P12657 (ACM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Muscarinic acetylcholine receptor M1

Gene names

Name:	Chrm1
Synonyms:	Chrm-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subunit structure	Interacts with GPRASP2 By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	neuromuscular synaptic transmission Inferred from electronic annotation. Source: Compara positive regulation of ion transport Inferred from sequence orthology PubMed 14657398. Source: MGI regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: InterPro regulation of locomotion Inferred from mutant phenotype PubMed 11752469. Source: MGI regulation of phospholipase C activity Inferred from electronic annotation. Source: InterPro
Cellular_component	asymmetric synapse Inferred from electronic annotation. Source: Compara axon terminus Inferred from electronic annotation. Source: Compara cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Inferred from electronic annotation. Source: InterPro postsynaptic density Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein coupled acetylcholine receptor activity Inferred from electronic annotation. Source: Compara drug binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 460	460	Muscarinic acetylcholine receptor M1		PRO_0000069017
Regions
	Topological domain	1 – 24	24	Extracellular Potential
	Transmembrane	25 – 47	23	Helical; Name=1; By similarity
	Topological domain	48 – 61	14	Cytoplasmic Potential
	Transmembrane	62 – 82	21	Helical; Name=2; By similarity
	Topological domain	83 – 99	17	Extracellular Potential
	Transmembrane	100 – 121	22	Helical; Name=3; By similarity
	Topological domain	122 – 141	20	Cytoplasmic Potential
	Transmembrane	142 – 164	23	Helical; Name=4; By similarity
	Topological domain	165 – 186	22	Extracellular Potential
	Transmembrane	187 – 209	23	Helical; Name=5; By similarity
	Topological domain	210 – 366	157	Cytoplasmic Potential
	Transmembrane	367 – 387	21	Helical; Name=6; By similarity
	Topological domain	388 – 401	14	Extracellular Potential
	Transmembrane	402 – 421	20	Helical; Name=7; By similarity
	Topological domain	422 – 460	39	Cytoplasmic Potential
Amino acid modifications
	Modified residue	451	1	Phosphoserine Potential
	Modified residue	455	1	Phosphothreonine Potential
	Modified residue	457	1	Phosphoserine Potential
	Glycosylation	2	1	N-linked (GlcNAc...) Probable
	Glycosylation	12	1	N-linked (GlcNAc...) Probable
	Disulfide bond	98 ↔ 178		By similarity
Experimental info
	Sequence conflict	30	1	I → S in AAA37158. Ref.1
	Sequence conflict	50	1	F → I in AAA37158. Ref.1
	Sequence conflict	420	1	L → S in AAA37158. Ref.1
	Sequence conflict	428	1	T → H in AAA37158. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P12657 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 2F6A93DE8FF4F325	FASTA	460	51,379
	10 20 30 40 50 60 MNTSVPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN 70 80 90 100 110 120 NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS 130 140 150 160 170 180 FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI 190 200 210 220 230 240 QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS 250 260 270 280 290 300 SERSQPGAEG SPESPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV 310 320 330 340 350 360 VIKMPMVDPE AQAPTKQPPK SSPNTVKRPT KKGRDRGGKG QKPRGKEQLA KRKTFSLVKE 370 380 390 400 410 420 KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STVNPMCYAL 430 440 450 460 CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, sequence, and functional expression of the mouse M1 muscarinic acetylcholine receptor gene." Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M., Nathanson N.M. J. Biol. Chem. 263:18397-18403(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Erratum Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M., Nathanson N.M. J. Biol. Chem. 264:6596-6596(1989)
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Corpus striatum and Hypothalamus.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04192 Genomic DNA. Translation: AAA37158.1. AK081248 mRNA. Translation: BAC38175.1. AK138282 mRNA. Translation: BAE23612.1. AC025794 Genomic DNA. No translation available. CH466612 Genomic DNA. Translation: EDL33348.1. CH466612 Genomic DNA. Translation: EDL33349.1. BC094242 mRNA. Translation: AAH94242.1.
IPI	IPI00119416.
PIR	A31897.
RefSeq	NP_001106167.1. NM_001112697.1. NP_031724.2. NM_007698.3.
UniGene	Mm.240607.
3D structure databases
ProteinModelPortal	P12657.
SMR	P12657. Positions 23-216, 362-430.
ModBase	Search...
Protein family/group databases
TCDB	9.A.40.3.3. HlyC/CorC (HCC) family.
GPCRDB	Search...
PTM databases
PhosphoSite	P12657.
Proteomic databases
PaxDb	P12657.
PRIDE	P12657.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035444; ENSMUSP00000042632; ENSMUSG00000032773. ENSMUST00000163785; ENSMUSP00000126103; ENSMUSG00000032773.
GeneID	12669.
KEGG	mmu:12669.
UCSC	uc008gmf.2. mouse.
Organism-specific databases
CTD	1128.
MGI	MGI:88396. Chrm1.
Phylogenomic databases
eggNOG	NOG250863.
GeneTree	ENSGT00690000101881.
HOGENOM	HOG000231484.
HOVERGEN	HBG105720.
InParanoid	P12657.
KO	K04129.
OMA	RCCRTPR.
OrthoDB	EOG4NVZK1.
Gene expression databases
CleanEx	MM_CHRM1.
Genevestigator	P12657.
GermOnline	ENSMUSG00000032773. Mus musculus.
Family and domain databases
InterPro	IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR002228. Musac_Ach_M1_rcpt. IPR000995. Musac_Ach_rcpt. [Graphical view]
PANTHER	PTHR24249:SF59. PTHR24249:SF59. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00243. MUSCARINICR. PR00538. MUSCRINICM1R.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P12657.
ChEMBL	CHEMBL3733.
NextBio	281906.
SOURCE	Search...

Entry information

Entry name

ACM1_MOUSE

Accession

Primary (citable) accession number: P12657
Secondary accession number(s): Q52KQ0, Q8BJN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 3, 2012
Last modified:	May 29, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program