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Neuronal acetylcholine receptor subunit alpha-9 (Nicotinic acetylcholine receptor subunit alpha-9) (NACHR alpha-9)

 ACHA9_HUMAN             Reviewed;         479 AA.
Q9UGM1; Q14CY7; Q4W5A2; Q9NYV2;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
27-SEP-2017, entry version 154.
RecName: Full=Neuronal acetylcholine receptor subunit alpha-9;
AltName: Full=Nicotinic acetylcholine receptor subunit alpha-9;
Short=NACHR alpha-9;
Flags: Precursor;
Name=CHRNA9; Synonyms=NACHRA9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CHRNA10,
SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT
SER-442.
TISSUE=Embryo;
PubMed=11752216; DOI=10.1124/mol.61.1.150;
Sgard F., Charpantier E., Bertrand S., Walker N., Caput D., Graham D.,
Bertrand D., Besnard F.;
"A novel human nicotinic receptor subunit, alpha10, that confers
functionality to the alpha9-subunit.";
Mol. Pharmacol. 61:150-159(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-442.
PubMed=12697997; DOI=10.1159/000069804;
Lustig L.R., Peng H.;
"Chromosome location and characterization of the human nicotinic
acetylcholine receptor subunit alpha (alpha) 9 (CHRNA9) gene.";
Cytogenet. Genome Res. 98:154-159(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-442.
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-476, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11021840; DOI=10.1016/S0002-9440(10)64651-2;
Nguyen V.T., Ndoye A., Grando S.A.;
"Novel human alpha9 acetylcholine receptor regulating keratinocyte
adhesion is targeted by Pemphigus vulgaris autoimmunity.";
Am. J. Pathol. 157:1377-1391(2000).
[6]
TISSUE SPECIFICITY.
PubMed=15531379; DOI=10.1016/j.lfs.2004.05.031;
Peng H., Ferris R.L., Matthews T., Hiel H., Lopez-Albaitero A.,
Lustig L.R.;
"Characterization of the human nicotinic acetylcholine receptor
subunit alpha (alpha) 9 (CHRNA9) and alpha (alpha) 10 (CHRNA10) in
lymphocytes.";
Life Sci. 76:263-280(2004).
[7]
MUTAGENESIS OF ILE-86, AND SUBUNIT.
PubMed=22774872; DOI=10.1111/j.1471-4159.2012.07867.x;
Azam L., McIntosh J.M.;
"Molecular basis for the differential sensitivity of rat and human
alpha9alpha10 nAChRs to alpha-conotoxin RgIA.";
J. Neurochem. 122:1137-1144(2012).
[8]
X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 26-237, FUNCTION,
SUBCELLULAR LOCATION, DISULFIDE BOND, AND GLYCOSYLATION.
PubMed=25282151; DOI=10.1038/nsmb.2900;
Zouridakis M., Giastas P., Zarkadas E., Chroni-Tzartou D.,
Bregestovski P., Tzartos S.J.;
"Crystal structures of free and antagonist-bound states of human
alpha9 nicotinic receptor extracellular domain.";
Nat. Struct. Mol. Biol. 21:976-980(2014).
-!- FUNCTION: Ionotropic receptor with a probable role in the
modulation of auditory stimuli. Agonist binding induces a
conformation change that leads to the opening of an ion-conducting
channel across the plasma membrane (PubMed:11752216,
PubMed:25282151). The channel is permeable to a range of divalent
cations including calcium, the influx of which may activate a
potassium current which hyperpolarizes the cell membrane
(PubMed:11752216, PubMed:25282151). In the ear, this may lead to a
reduction in basilar membrane motion, altering the activity of
auditory nerve fibers and reducing the range of dynamic hearing.
This may protect against acoustic trauma. May also regulate
keratinocyte adhesion (PubMed:11021840).
{ECO:0000269|PubMed:11021840, ECO:0000269|PubMed:11752216,
ECO:0000269|PubMed:25282151, ECO:0000305}.
-!- SUBUNIT: Can form homo- or heterooligomeric channels in
conjunction with CHRNA10 (PubMed:11752216). The native outer hair
cell receptor may be composed of CHRNA9-CHRNA10 heterooligomers.
Interacts with the alpha-conotoxon RgIA (PubMed:22774872).
