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Protein

Muscarinic acetylcholine receptor M1

Gene

Chrm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.

GO - Molecular functioni

  1. drug binding Source: Ensembl
  2. G-protein coupled acetylcholine receptor activity Source: Ensembl

GO - Biological processi

  1. cognition Source: InterPro
  2. neuromuscular synaptic transmission Source: Ensembl
  3. positive regulation of intracellular protein transport Source: Ensembl
  4. positive regulation of ion transport Source: MGI
  5. regulation of locomotion Source: MGI
  6. saliva secretion Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_240390. Muscarinic acetylcholine receptors.

Protein family/group databases

TCDBi9.A.14.3.2. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Muscarinic acetylcholine receptor M1
Gene namesi
Name:Chrm1
Synonyms:Chrm-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:88396. Chrm1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424ExtracellularSequence AnalysisAdd
BLAST
Transmembranei25 – 4723Helical; Name=1By similarityAdd
BLAST
Topological domaini48 – 6114CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei62 – 8221Helical; Name=2By similarityAdd
BLAST
Topological domaini83 – 9917ExtracellularSequence AnalysisAdd
BLAST
Transmembranei100 – 12122Helical; Name=3By similarityAdd
BLAST
Topological domaini122 – 14120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei142 – 16423Helical; Name=4By similarityAdd
BLAST
Topological domaini165 – 18622ExtracellularSequence AnalysisAdd
BLAST
Transmembranei187 – 20923Helical; Name=5By similarityAdd
BLAST
Topological domaini210 – 366157CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei367 – 38721Helical; Name=6By similarityAdd
BLAST
Topological domaini388 – 40114ExtracellularSequence AnalysisAdd
BLAST
Transmembranei402 – 42120Helical; Name=7By similarityAdd
BLAST
Topological domaini422 – 46039CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. asymmetric synapse Source: Ensembl
  2. axon terminus Source: Ensembl
  3. cell junction Source: UniProtKB-KW
  4. dendrite Source: Ensembl
  5. integral component of plasma membrane Source: InterPro
  6. postsynaptic density Source: Ensembl
  7. postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Muscarinic acetylcholine receptor M1PRO_0000069017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi2 – 21N-linked (GlcNAc...)Curated
Glycosylationi12 – 121N-linked (GlcNAc...)Curated
Disulfide bondi98 ↔ 178PROSITE-ProRule annotation
Modified residuei451 – 4511PhosphoserineSequence Analysis
Modified residuei455 – 4551PhosphothreonineSequence Analysis
Modified residuei457 – 4571PhosphoserineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP12657.
PRIDEiP12657.

PTM databases

PhosphoSiteiP12657.

Expressioni

Gene expression databases

CleanExiMM_CHRM1.
ExpressionAtlasiP12657. baseline and differential.
GenevestigatoriP12657.

Interactioni

Subunit structurei

Interacts with GPRASP2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP12657.
SMRiP12657. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG250863.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP12657.
KOiK04129.
OMAiRCCRTPR.
PhylomeDBiP12657.
TreeFamiTF320495.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002228. Musac_Ach_M1_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF216. PTHR24249:SF216. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00538. MUSCRINICM1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12657-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTSVPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF
60 70 80 90 100
KVNTELKTVN NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL
110 120 130 140 150
WLALDYVASN ASVMNLLLIS FDRYFSVTRP LSYRAKRTPR RAALMIGLAW
160 170 180 190 200
LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI QFLSQPIITF GTAMAAFYLP
210 220 230 240 250
VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS SERSQPGAEG
260 270 280 290 300
SPESPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
310 320 330 340 350
VIKMPMVDPE AQAPTKQPPK SSPNTVKRPT KKGRDRGGKG QKPRGKEQLA
360 370 380 390 400
KRKTFSLVKE KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW
410 420 430 440 450
ELGYWLCYVN STVNPMCYAL CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG
460
SVHRTPSRQC
Length:460
Mass (Da):51,379
Last modified:October 3, 2012 - v2
Checksum:i2F6A93DE8FF4F325
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301I → S in AAA37158 (PubMed:2848036).Curated
Sequence conflicti50 – 501F → I in AAA37158 (PubMed:2848036).Curated
Sequence conflicti420 – 4201L → S in AAA37158 (PubMed:2848036).Curated
Sequence conflicti428 – 4281T → H in AAA37158 (PubMed:2848036).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29539.1.
PIRiA31897.
RefSeqiNP_001106167.1. NM_001112697.1.
NP_031724.2. NM_007698.3.
UniGeneiMm.240607.

Genome annotation databases

EnsembliENSMUST00000035444; ENSMUSP00000042632; ENSMUSG00000032773.
ENSMUST00000163785; ENSMUSP00000126103; ENSMUSG00000032773.
GeneIDi12669.
KEGGimmu:12669.
UCSCiuc008gmf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29539.1.
PIRiA31897.
RefSeqiNP_001106167.1. NM_001112697.1.
NP_031724.2. NM_007698.3.
UniGeneiMm.240607.

3D structure databases

ProteinModelPortaliP12657.
SMRiP12657. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP12657.
ChEMBLiCHEMBL2097162.
GuidetoPHARMACOLOGYi13.

Protein family/group databases

TCDBi9.A.14.3.2. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

PhosphoSiteiP12657.

Proteomic databases

PaxDbiP12657.
PRIDEiP12657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035444; ENSMUSP00000042632; ENSMUSG00000032773.
ENSMUST00000163785; ENSMUSP00000126103; ENSMUSG00000032773.
GeneIDi12669.
KEGGimmu:12669.
UCSCiuc008gmf.2. mouse.

Organism-specific databases

CTDi1128.
MGIiMGI:88396. Chrm1.

Phylogenomic databases

eggNOGiNOG250863.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP12657.
KOiK04129.
OMAiRCCRTPR.
PhylomeDBiP12657.
TreeFamiTF320495.

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_240390. Muscarinic acetylcholine receptors.

Miscellaneous databases

NextBioi281906.
PROiP12657.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CHRM1.
ExpressionAtlasiP12657. baseline and differential.
GenevestigatoriP12657.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002228. Musac_Ach_M1_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF216. PTHR24249:SF216. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00538. MUSCRINICM1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiACM1_MOUSE
AccessioniPrimary (citable) accession number: P12657
Secondary accession number(s): Q52KQ0, Q8BJN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 3, 2012
Last modified: March 4, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.