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Protein

Muscarinic acetylcholine receptor

Gene

CHRM1

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptorUniRule annotation, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
Muscarinic acetylcholine receptorUniRule annotation
Gene namesi
Name:CHRM1Imported
ORF Names:hCG_2020133Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
  • Cell junctionsynapsepostsynaptic cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei25 – 5026HelicalUniRule annotationAdd
BLAST
Transmembranei62 – 8827HelicalUniRule annotationAdd
BLAST
Transmembranei100 – 12122HelicalUniRule annotationAdd
BLAST
Transmembranei142 – 16726HelicalUniRule annotationAdd
BLAST
Transmembranei187 – 20923HelicalUniRule annotationAdd
BLAST
Transmembranei369 – 39022HelicalUniRule annotationAdd
BLAST
Transmembranei402 – 42120HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membraneUniRule annotation, Membrane, Postsynaptic cell membraneUniRule annotation, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26484.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000306490.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 418377G_PROTEIN_RECEP_F1_2InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

eggNOGiKOG4220. Eukaryota.
ENOG410YCQR. LUCA.
GeneTreeiENSGT00780000121874.
HOVERGENiHBG105720.
KOiK04129.
OMAiRCCRTPR.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002228. Musac_Ach_M1_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
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.

Q53XZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTSAPPAVS 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
SPETPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
310 320 330 340 350
VIKMPMVDPE AQAPTKQPPR SSPNTVKRPT KKGRDRAGKG QKPRGKEQLA
360 370 380 390 400
KRKTFSLVKE KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW
410 420 430 440 450
ELGYWLCYVN STINPMCYAL CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG
460
SVHRTPSRQC
Length:460
Mass (Da):51,421
Last modified:May 24, 2005 - v1
Checksum:i567C20F63541C8D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007166 mRNA. Translation: AAP35830.1.
AK312374 mRNA. Translation: BAG35292.1.
CH471076 Genomic DNA. Translation: EAW74124.1.
CH471076 Genomic DNA. Translation: EAW74125.1.
CH471076 Genomic DNA. Translation: EAW74126.1.
RefSeqiNP_000729.2. NM_000738.2.
XP_011543044.1. XM_011544742.1.
UniGeneiHs.632119.

Genome annotation databases

GeneIDi1128.
KEGGihsa:1128.
UCSCiuc001nwi.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT007166 mRNA. Translation: AAP35830.1.
AK312374 mRNA. Translation: BAG35292.1.
CH471076 Genomic DNA. Translation: EAW74124.1.
CH471076 Genomic DNA. Translation: EAW74125.1.
CH471076 Genomic DNA. Translation: EAW74126.1.
RefSeqiNP_000729.2. NM_000738.2.
XP_011543044.1. XM_011544742.1.
UniGeneiHs.632119.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000306490.

Protein family/group databases

GPCRDBiSearch...

Protocols and materials databases

DNASUi1128.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1128.
KEGGihsa:1128.
UCSCiuc001nwi.4. human.

Organism-specific databases

CTDi1128.
PharmGKBiPA26484.

Phylogenomic databases

eggNOGiKOG4220. Eukaryota.
ENOG410YCQR. LUCA.
GeneTreeiENSGT00780000121874.
HOVERGENiHBG105720.
KOiK04129.
OMAiRCCRTPR.

Miscellaneous databases

GenomeRNAii1128.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR002228. Musac_Ach_M1_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
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. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE.
  4. "NEDO functional analysis of protein and research application project."
    Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: AmygdalaImported.

Entry informationi

Entry nameiQ53XZ3_HUMAN
AccessioniPrimary (citable) accession number: Q53XZ3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny 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.

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 one 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.