno:25753; -.
DR UCSC; RGD:2354; rat.
DR CTD; 1146; -.
DR RGD; 2354; Chrng.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P18916; -.
DR OrthoDB; 588360at2759; -.
DR PhylomeDB; P18916; -.
DR Reactome; R-RNO-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR PRO; PR:P18916; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0006812; P:cation transport; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IDA:RGD.
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 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..519
FT /note="Acetylcholine receptor subunit gamma"
FT /id="PRO_0000000336"
FT TOPO_DOM 23..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..164
FT /evidence="ECO:0000250"
SQ SEQUENCE 519 AA; 58621 MW; 1C97A83DE42A0D09 CRC64;
MHGGQGPQLL LLLLATCLGA QSRNQEERLL ADLMRNYDPH LRPAERDSDV VNVSLKLTLT
NLISLNEREE ALTTNVWIEM QWCDYRLRWD PKDYEGLWIL RVPSTMVWQP DIVLGNNVDG
VFEVALYCNV LVSPDGCIYW LPPAIFRSSC SISVTYFPFD WQNCSLVFQS QTYSTSEINL
QLSQEDGQAI EWIFIDPEAF TENGEWAIRH RPAKMLLDPV TPAEEAGHQK VVFYLLIQRK
PLFYVINIIV PCVLISSVAI LIYFLPAKAG GQKCTVATNV LLAQTVFLFL VAKKVPETSQ
AVPLISKYLT FLMVVTILIV VNSVVVLNVS LRSPHTHSMA RGVRKVFLRL LPQLLRMHVH
PRAPAAVQDA RLRLQNGSSS GWPIMTREEG DLCLPRSELL FRQRQRNGLV QAVLEKLENG
PEMRQSQEFC GSLKQASPAI QACVDACNLM ARARHQQSHF DSGNEEWLLV GRVLDRVCFL
AMLSLFICGT AGIFLMAHYN QVPDLPFPGD PRPYLPLPD
