ACHA7_CHICK
ID ACHA7_CHICK Reviewed; 502 AA.
AC P22770;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
DE Flags: Precursor;
GN Name=CHRNA7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1702646; DOI=10.1016/0896-6273(90)90344-f;
RA Couturier S., Bertrand D., Matter J.-M., Hernandez M.-C., Bertrand S.,
RA Millar N., Valera S., Barkas T., Ballivet M.;
RT "A neuronal nicotinic acetylcholine receptor subunit (alpha 7) is
RT developmentally regulated and forms a homo-oligomeric channel blocked by
RT alpha-BTX.";
RL Neuron 5:847-856(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2369519; DOI=10.1016/0896-6273(90)90031-a;
RA Schoepfer R., Conroy W.G., Whiting P., Gore M., Lindstroem J.;
RT "Brain alpha-bungarotoxin binding protein cDNAs and MAbs reveal subtypes of
RT this branch of the ligand-gated ion channel gene superfamily.";
RL Neuron 5:35-48(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=White leghorn; TISSUE=Erythrocyte;
RX PubMed=1425587; DOI=10.1002/j.1460-2075.1992.tb05554.x;
RA Matter-Sadzinski L., Hernandez M.-C., Roztocil T., Ballivet M.,
RA Matter J.-M.;
RT "Neuronal specificity of the alpha 7 nicotinic acetylcholine receptor
RT promoter develops during morphogenesis of the central nervous system.";
RL EMBO J. 11:4529-4538(1992).
RN [4]
RP PROTEIN SEQUENCE OF 24-47.
RC TISSUE=Brain;
RX PubMed=3860855; DOI=10.1073/pnas.82.15.5208;
RA Conti-Tronconi B.M., Dunn S.M.J., Barnard E.A., Dolly J.O., Lai F.A.,
RA Ray N., Raftery M.A.;
RT "Brain and muscle nicotinic acetylcholine receptors are different but
RT homologous proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5208-5212(1985).
RN [5]
RP MUTAGENESIS OF LEU-270.
RX PubMed=1719423; DOI=10.1038/353846a0;
RA Recah F., Bertrand D., Galzi J.-L., Devillers-Thiery A., Mulle C.,
RA Hussy N., Bertrand S., Ballivet M., Changeux J.-P.;
RT "Mutations in the channel domain alter desensitization of a neuronal
RT nicotinic receptor.";
RL Nature 353:846-849(1991).
RN [6]
RP MUTAGENESIS TO CONVERT ION SELECTIVITY FROM CATIONIC TO ANIONIC.
RX PubMed=1383829; DOI=10.1038/359500a0;
RA Galzi J.-L., Devillers-Thiery A., Hussy N., Bertrand S., Changeux J.-P.,
RA Bertrand D.;
RT "Mutations in the channel domain of a neuronal nicotinic receptor convert
RT ion selectivity from cationic to anionic.";
RL Nature 359:500-505(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: Forms a homooligomeric channel blocked by alpha-bungarotoxin.
CC The structure is probably pentameric (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Alpha-7 transcripts transiently accumulate in the
CC developing optic tectum between E5 and E16.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-7/CHRNA7 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X68586; CAA48576.1; -; mRNA.
DR EMBL; X52295; CAA36543.1; -; mRNA.
DR EMBL; X68246; CAA48317.1; -; Genomic_DNA.
DR PIR; JN0113; JN0113.
DR PDB; 1KC4; NMR; -; B=201-219.
DR PDB; 1KL8; NMR; -; B=201-219.
DR PDBsum; 1KC4; -.
DR PDBsum; 1KL8; -.
DR AlphaFoldDB; P22770; -.
DR SMR; P22770; -.
DR ComplexPortal; CPX-235; Neuronal nicotinic acetylcholine receptor complex, alpha7.
DR ComplexPortal; CPX-239; Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2.
DR IntAct; P22770; 1.
DR STRING; 9031.ENSGALP00000006509; -.
DR iPTMnet; P22770; -.
DR SwissPalm; P22770; -.
DR PaxDb; P22770; -.
DR VEuPathDB; HostDB:geneid_374001; -.
DR eggNOG; KOG3646; Eukaryota.
DR InParanoid; P22770; -.
DR PhylomeDB; P22770; -.
DR EvolutionaryTrace; P22770; -.
DR PRO; PR:P22770; -.
DR Proteomes; UP000000539; 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:0030424; C:axon; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0030425; C:dendrite; IDA:AgBase.
DR GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
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:0001540; F:amyloid-beta binding; ISS:UniProtKB.
DR GO; GO:0017081; F:chloride channel regulator activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IDA:ComplexPortal.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; 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 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; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3860855"
FT CHAIN 24..502
FT /note="Neuronal acetylcholine receptor subunit alpha-7"
FT /id="PRO_0000000370"
FT TOPO_DOM 24..230
FT /note="Extracellular"
FT TRANSMEM 231..255
FT /note="Helical"
FT TRANSMEM 262..280
FT /note="Helical"
FT TRANSMEM 296..317
FT /note="Helical"
FT TOPO_DOM 318..469
FT /note="Cytoplasmic"
FT TRANSMEM 470..490
FT /note="Helical"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..164
FT /evidence="ECO:0000250"
FT DISULFID 212..213
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250"
FT MUTAGEN 270
FT /note="L->S,T: Suppresses inhibition by the open-channel
FT blocker QX-222."
FT /evidence="ECO:0000269|PubMed:1719423"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1KL8"
SQ SEQUENCE 502 AA; 56947 MW; 572325D4309AD2FD CRC64;
MGLRALMLWL LAAAGLVRES LQGEFQRKLY KELLKNYNPL ERPVANDSQP LTVYFTLSLM
QIMDVDEKNQ VLTTNIWLQM YWTDHYLQWN VSEYPGVKNV RFPDGLIWKP DILLYNSADE
RFDATFHTNV LVNSSGHCQY LPPGIFKSSC YIDVRWFPFD VQKCNLKFGS WTYGGWSLDL
QMQEADISGY ISNGEWDLVG IPGKRTESFY ECCKEPYPDI TFTVTMRRRT LYYGLNLLIP
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE DKVRPACQHK
QRRCSLSSME MNTVSGQQCS NGNMLYIGFR GLDGVHCTPT TDSGVICGRM TCSPTEEENL
LHSGHPSEGD PDLAKILEEV RYIANRFRDQ DEEEAICNEW KFAASVVDRL CLMAFSVFTI
ICTIGILMSA PNFVEAVSKD FA