{ECO:0000269|PubMed:11752216, ECO:0000269|PubMed:22774872}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Cell membrane {ECO:0000269|PubMed:25282151}; Multi-pass membrane
protein {ECO:0000305|PubMed:25282151}.
-!- TISSUE SPECIFICITY: Expressed in cochlea, keratinocytes, pituitary
gland, B-cells and T-cells. {ECO:0000269|PubMed:11021840,
ECO:0000269|PubMed:11752216, ECO:0000269|PubMed:15531379}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:25282151}.
-!- MISCELLANEOUS: The heterooligomeric receptor composed of CHRNA9
and CHRNA10 has an atypical pharmacological profile, binding
several non-nicotinic ligands including strychnine (a glycine
receptor antagonist) and atropine (a muscarinic acetylcholine
receptor antagonist). {ECO:0000305|PubMed:11752216}.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
9/CHRNA9 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ243342; CAB65091.1; -; mRNA.
EMBL; AY123244; AAM74523.1; -; Genomic_DNA.
EMBL; AC118275; AAY40986.1; -; Genomic_DNA.
EMBL; BC113549; AAI13550.1; -; mRNA.
EMBL; BC113575; AAI13576.1; -; mRNA.
EMBL; AF227732; AAF61920.1; -; mRNA.
CCDS; CCDS3459.1; -.
RefSeq; NP_060051.2; NM_017581.3.
UniGene; Hs.272278; -.
PDB; 4D01; X-ray; 1.80 A; A=26-237.
PDB; 4UXU; X-ray; 1.71 A; A/B=26-237.
PDB; 4UY2; X-ray; 2.70 A; A/B=26-237.
PDBsum; 4D01; -.
PDBsum; 4UXU; -.
PDBsum; 4UY2; -.
ProteinModelPortal; Q9UGM1; -.
SMR; Q9UGM1; -.
BioGrid; 120731; 75.
CORUM; Q9UGM1; -.
DIP; DIP-61053N; -.
STRING; 9606.ENSP00000312663; -.
BindingDB; Q9UGM1; -.
ChEMBL; CHEMBL2184; -.
DrugBank; DB05069; ATG003.
DrugBank; DB00898; Ethanol.
DrugBank; DB00674; Galantamine.
DrugBank; DB05137; Lobeline.
DrugBank; DB00184; Nicotine.
DrugBank; DB05740; RPI-78M.
DrugBank; DB08837; Tetraethylammonium.
GuidetoPHARMACOLOGY; 469; -.
iPTMnet; Q9UGM1; -.
PhosphoSitePlus; Q9UGM1; -.
BioMuta; CHRNA9; -.
DMDM; 308153406; -.
MaxQB; Q9UGM1; -.
PaxDb; Q9UGM1; -.
PeptideAtlas; Q9UGM1; -.
PRIDE; Q9UGM1; -.
DNASU; 55584; -.
Ensembl; ENST00000310169; ENSP00000312663; ENSG00000174343.
GeneID; 55584; -.
KEGG; hsa:55584; -.
UCSC; uc003gva.2; human.
CTD; 55584; -.
DisGeNET; 55584; -.
EuPathDB; HostDB:ENSG00000174343.5; -.
GeneCards; CHRNA9; -.
H-InvDB; HIX0031380; -.
HGNC; HGNC:14079; CHRNA9.
MIM; 605116; gene.
neXtProt; NX_Q9UGM1; -.
OpenTargets; ENSG00000174343; -.
PharmGKB; PA26493; -.
eggNOG; KOG3645; Eukaryota.
eggNOG; ENOG410XQGR; LUCA.
GeneTree; ENSGT00790000122957; -.
HOGENOM; HOG000006756; -.
HOVERGEN; HBG003756; -.
InParanoid; Q9UGM1; -.
KO; K04810; -.
OMA; ATKNVIM; -.
OrthoDB; EOG091G0R20; -.
PhylomeDB; Q9UGM1; -.
TreeFam; TF315605; -.
Reactome; R-HSA-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
ChiTaRS; CHRNA9; human.
GeneWiki; CHRNA9; -.
GenomeRNAi; 55584; -.
PRO; PR:Q9UGM1; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000174343; -.
CleanEx; HS_CHRNA9; -.
Genevisible; Q9UGM1; HS.
