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Neuronal acetylcholine receptor subunit alpha-7

 ACHA7_HUMAN             Reviewed;         502 AA.
P36544; A8K7Q4; B4DFS0; Q15826; Q8IUZ4; Q96RH2; Q99555; Q9BXH0;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 5.
25-OCT-2017, entry version 187.
RecName: Full=Neuronal acetylcholine receptor subunit alpha-7;
Flags: Precursor;
Name=CHRNA7; Synonyms=NACHRA7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8145738;
Peng X., Katz M., Gerzanich V., Anand R., Lindstrom J.;
"Human alpha 7 acetylcholine receptor: cloning of the alpha 7 subunit
from the SH-SY5Y cell line and determination of pharmacological
properties of native receptors and functional alpha 7 homomers
expressed in Xenopus oocytes.";
Mol. Pharmacol. 45:546-554(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
Logel J., Drebing C., Barnhart M., Antle C., Leonard S.;
"Nucleotide sequence and transcript size of the alpha-7 neuronal
nicotinic acetylcholine receptor in human postmortem brain.";
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8906617; DOI=10.1007/BF02736842;
Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A.,
Chavez-Noriega L.E., Johnson E.C., Velicelebi G., Harpold M.M.;
"Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-
beta 4 nicotinic acetylcholine receptor subunits and functional
expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta
4 subunits.";
J. Mol. Neurosci. 7:217-228(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9009220; DOI=10.1016/S0014-5793(96)01383-X;
Groot Kormelink P.J., Luyten W.H.M.L.;
"Cloning and sequence of full-length cDNAs encoding the human neuronal
nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and
expression of seven nAChR subunits in the human neuroblastoma cell
line SH-SY5Y and/or IMR-32.";
FEBS Lett. 400:309-314(1997).
[5]
SEQUENCE REVISION.
Groot Kormelink P.J., Luyten W.H.M.L.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Keratinocyte;
Arredondo J., Grando S.A.;
"Cloning cholinergic receptors in human keratinocytes.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-502 (ISOFORM 1).
TISSUE=Brain;
Doucette-Stamm L., Monteggia L.M., Donnelly-Roberts D., Wang M.T.,
Lee J., Tian J., Giordano T.;
"Cloning and sequence of the human alpha-7 nicotinic acetylcholine
receptor.";
Drug Dev. Res. 30:252-256(1993).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-502 (ISOFORM 1).
TISSUE=Retina;
PubMed=8188270; DOI=10.1006/geno.1994.1075;
Chini B., Raimondi E., Elgoyhen A.B., Moralli D., Balzaretti M.,
Heinemann S.F.;
"Molecular cloning and chromosomal localization of the human alpha 7-
nicotinic receptor subunit gene (CHRNA7).";
Genomics 19:379-381(1994).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-129.
PubMed=11829490; DOI=10.1006/geno.2002.6694;
Riley B., Williamson M., Collier D., Wilkie H., Makoff A.;
"A 3-Mb map of a large segmental duplication overlapping the alpha7-
nicotinic acetylcholine receptor gene (CHRNA7) at human 15q13-q14.";
Genomics 79:197-209(2002).
[13]
SUBUNIT, AND MUTAGENESIS OF GLN-139.
PubMed=15609996; DOI=10.1021/bi048918g;
Ellison M., Gao F., Wang H.L., Sine S.M., McIntosh J.M., Olivera B.M.;
"Alpha-conotoxins ImI and ImII target distinct regions of the human
alpha7 nicotinic acetylcholine receptor and distinguish human
nicotinic receptor subtypes.";
Biochemistry 43:16019-16026(2004).
[14]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[15]
INTERACTION WITH RIC3.
PubMed=15504725; DOI=10.1074/jbc.M410039200;
Williams M.E., Burton B., Urrutia A., Shcherbatko A.,
Chavez-Noriega L.E., Cohen C.J., Aiyar J.;
"Ric-3 promotes functional expression of the nicotinic acetylcholine
receptor alpha7 subunit in mammalian cells.";
J. Biol. Chem. 280:1257-1263(2005).
[16]
INTERACTION WITH RIC3.
PubMed=16120769; DOI=10.1124/mol.105.017459;
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R.,
Gibb A.J., Millar N.S.;
"RIC-3 enhances functional expression of multiple nicotinic
acetylcholine receptor subtypes in mammalian cells.";
Mol. Pharmacol. 68:1431-1438(2005).
[17]
INTERACTION WITH LYPD6.
PubMed=27344019; DOI=10.1111/jnc.13718;
Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N.,
Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M.,
Kohlmeier K.A., Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S.;
"Functional interaction between Lypd6 and nicotinic acetylcholine
receptors.";
J. Neurochem. 138:806-820(2016).
-!- FUNCTION: After binding acetylcholine, the AChR responds by an
extensive change in conformation that affects all subunits and
leads to opening of an ion-conducting channel across the plasma
membrane. The channel is blocked by alpha-bungarotoxin.
