ACHG_TETCF
ID ACHG_TETCF Reviewed; 506 AA.
AC P02714;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Acetylcholine receptor subunit gamma;
DE Flags: Precursor;
GN Name=CHRNG;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6188060; DOI=10.1038/302528a0;
RA Noda M., Takahashi H., Tanabe T., Toyosato M., Kikyotani S., Furutani Y.,
RA Hirose T., Takashima H., Inayama S., Miyata T., Numa S.;
RT "Structural homology of Torpedo californica acetylcholine receptor
RT subunits.";
RL Nature 302:528-532(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6573658; DOI=10.1073/pnas.80.4.1111;
RA Claudio T., Ballivet M., Patrick J., Heinemann S.F.;
RT "Nucleotide and deduced amino acid sequences of Torpedo californica
RT acetylcholine receptor gamma subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:1111-1115(1983).
RN [3]
RP PROTEIN SEQUENCE OF 123-147, AND DISULFIDE BOND.
RX PubMed=2742850; DOI=10.1021/bi00434a048;
RA Kellaris K.V., Ware D.K., Smith S., Kyte J.;
RT "Assessment of the number of free cysteines and isolation and
RT identification of cystine-containing peptides from acetylcholine
RT receptor.";
RL Biochemistry 28:3469-3482(1989).
RN [4]
RP PHOSPHORYLATION AT TYR-381.
RX PubMed=1721053; DOI=10.1016/s0021-9258(18)54351-9;
RA Wagner K., Edson K., Heginbotham L., Post M., Huganir R.L., Czernik A.J.;
RT "Determination of the tyrosine phosphorylation sites of the nicotinic
RT acetylcholine receptor.";
RL J. Biol. Chem. 266:23784-23789(1991).
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 chains.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Seems not to be glycosylated on Asn-158.
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; V01393; CAA24682.1; -; mRNA.
DR EMBL; V01394; CAA24683.1; -; mRNA.
DR EMBL; J00966; AAA49276.1; -; mRNA.
DR PIR; A93300; ACRYG1.
DR PDB; 1OED; EM; 4.00 A; E=236-495.
DR PDB; 6UWZ; EM; 2.69 A; E=18-506.
DR PDB; 7QKO; EM; 2.90 A; E=18-506.
DR PDB; 7QL5; EM; 2.50 A; E=18-506.
DR PDB; 7QL6; EM; 3.23 A; E=18-506.
DR PDB; 7SMM; EM; 2.50 A; E=18-506.
DR PDB; 7SMQ; EM; 2.70 A; E=18-506.
DR PDB; 7SMR; EM; 2.77 A; E=18-506.
DR PDB; 7SMS; EM; 3.18 A; E=18-506.
DR PDB; 7SMT; EM; 2.56 A; E=18-506.
DR PDBsum; 1OED; -.
DR PDBsum; 6UWZ; -.
DR PDBsum; 7QKO; -.
DR PDBsum; 7QL5; -.
DR PDBsum; 7QL6; -.
DR PDBsum; 7SMM; -.
DR PDBsum; 7SMQ; -.
DR PDBsum; 7SMR; -.
DR PDBsum; 7SMS; -.
DR PDBsum; 7SMT; -.
DR AlphaFoldDB; P02714; -.
DR SMR; P02714; -.
DR ComplexPortal; CPX-2187; Acetylcholine receptor, alpha1-beta1-gamma-delta.
DR IntAct; P02714; 2.
DR BindingDB; P02714; -.
DR ChEMBL; CHEMBL2096975; -.
DR DrugCentral; P02714; -.
DR TCDB; 1.A.9.1.9; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyConnect; 7; 35 N-Linked glycans.
DR iPTMnet; P02714; -.
DR SwissPalm; P02714; -.
DR EvolutionaryTrace; P02714; -.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; IPI:ComplexPortal.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IMP:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..17
FT CHAIN 18..506
FT /note="Acetylcholine receptor subunit gamma"
FT /id="PRO_0000000338"
FT TOPO_DOM 18..235
FT /note="Extracellular"
FT TRANSMEM 236..260
FT /note="Helical"
FT TRANSMEM 269..287
FT /note="Helical"
FT TRANSMEM 303..324
FT /note="Helical"
FT TOPO_DOM 325..466
FT /note="Cytoplasmic"
FT TRANSMEM 467..490
FT /note="Helical"
FT MOD_RES 381
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:1721053"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..159
FT /evidence="ECO:0000269|PubMed:2742850"
FT CONFLICT 298
FT /note="P -> S (in Ref. 2; CAA24682)"
FT /evidence="ECO:0000305"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 46..61
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 66..83
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 156..167
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 223..234
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 238..243
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 268..287
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 299..325
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:6UWZ"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 428..467
FT /evidence="ECO:0007829|PDB:6UWZ"
FT HELIX 470..489
FT /evidence="ECO:0007829|PDB:6UWZ"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:6UWZ"
SQ SEQUENCE 506 AA; 58164 MW; 48A5F5D82BC66C9D CRC64;
MVLTLLLIIC LALEVRSENE EGRLIEKLLG DYDKRIIPAK TLDHIIDVTL KLTLTNLISL
NEKEEALTTN VWIEIQWNDY RLSWNTSEYE GIDLVRIPSE LLWLPDVVLE NNVDGQFEVA
YYANVLVYND GSMYWLPPAI YRSTCPIAVT YFPFDWQNCS LVFRSQTYNA HEVNLQLSAE
EGEAVEWIHI DPEDFTENGE WTIRHRPAKK NYNWQLTKDD TDFQEIIFFL IIQRKPLFYI
INIIAPCVLI SSLVVLVYFL PAQAGGQKCT LSISVLLAQT IFLFLIAQKV PETSLNVPLI
GKYLIFVMFV SMLIVMNCVI VLNVSLRTPN THSLSEKIKH LFLGFLPKYL GMQLEPSEET
PEKPQPRRRS SFGIMIKAEE YILKKPRSEL MFEEQKDRHG LKRVNKMTSD IDIGTTVDLY
KDLANFAPEI KSCVEACNFI AKSTKEQNDS GSENENWVLI GKVIDKACFW IALLLFSIGT
LAIFLTGHFN QVPEFPFPGD PRKYVP