GO; GO:0005892; C:acetylcholine-gated channel complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
GO; GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IGI:MGI.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR006201; Neur_channel.
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; Calcium; Calcium channel; Calcium transport;
Cell junction; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Membrane; Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 479 Neuronal acetylcholine receptor subunit
alpha-9.
/FTId=PRO_0000000371.
TOPO_DOM 26 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 262 Helical. {ECO:0000255}.
TRANSMEM 269 287 Helical. {ECO:0000255}.
TRANSMEM 302 323 Helical. {ECO:0000255}.
TOPO_DOM 324 457 Cytoplasmic. {ECO:0000255}.
TRANSMEM 458 476 Helical. {ECO:0000255}.
SITE 146 146 Key residue important for potent
inhibition of the CHRNA9-CHRNA10 receptor
by the alpha-conotoxin RgIA (AC P0C1D0).
{ECO:0000250|UniProtKB:P43144}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 155 169 {ECO:0000269|PubMed:25282151}.
DISULFID 219 220 {ECO:0000269|PubMed:25282151}.
VARIANT 96 96 R -> Q (in dbSNP:rs10024518).
/FTId=VAR_031151.
VARIANT 315 315 A -> V (in dbSNP:rs55633891).
/FTId=VAR_060996.
VARIANT 442 442 N -> S (in dbSNP:rs10009228).
{ECO:0000269|PubMed:11752216,
ECO:0000269|PubMed:12697997,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_025425.
MUTAGEN 86 86 I->T: The CHRNA9-CHRNA10 receptor is 250-
fold more potently inhibited by the
alpha-conotoxin RgIA.
{ECO:0000269|PubMed:22774872}.
HELIX 30 39 {ECO:0000244|PDB:4UXU}.
STRAND 49 51 {ECO:0000244|PDB:4UY2}.
STRAND 56 71 {ECO:0000244|PDB:4UXU}.
TURN 72 75 {ECO:0000244|PDB:4UXU}.
STRAND 76 93 {ECO:0000244|PDB:4UXU}.
HELIX 96 98 {ECO:0000244|PDB:4UXU}.
TURN 99 101 {ECO:0000244|PDB:4UXU}.
STRAND 104 108 {ECO:0000244|PDB:4UXU}.
HELIX 109 111 {ECO:0000244|PDB:4UXU}.
STRAND 117 119 {ECO:0000244|PDB:4UXU}.
STRAND 134 138 {ECO:0000244|PDB:4UXU}.
STRAND 140 154 {ECO:0000244|PDB:4UXU}.
STRAND 156 158 {ECO:0000244|PDB:4UXU}.
STRAND 164 177 {ECO:0000244|PDB:4UXU}.
TURN 180 182 {ECO:0000244|PDB:4UXU}.
STRAND 183 191 {ECO:0000244|PDB:4UXU}.
STRAND 201 207 {ECO:0000244|PDB:4UXU}.
STRAND 209 217 {ECO:0000244|PDB:4UXU}.
TURN 218 220 {ECO:0000244|PDB:4UXU}.
STRAND 224 235 {ECO:0000244|PDB:4UXU}.
SEQUENCE 479 AA; 54807 MW; AA6B46B559D6111D CRC64;
MNWSHSCISF CWIYFAASRL RAAETADGKY AQKLFNDLFE DYSNALRPVE DTDKVLNVTL
QITLSQIKDM DERNQILTAY LWIRQIWHDA YLTWDRDQYD GLDSIRIPSD LVWRPDIVLY
NKADDESSEP VNTNVVLRYD GLITWDAPAI TKSSCVVDVT YFPFDNQQCN LTFGSWTYNG
NQVDIFNALD SGDLSDFIED VEWEVHGMPA VKNVISYGCC SEPYPDVTFT LLLKRRSSFY
IVNLLIPCVL ISFLAPLSFY LPAASGEKVS LGVTILLAMT VFQLMVAEIM PASENVPLIG
KYYIATMALI TASTALTIMV MNIHFCGAEA RPVPHWARVV ILKYMSRVLF VYDVGESCLS
PHHSRERDHL TKVYSKLPES NLKAARNKDL SRKKDMNKRL KNDLGCQGKN PQEAESYCAQ
YKVLTRNIEY IAKCLKDHKA TNSKGSEWKK VAKVIDRFFM WIFFIMVFVM TILIIARAD


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