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P12657 (ACM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Muscarinic acetylcholine receptor M1
Gene names
Name:Chrm1
Synonyms:Chrm-1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Muscarinic acetylcholine receptor M1
PRO_0000069017

Regions

Topological domain1 – 2424Extracellular Potential
Transmembrane25 – 4723Helical; Name=1; By similarity
Topological domain48 – 6114Cytoplasmic Potential
Transmembrane62 – 8221Helical; Name=2; By similarity
Topological domain83 – 9917Extracellular Potential
Transmembrane100 – 12122Helical; Name=3; By similarity
Topological domain122 – 14120Cytoplasmic Potential
Transmembrane142 – 16423Helical; Name=4; By similarity
Topological domain165 – 18622Extracellular Potential
Transmembrane187 – 20923Helical; Name=5; By similarity
Topological domain210 – 366157Cytoplasmic Potential
Transmembrane367 – 38721Helical; Name=6; By similarity
Topological domain388 – 40114Extracellular Potential
Transmembrane402 – 42120Helical; Name=7; By similarity
Topological domain422 – 46039Cytoplasmic Potential

Amino acid modifications

Modified residue4281Phosphohistidine Potential
Modified residue4511Phosphoserine Potential
Modified residue4551Phosphothreonine Potential
Modified residue4571Phosphoserine Potential
Glycosylation21N-linked (GlcNAc...) Probable
Glycosylation121N-linked (GlcNAc...) Probable
Disulfide bond98 ↔ 178 By similarity

Experimental info

Sequence conflict301S → I in BAC38175. Ref.3
Sequence conflict501I → F in BAC38175. Ref.3
Sequence conflict4201S → L in BAC38175. Ref.3
Sequence conflict4281H → T in BAC38175. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P12657 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 121A625C50BE3993

FASTA46051,329
        10         20         30         40         50         60 
MNTSVPPAVS PNITVLAPGK GPWQVAFIGS TTGLLSLATV TGNLLVLISI 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 STVNPMCYAS 

       430        440        450        460 
CNKAFRDHFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC

« Hide

References

« Hide '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: 2848036] [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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Corpus striatum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04192 Genomic DNA. Translation: AAA37158.1.
AK081248 mRNA. Translation: BAC38175.1.
IPIIPI00119416.
PIRA31897.
RefSeqNP_001106167.1. NM_001112697.1.
NP_031724.2. NM_007698.3.
UniGeneMm.240607.

3D structure databases

ProteinModelPortalP12657.
SMRP12657. Positions 27-435.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12657.

Protein family/group databases

TCDB9.A.40.3.3. HlyC/CorC (HCC) family.
GPCRDBSearch...

PTM databases

PhosphoSiteP12657.

Proteomic databases

PRIDEP12657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12669.
KEGGmmu:12669.

Organism-specific databases

CTD1128.
MGIMGI:88396. Chrm1.

Phylogenomic databases

eggNOGroNOG04436.
HOGENOMHBG713567.
HOVERGENHBG105720.
InParanoidP12657.
OrthoDBEOG4NVZK1.

Gene expression databases

ArrayExpressP12657.
BgeeP12657.
CleanExMM_CHRM1.
GenevestigatorP12657.
GermOnlineENSMUSG00000032773. Mus musculus.

Family and domain databases

InterProIPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
IPR002228. Musac_M1_rcpt.
IPR000995. Musac_rcpt.
[Graphical view]
KOK04129.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00538. MUSCRINICM1R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameACM1_MOUSE
AccessionPrimary (citable) accession number: P12657
Secondary accession number(s): Q8BJN3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents