P32297 (ACHA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuronal acetylcholine receptor subunit alpha-3

Gene names

Name:	CHRNA3
Synonyms:	NACHRA3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Ref.12
Subcellular location	Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Polymorphism	Genetic variations in CHRNA3 have been associated with susceptibility to smoking-related behavioral traits and lung cancer, contributing to the smoking quantitative trait locus 3 (SQTL3) [MIM:612052].
Sequence similarities	Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of transmembrane receptor protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB behavioral response to nicotine Inferred from mutant phenotype PubMed 18227835. Source: UniProtKB locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB regulation of acetylcholine secretion Inferred from sequence or structural similarity. Source: UniProtKB regulation of dendrite morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of excitatory postsynaptic membrane potential Inferred from sequence or structural similarity. Source: UniProtKB regulation of smooth muscle contraction Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission involved in micturition Inferred from mutant phenotype Ref.6. Source: UniProtKB synaptic transmission, cholinergic Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	acetylcholine-gated channel complex Inferred from direct assay Ref.3. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW neuronal cell body Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic density Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylcholine binding Inferred by curator Ref.3. Source: UniProtKB acetylcholine receptor activity Inferred from direct assay Ref.3. Source: UniProtKB acetylcholine-activated cation-selective channel activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: P32297-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: P32297-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MGSGPL → MALAV

Isoform 3 (identifier: P32297-3)