-!- SUBUNIT: Homopentamer (By similarity). Interacts with RIC3; which
is required for proper folding and assembly (PubMed:15504725,
PubMed:16120769). Interacts with LYPD6 (PubMed:27344019).
Interacts with the alpha-conotoxin RgIA (By similarity). Interacts
with alpha-conotoxins ImI and ImII (PubMed:15609996).
{ECO:0000250|UniProtKB:P54131, ECO:0000250|UniProtKB:Q05941,
ECO:0000269|PubMed:15504725, ECO:0000269|PubMed:15609996,
ECO:0000269|PubMed:16120769, ECO:0000269|PubMed:27344019}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P36544-1; Sequence=Displayed;
Name=2;
IsoId=P36544-2; Sequence=VSP_043019;
Note=No experimental confirmation available.;
Name=3;
IsoId=P36544-3; Sequence=VSP_058107, VSP_058108;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- MASS SPECTROMETRY: Mass=54157.68; Method=MALDI; Range=23-502;
Evidence={ECO:0000269|PubMed:11840567};
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
7/CHRNA7 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37571.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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EMBL; X70297; CAA49778.1; -; mRNA.
EMBL; U40583; AAA83561.1; -; mRNA.
EMBL; U62436; AAB40114.1; -; mRNA.
EMBL; Y08420; CAA69697.1; -; mRNA.
EMBL; AF385585; AAK68111.1; -; mRNA.
EMBL; AK292069; BAF84758.1; -; mRNA.
EMBL; AK294229; BAG57531.1; -; mRNA.
EMBL; AC004460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC012236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC021316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC058803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037571; AAH37571.1; ALT_SEQ; mRNA.
EMBL; BC101345; AAI01346.1; -; mRNA.
EMBL; L25827; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; Z23141; CAA80672.1; -; mRNA.
EMBL; AF332758; AAK19515.1; -; Genomic_DNA.
CCDS; CCDS10027.1; -. [P36544-1]
CCDS; CCDS53924.1; -. [P36544-2]
PIR; G02259; G02259.
PIR; I37185; ACHUA7.
RefSeq; NP_000737.1; NM_000746.5. [P36544-1]
RefSeq; NP_001177384.1; NM_001190455.2. [P36544-2]
RefSeq; NP_683709.1; NM_148911.1.
RefSeq; XP_005254807.1; XM_005254750.2.
RefSeq; XP_016877373.1; XM_017021884.1.
UniGene; Hs.510853; -.
UniGene; Hs.511772; -.
UniGene; Hs.713151; -.
PDB; 2MAW; NMR; -; A=228-326, A=467-495.
PDB; 5AFH; X-ray; 2.40 A; A/B/C/D/E=23-227.
PDB; 5AFJ; X-ray; 2.20 A; A/B/C/D/E=23-227.
PDB; 5AFK; X-ray; 2.38 A; A/B/C/D/E=23-227.
PDB; 5AFL; X-ray; 2.38 A; A/B/C/D/E=23-227.
PDB; 5AFM; X-ray; 2.85 A; A/B/C/D/E=23-38, A/B/C/D/E=52-71, A/B/C/D/E=77-98, A/C/D/E=23-192, A/C/D/E=96-227, B=131-141, B=164-168, B=178-192.
PDB; 5AFN; X-ray; 2.15 A; A/B/C/D/E=23-227.
PDBsum; 2MAW; -.
PDBsum; 5AFH; -.
PDBsum; 5AFJ; -.
PDBsum; 5AFK; -.
PDBsum; 5AFL; -.
PDBsum; 5AFM; -.
PDBsum; 5AFN; -.
ProteinModelPortal; P36544; -.
SMR; P36544; -.
BioGrid; 107561; 3.
IntAct; P36544; 3.
BindingDB; P36544; -.
ChEMBL; CHEMBL2492; -.
DrugBank; DB01351; Amobarbital.
DrugBank; DB01352; Aprobarbital.
DrugBank; DB01483; Barbital.
DrugBank; DB01496; Barbituric acid derivative.
DrugBank; DB00237; Butabarbital.
DrugBank; DB00241; Butalbital.
DrugBank; DB01353; Butethal.
DrugBank; DB09028; Cytisine.
DrugBank; DB00514; Dextromethorphan.
DrugBank; DB00898; Ethanol.
DrugBank; DB00674; Galantamine.
DrugBank; DB05708; GTS-21.
DrugBank; DB01354; Heptabarbital.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB00463; Metharbital.
DrugBank; DB00849; Methylphenobarbital.
DrugBank; DB00184; Nicotine.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB00794; Primidone.
DrugBank; DB05740; RPI-78M.
DrugBank; DB00418; Secobarbital.
DrugBank; DB00306; Talbutal.
DrugBank; DB00599; Thiopental.
DrugBank; DB01273; Varenicline.
GuidetoPHARMACOLOGY; 468; -.
TCDB; 1.A.9.1.7; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
iPTMnet; P36544; -.
PhosphoSitePlus; P36544; -.
SwissPalm; P36544; -.
BioMuta; CHRNA7; -.
DMDM; 2506127; -.
PaxDb; P36544; -.
PRIDE; P36544; -.
Ensembl; ENST00000306901; ENSP00000303727; ENSG00000175344. [P36544-1]
Ensembl; ENST00000437966; ENSP00000399087; ENSG00000175344. [P36544-3]
Ensembl; ENST00000454250; ENSP00000407546; ENSG00000175344. [P36544-2]
GeneID; 1139; -.
GeneID; 89832; -.
KEGG; hsa:1139; -.
UCSC; uc001zft.5; human. [P36544-1]
CTD; 1139; -.
CTD; 89832; -.
DisGeNET; 1139; -.
DisGeNET; 89832; -.
EuPathDB; HostDB:ENSG00000175344.16; -.
GeneCards; CHRNA7; -.
HGNC; HGNC:1960; CHRNA7.
HPA; CAB033624; -.
HPA; HPA029422; -.
MalaCards; CHRNA7; -.
MIM; 118511; gene.
neXtProt; NX_P36544; -.
OpenTargets; ENSG00000175344; -.
Orphanet; 199318; 15q13.3 microdeletion syndrome.
PharmGKB; PA114; -.
PharmGKB; PA26483; -.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00790000122957; -.
HOGENOM; HOG000006756; -.
HOVERGEN; HBG003756; -.
InParanoid; P36544; -.
KO; K04809; -.
OMA; EAICNEW; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; P36544; -.
TreeFam; TF315605; -.
Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
SignaLink; P36544; -.
SIGNOR; P36544; -.
ChiTaRS; CHRNA7; human.
GeneWiki; CHRFAM7A; -.
GeneWiki; CHRNA7; -.
PRO; PR:P36544; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000175344; -.
CleanEx; HS_CHRNA7; -.
ExpressionAtlas; P36544; baseline and differential.
Genevisible; P36544; HS.
GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; ISS:ARUK-UCL.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042166; F:acetylcholine binding; IDA:UniProtKB.
GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:UniProtKB.
GO; GO:0005262; F:calcium channel activity; TAS:ARUK-UCL.
GO; GO:0017081; F:chloride channel regulator activity; IDA:UniProtKB.
GO; GO:0005216; F:ion channel activity; IDA:ARUK-UCL.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISS:ARUK-UCL.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0042113; P:B cell activation; IEA:Ensembl.
GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0050890; P:cognition; IMP:UniProtKB.
GO; GO:0140059; P:dendrite arborization; ISS:ARUK-UCL.
GO; GO:0097061; P:dendritic spine organization; ISS:ARUK-UCL.
GO; GO:0006897; P:endocytosis; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0060112; P:generation of ovulation cycle rhythm; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; IDA:ParkinsonsUK-UCL.
GO; GO:0006811; P:ion transport; NAS:UniProtKB.
GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
GO; GO:0007613; P:memory; ISS:ARUK-UCL.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISS:ARUK-UCL.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IGI:ARUK-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:MGI.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:ARUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISS:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ARUK-UCL.
GO; GO:0001988; P:positive regulation of heart rate involved in baroreceptor response to decreased systemic arterial blood pressure; IEA:Ensembl.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0051247; P:positive regulation of protein metabolic process; ISS:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:ARUK-UCL.
GO; GO:1905906; P:regulation of amyloid fibril formation; ISS:ARUK-UCL.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IGI:ARUK-UCL.
GO; GO:1901214; P:regulation of neuron death; ISS:ARUK-UCL.
GO; GO:0014061; P:regulation of norepinephrine secretion; IEA:Ensembl.
GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:1905144; P:response to acetylcholine; IDA:ARUK-UCL.
GO; GO:1904645; P:response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0035094; P:response to nicotine; IDA:UniProtKB.
GO; GO:0050893; P:sensory processing; ISS:ARUK-UCL.
GO; GO:0007614; P:short-term memory; ISS:ARUK-UCL.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0050808; P:synapse organization; ISS:ARUK-UCL.
GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IEA:Ensembl.
Gene3D; 1.20.58.390; -; 1.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00254; NICOTINICR.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 502 Neuronal acetylcholine receptor subunit
alpha-7.