The sequence of this isoform differs from the canonical sequence as follows:
     464-505: IQDDWKYVAMVIDRIFLWVFTLVCILGTAGLFLQPLMAREDA → EQKAQEIQQLKRKEKSTETSDQEPGL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 505	474	Neuronal acetylcholine receptor subunit alpha-3		PRO_0000000346
Regions
	Topological domain	32 – 240	209	Extracellular Potential
	Transmembrane	241 – 265	25	Helical; Potential
	Transmembrane	273 – 291	19	Helical; Potential
	Transmembrane	307 – 328	22	Helical; Potential
	Topological domain	329 – 477	149	Cytoplasmic Potential
	Transmembrane	478 – 497	20	Helical; Potential
Amino acid modifications
	Glycosylation	55	1	N-linked (GlcNAc...) Potential
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Disulfide bond	159 ↔ 173		By similarity
	Disulfide bond	223 ↔ 224		Associated with receptor activation By similarity
Natural variations
	Alternative sequence	1 – 6	6	MGSGPL → MALAV in isoform 1.		VSP_037750
	Alternative sequence	464 – 505	42	IQDDW…AREDA → EQKAQEIQQLKRKEKSTETS DQEPGL in isoform 3.		VSP_037751
	Natural variant	23	1	Missing. Ref.3 Ref.4 Ref.5 Ref.9		VAR_013240
	Natural variant	37	1	R → H. Corresponds to variant rs8192475 [ dbSNP | Ensembl ].		VAR_059110
Experimental info
	Sequence conflict	5 – 14	10	PLSLPLALSP → ALAAPGAVA in AAA59942. Ref.2
	Sequence conflict	12 – 15	4	LSPP → CRA in AAC84176. Ref.1
	Sequence conflict	102	1	D → G in AAC84176. Ref.1
	Sequence conflict	134 – 135	2	DD → TT in AAC84176. Ref.1
	Sequence conflict	237	1	I → S in AAC84176. Ref.1
	Sequence conflict	432	1	L → V in AAC84176. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified July 28, 2009. Version 4. Checksum: 478D7712D59ACB2D	FASTA	505	57,480
	10 20 30 40 50 60 MGSGPLSLPL ALSPPRLLLL LLLSLLPVAR ASEAEHRLFE RLFEDYNEII RPVANVSDPV 70 80 90 100 110 120 IIHFEVSMSQ LVKVDEVNQI METNLWLKQI WNDYKLKWNP SDYGGAEFMR VPAQKIWKPD 130 140 150 160 170 180 IVLYNNAVGD FQVDDKTKAL LKYTGEVTWI PPAIFKSSCK IDVTYFPFDY QNCTMKFGSW 190 200 210 220 230 240 SYDKAKIDLV LIGSSMNLKD YWESGEWAII KAPGYKHDIK YNCCEEIYPD ITYSLYIRRL 250 260 270 280 290 300 PLFYTINLII PCLLISFLTV LVFYLPSDCG EKVTLCISVL LSLTVFLLVI TETIPSTSLV 310 320 330 340 350 360 IPLIGEYLLF TMIFVTLSIV ITVFVLNVHY RTPTTHTMPS WVKTVFLNLL PRVMFMTRPT 370 380 390 400 410 420 SNEGNAQKPR PLYGAELSNL NCFSRAESKG CKEGYPCQDG MCGYCHHRRI KISNFSANLT 430 440 450 460 470 480 RSSSSESVDA VLSLSALSPE IKEAIQSVKY IAENMKAQNE AKEIQDDWKY VAMVIDRIFL 490 500 WVFTLVCILG TAGLFLQPLM AREDA
	Isoform 1 [UniParc]. Checksum: F4D2DA153F2B3476	FASTA	504	57,423
	10 20 30 40 50 60 MALAVSLPLA LSPPRLLLLL LLSLLPVARA SEAEHRLFER LFEDYNEIIR PVANVSDPVI 70 80 90 100 110 120 IHFEVSMSQL VKVDEVNQIM ETNLWLKQIW NDYKLKWNPS DYGGAEFMRV PAQKIWKPDI 130 140 150 160 170 180 VLYNNAVGDF QVDDKTKALL KYTGEVTWIP PAIFKSSCKI DVTYFPFDYQ NCTMKFGSWS 190 200 210 220 230 240 YDKAKIDLVL IGSSMNLKDY WESGEWAIIK APGYKHDIKY NCCEEIYPDI TYSLYIRRLP 250 260 270 280 290 300 LFYTINLIIP CLLISFLTVL VFYLPSDCGE KVTLCISVLL SLTVFLLVIT ETIPSTSLVI 310 320 330 340 350 360 PLIGEYLLFT MIFVTLSIVI TVFVLNVHYR TPTTHTMPSW VKTVFLNLLP RVMFMTRPTS 370 380 390 400 410 420 NEGNAQKPRP LYGAELSNLN CFSRAESKGC KEGYPCQDGM CGYCHHRRIK ISNFSANLTR 430 440 450 460 470 480 SSSSESVDAV LSLSALSPEI KEAIQSVKYI AENMKAQNEA KEIQDDWKYV AMVIDRIFLW 490 500 VFTLVCILGT AGLFLQPLMA REDA
	Isoform 3 [UniParc]. Checksum: F8C4F79BDC30A44E	FASTA	489	55,637
	10 20 30 40 50 60 MGSGPLSLPL ALSPPRLLLL LLLSLLPVAR ASEAEHRLFE RLFEDYNEII RPVANVSDPV 70 80 90 100 110 120 IIHFEVSMSQ LVKVDEVNQI METNLWLKQI WNDYKLKWNP SDYGGAEFMR VPAQKIWKPD 130 140 150 160 170 180 IVLYNNAVGD FQVDDKTKAL LKYTGEVTWI PPAIFKSSCK IDVTYFPFDY QNCTMKFGSW 190 200 210 220 230 240 SYDKAKIDLV LIGSSMNLKD YWESGEWAII KAPGYKHDIK YNCCEEIYPD ITYSLYIRRL 250 260 270 280 290 300 PLFYTINLII PCLLISFLTV LVFYLPSDCG EKVTLCISVL LSLTVFLLVI TETIPSTSLV 310 320 330 340 350 360 IPLIGEYLLF TMIFVTLSIV ITVFVLNVHY RTPTTHTMPS WVKTVFLNLL PRVMFMTRPT 370 380 390 400 410 420 SNEGNAQKPR PLYGAELSNL NCFSRAESKG CKEGYPCQDG MCGYCHHRRI KISNFSANLT 430 440 450 460 470 480 RSSSSESVDA VLSLSALSPE IKEAIQSVKY IAENMKAQNE AKEEQKAQEI QQLKRKEKST ETSDQEPGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit." Fornasari D., Chini B., Tarroni P., Clementi F. Neurosci. Lett. 111:351-356(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Expression of mRNAs in human thymus coding for the alpha 3 subunit of a neuronal acetylcholine receptor." Mihovilovic M., Roses A.D. Exp. Neurol. 111:175-180(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Thymus.
[3]	"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." Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E., Johnson E.C., Velicelebi G., Harpold M.M. J. Mol. Neurosci. 7:217-228(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-23 DEL.
[4]	"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." Groot Kormelink P.J., Luyten W.H.M.L. FEBS Lett. 400:309-314(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-23 DEL.
[5]	"The structures of the human neuronal nicotinic acetylcholine receptor beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3)." Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K. Hum. Genet. 103:645-653(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT LEU-23 DEL.
[6]	"Characterization of the human beta4 nAChR gene and polymorphisms in CHRNA3 and CHRNB4." Lev-Lehman E., Bercovich D., Xu W., Stockton D.W., Beaudet A.L. J. Hum. Genet. 46:362-366(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
[8]	"Analysis of the DNA sequence and duplication history of human chromosome 15." 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. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT LEU-23 DEL. Tissue: Brain and Lung.
[10]	"Cloning cholinergic receptors in human keratinocytes." Arredondo J., Grando S.A. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-495 (ISOFORMS 1/2). Tissue: Keratinocyte.
[11]	Anand R., Lindstrom J. Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-505 (ISOFORMS 1/2). Tissue: Brain.
[12]	"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells." Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S. Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIC3.
[13]	"Genomics: when the smoke clears." Chanock S.J., Hunter D.J. Nature 452:537-538(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[14]	"A susceptibility locus for lung cancer maps to nicotinic acetylcholine receptor subunit genes on 15q25." Hung R.J., McKay J.D., Gaborieau V., Boffetta P., Hashibe M., Zaridze D., Mukeria A., Szeszenia-Dabrowska N., Lissowska J., Rudnai P., Fabianova E., Mates D., Bencko V., Foretova L., Janout V., Chen C., Goodman G., Field J.K. , Liloglou T., Xinarianos G., Cassidy A., McLaughlin J., Liu G., Narod S., Krokan H.E., Skorpen F., Elvestad M.B., Hveem K., Vatten L., Linseisen J., Clavel-Chapelon F., Vineis P., Bueno-de-Mesquita H.B., Lund E., Martinez C., Bingham S., Rasmuson T., Hainaut P., Riboli E., Ahrens W., Benhamou S., Lagiou P., Trichopoulos D., Holcatova I., Merletti F., Kjaerheim K., Agudo A., Macfarlane G., Talamini R., Simonato L., Lowry R., Conway D.I., Znaor A., Healy C., Zelenika D., Boland A., Delepine M., Foglio M., Lechner D., Matsuda F., Blanche H., Gut I., Heath S., Lathrop M., Brennan P. Nature 452:633-637(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[15]	"A variant associated with nicotine dependence, lung cancer and peripheral arterial disease." Thorgeirsson T.E., Geller F., Sulem P., Rafnar T., Wiste A., Magnusson K.P., Manolescu A., Thorleifsson G., Stefansson H., Ingason A., Stacey S.N., Bergthorsson J.T., Thorlacius S., Gudmundsson J., Jonsson T., Jakobsdottir M., Saemundsdottir J., Olafsdottir O. , Gudmundsson L.J., Bjornsdottir G., Kristjansson K., Skuladottir