/FTId=PRO_0000000366.
TOPO_DOM 23 230 Extracellular. {ECO:0000255}.
TRANSMEM 231 255 Helical. {ECO:0000255}.
TRANSMEM 262 280 Helical. {ECO:0000255}.
TRANSMEM 296 317 Helical. {ECO:0000255}.
TOPO_DOM 318 469 Cytoplasmic. {ECO:0000255}.
TRANSMEM 470 490 Helical. {ECO:0000255}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 150 164 {ECO:0000250}.
DISULFID 212 213 Associated with receptor activation.
{ECO:0000250}.
VAR_SEQ 18 18 H -> HGKATASPPSTPPWDPGHIPGASVRPAPGP (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043019.
VAR_SEQ 81 102 SWTDHYLQWNVSEYPGVKTVRF -> AYSRVPATSMYAGFP
LMCSTAN (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_058107.
VAR_SEQ 103 502 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_058108.
MUTAGEN 139 139 Q->S: 115-fold more potently inhibited by
the alpha-conotoxin ImI; but no change in
inhibition by the alpha-conotoxin ImII.
{ECO:0000269|PubMed:15609996}.
CONFLICT 11 11 A -> G (in Ref. 1; CAA49778).
{ECO:0000305}.
CONFLICT 58 58 S -> N (in Ref. 2; AAA83561 and 6;
AAK68111). {ECO:0000305}.
CONFLICT 134 134 S -> P (in Ref. 2; AAA83561 and 6;
AAK68111). {ECO:0000305}.
CONFLICT 364 364 C -> S (in Ref. 11; CAA80672).
{ECO:0000305}.
CONFLICT 375 375 A -> G (in Ref. 1; CAA49778).
{ECO:0000305}.
CONFLICT 409 413 RMACS -> AWPAP (in Ref. 11; CAA80672).
{ECO:0000305}.
HELIX 24 34 {ECO:0000244|PDB:5AFN}.
STRAND 51 66 {ECO:0000244|PDB:5AFN}.
TURN 67 70 {ECO:0000244|PDB:5AFN}.
STRAND 71 83 {ECO:0000244|PDB:5AFN}.
HELIX 85 87 {ECO:0000244|PDB:5AFN}.
TURN 91 93 {ECO:0000244|PDB:5AFN}.
STRAND 94 96 {ECO:0000244|PDB:5AFM}.
STRAND 99 103 {ECO:0000244|PDB:5AFN}.
HELIX 104 106 {ECO:0000244|PDB:5AFN}.
STRAND 112 114 {ECO:0000244|PDB:5AFN}.
STRAND 118 120 {ECO:0000244|PDB:5AFN}.
STRAND 129 133 {ECO:0000244|PDB:5AFN}.
STRAND 137 140 {ECO:0000244|PDB:5AFN}.
STRAND 143 149 {ECO:0000244|PDB:5AFN}.
STRAND 158 160 {ECO:0000244|PDB:5AFN}.
STRAND 162 172 {ECO:0000244|PDB:5AFN}.
TURN 175 177 {ECO:0000244|PDB:5AFN}.
STRAND 178 182 {ECO:0000244|PDB:5AFN}.
STRAND 194 208 {ECO:0000244|PDB:5AFN}.
STRAND 217 227 {ECO:0000244|PDB:5AFN}.
HELIX 229 253 {ECO:0000244|PDB:2MAW}.
HELIX 260 282 {ECO:0000244|PDB:2MAW}.
STRAND 286 288 {ECO:0000244|PDB:2MAW}.
HELIX 293 317 {ECO:0000244|PDB:2MAW}.
STRAND 324 326 {ECO:0000244|PDB:2MAW}.
HELIX 467 489 {ECO:0000244|PDB:2MAW}.
SEQUENCE 502 AA; 56449 MW; D94B3A482EAA0E42 CRC64;
MRCSPGGVWL ALAASLLHVS LQGEFQRKLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL
QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN VSEYPGVKTV RFPDGQIWKP DILLYNSADE
RFDATFHTNV LVNSSGHCQY LPPGIFKSSC YIDVRWFPFD VQHCKLKFGS WSYGGWSLDL
QMQEADISGY IPNGEWDLVG IPGKRSERFY ECCKEPYPDV TFTVTMRRRT LYYGLNLLIP
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST
MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE DKVRPACQHK
QRRCSLASVE MSAVAPPPAS NGNLLYIGFR GLDGVHCVPT PDSGVVCGRM ACSPTHDEHL
LHGGQPPEGD PDLAKILEEV RYIANRFRCQ DESEAVCSEW KFAACVVDRL CLMAFSVFTI
ICTIGILMSA PNFVEAVSKD FA


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