H., Isaksson H.J., Gudbjartsson T., Jones G.T., Mueller T., Gottsaeter A., Flex A., Aben K.K.H., de Vegt F., Mulders P.F.A., Isla D., Vidal M.J., Asin L., Saez B., Murillo L., Blondal T., Kolbeinsson H., Stefansson J.G., Hansdottir I., Runarsdottir V., Pola R., Lindblad B., van Rij A.M., Dieplinger B., Haltmayer M., Mayordomo J.I., Kiemeney L.A., Matthiasson S.E., Oskarsson H., Tyrfingsson T., Gudbjartsson D.F., Gulcher J.R., Jonsson S., Thorsteinsdottir U., Kong A., Stefansson K. Nature 452:638-642(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[16]	"Genome-wide association scan of tag SNPs identifies a susceptibility locus for lung cancer at 15q25.1." Amos C.I., Wu X., Broderick P., Gorlov I.P., Gu J., Eisen T., Dong Q., Zhang Q., Gu X., Vijayakrishnan J., Sullivan K., Matakidou A., Wang Y., Mills G., Doheny K., Tsai Y.-Y., Chen W.V., Shete S., Spitz M.R., Houlston R.S. Nat. Genet. 40:616-622(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M86383 mRNA. Translation: AAC84176.1. M37981 mRNA. Translation: AAA59942.1. U62432 mRNA. Translation: AAB40110.1. Y08418 mRNA. Translation: CAA69695.1. AJ007783 , AJ007784, AJ007785, AJ007786, AJ007787 Genomic DNA. Translation: CAA07682.1. BT006646 mRNA. Translation: AAP35292.1. BT006897 mRNA. Translation: AAP35543.1. AC027228 Genomic DNA. No translation available. AC067863 Genomic DNA. No translation available. BC000513 mRNA. Translation: AAH00513.1. BC001642 mRNA. Translation: AAH01642.1. BC002996 mRNA. Translation: AAH02996.1. BC006114 mRNA. Translation: AAH06114.1. BC098443 mRNA. Translation: AAH98443.1. AF385584 mRNA. Translation: AAK68110.1. X53559 mRNA. Translation: CAA37625.1.
IPI	IPI00297165. IPI00852613. IPI00939562.
PIR	A37040. A53956.
RefSeq	NP_000734.2. NM_000743.4. NP_001160166.1. NM_001166694.1.
UniGene	Hs.89605.
3D structure databases
ProteinModelPortal	P32297.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000315602.
PTM databases
PhosphoSite	P32297.
Polymorphism databases
DMDM	254763435.
Proteomic databases
PaxDb	P32297.
PRIDE	P32297.
Protocols and materials databases
DNASU	1136.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326828; ENSP00000315602; ENSG00000080644. ENST00000348639; ENSP00000267951; ENSG00000080644. ENST00000559658; ENSP00000452896; ENSG00000080644.
GeneID	1136.
KEGG	hsa:1136.
UCSC	uc002beb.3. human. uc002bec.3. human.
Organism-specific databases
CTD	1136.
GeneCards	GC15M078885.
H-InvDB	HIX0017542.
HGNC	HGNC:1957. CHRNA3.
HPA	HPA029430.
MIM	118503. gene. 612052. phenotype.
neXtProt	NX_P32297.
PharmGKB	PA113.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG290206.
HOVERGEN	HBG003756.
InParanoid	P32297.
KO	K04805.
OMA	SKGCKEG.
PhylomeDB	P32297.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	P32297.
Bgee	P32297.
CleanEx	HS_CHRNA3.
Genevestigator	P32297.
GermOnline	ENSG00000080644. Homo sapiens.
Family and domain databases
Gene3D	2.70.170.10. 1 hit.
InterPro	IPR006202. Neur_chan_lig-bd. IPR006201. Neur_channel. IPR006029. Neurotrans-gated_channel_TM. IPR018000. Neurotransmitter_ion_chnl_CS. IPR002394. Nicotinic_acetylcholine_rcpt. [Graphical view]
PANTHER	PTHR18945. PTHR18945. 1 hit.
Pfam	PF02931. Neur_chan_LBD. 1 hit. PF02932. Neur_chan_memb. 1 hit. [Graphical view]
PRINTS	PR00254. NICOTINICR. PR00252. NRIONCHANNEL.
SUPFAM	SSF90112. Neu_channel_TM. 1 hit. SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMs	TIGR00860. LIC. 1 hit.
PROSITE	PS00236. NEUROTR_ION_CHANNEL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P32297.
ChEMBL	CHEMBL3068.
ChiTaRS	CHRNA3. human.
GenomeRNAi	1136.
NextBio	4726.
SOURCE	Search...

Entry information

Entry name

ACHA3_HUMAN

Accession

Primary (citable) accession number: P32297
Secondary accession number(s): Q15823 , Q4KMN8, Q86U77, Q96RH3, Q99553, Q9BQ93, Q9BRR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.