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Protein

Muscarinic acetylcholine receptor M3

Gene

CHRM3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

GO - Molecular functioni

  • acetylcholine binding Source: UniProtKB
  • drug binding Source: Ensembl
  • G-protein coupled acetylcholine receptor activity Source: UniProtKB
  • phosphatidylinositol phospholipase C activity Source: ProtInc
  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_16943. Muscarinic acetylcholine receptors.
REACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
SignaLinkiP20309.

Names & Taxonomyi

Protein namesi
Recommended name:
Muscarinic acetylcholine receptor M3
Gene namesi
Name:CHRM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1952. CHRM3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6767ExtracellularBy similarityAdd
BLAST
Transmembranei68 – 9124Helical; Name=1By similarityAdd
BLAST
Topological domaini92 – 10413CytoplasmicBy similarityAdd
BLAST
Transmembranei105 – 13026Helical; Name=2By similarityAdd
BLAST
Topological domaini131 – 14212ExtracellularBy similarityAdd
BLAST
Transmembranei143 – 16422Helical; Name=3By similarityAdd
BLAST
Topological domaini165 – 18420CytoplasmicBy similarityAdd
BLAST
Transmembranei185 – 20622Helical; Name=4By similarityAdd
BLAST
Topological domaini207 – 22923ExtracellularBy similarityAdd
BLAST
Transmembranei230 – 25223Helical; Name=5By similarityAdd
BLAST
Topological domaini253 – 491239CytoplasmicBy similarityAdd
BLAST
Transmembranei492 – 51423Helical; Name=6By similarityAdd
BLAST
Topological domaini515 – 52612ExtracellularBy similarityAdd
BLAST
Transmembranei527 – 54620Helical; Name=7By similarityAdd
BLAST
Topological domaini547 – 59044CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Eagle-Barrett syndrome (EGBRS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA syndrome characterized by thin abdominal musculature with overlying lax skin, cryptorchism, megacystis with disorganized detrusor muscle, and urinary tract abnormalities.

See also OMIM:100100

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi276 – 2761E → A: Loss of basolateral sorting. 1 Publication
Mutagenesisi276 – 2761E → D: Loss of basolateral sorting. No effect on basolateral sorting; when associated with L-280 and L-281. 1 Publication
Mutagenesisi280 – 2801F → A: Loss of basolateral sorting. 1 Publication
Mutagenesisi280 – 2801F → L: No effect on basolateral sorting. 1 Publication
Mutagenesisi281 – 2811V → A: Loss of basolateral sorting. 1 Publication
Mutagenesisi281 – 2811V → L: No effect on basolateral sorting. 1 Publication

Organism-specific databases

MIMi100100. phenotype.
Orphaneti2970. Prune belly syndrome.
PharmGKBiPA112.

Chemistry

DrugBankiDB08897. Aclidinium.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB00517. Anisotropine Methylbromide.
DB01238. Aripiprazole.
DB00572. Atropine.
DB00835. Brompheniramine.
DB00185. Cevimeline.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB00568. Cinnarizine.
DB00363. Clozapine.
DB00785. Cryptenamine.
DB00434. Cyproheptadine.
DB00496. Darifenacin.
DB01151. Desipramine.
DB00729. Diphemanil Methylsulfate.
DB01231. Diphenidol.
DB00280. Disopyramide.
DB01142. Doxepin.
DB06702. Fesoterodine.
DB00986. Glycopyrrolate.
DB00725. Homatropine Methylbromide.
DB00424. Hyoscyamine.
DB00458. Imipramine.
DB00332. Ipratropium bromide.
DB01625. Isopropamide.
DB01221. Ketamine.
DB00408. Loxapine.
DB00934. Maprotiline.
DB04843. Mepenzolate.
DB06709. Methacholine.
DB01403. Methotrimeprazine.
DB00462. Methylscopolamine bromide.
DB00340. Metixene.
DB01226. Mivacurium.
DB00622. Nicardipine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB01062. Oxybutynin.
DB00383. Oxyphencyclimine.
DB01337. Pancuronium.
DB00715. Paroxetine.
DB00454. Pethidine.
DB01085. Pilocarpine.
DB01338. Pipecuronium.
DB00387. Procyclidine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00747. Scopolamine.
DB01591. Solifenacin.
DB00202. Succinylcholine.
DB01409. Tiotropium.
DB01036. Tolterodine.
DB00193. Tramadol.
DB00376. Trihexyphenidyl.
DB00726. Trimipramine.
DB00809. Tropicamide.
DB00246. Ziprasidone.

Polymorphism and mutation databases

BioMutaiCHRM3.
DMDMi113125.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 590590Muscarinic acetylcholine receptor M3PRO_0000069029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51N-linked (GlcNAc...)Sequence Analysis
Glycosylationi6 – 61N-linked (GlcNAc...)Sequence Analysis
Glycosylationi15 – 151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi141 ↔ 221PROSITE-ProRule annotation
Disulfide bondi517 ↔ 520PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP20309.
PaxDbiP20309.
PRIDEiP20309.

PTM databases

PhosphoSiteiP20309.

Expressioni

Gene expression databases

BgeeiP20309.
CleanExiHS_CHRM3.
ExpressionAtlasiP20309. baseline and differential.
GenevestigatoriP20309.

Organism-specific databases

HPAiCAB010409.
HPA024106.

Interactioni

Subunit structurei

Homodimer; the dimers can form tetramers.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NALCNQ8IZF03EBI-2687785,EBI-7085333

Protein-protein interaction databases

BioGridi107553. 62 interactions.
DIPiDIP-44291N.
IntActiP20309. 3 interactions.
MINTiMINT-4953628.
STRINGi9606.ENSP00000255380.

Structurei

Secondary structure

1
590
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi280 – 2834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSANMR-A271-289[»]
ProteinModelPortaliP20309.
SMRiP20309. Positions 64-559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20309.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1525Agonist bindingBy similarity
Regioni507 – 53024Agonist bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi275 – 2817Basolateral sorting signal

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG250863.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP20309.
KOiK04131.
OMAiCDKKKRR.
OrthoDBiEOG7V49Z7.
PhylomeDBiP20309.
TreeFamiTF320495.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001183. Musac_Ach_M3_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF61. PTHR24249:SF61. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00540. MUSCRINICM3R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLHNNSTTS PLFPNISSSW IHSPSDAGLP PGTVTHFGSY NVSRAAGNFS
60 70 80 90 100
SPDGTTDDPL GGHTVWQVVF IAFLTGILAL VTIIGNILVI VSFKVNKQLK
110 120 130 140 150
TVNNYFLLSL ACADLIIGVI SMNLFTTYII MNRWALGNLA CDLWLAIDYV
160 170 180 190 200
ASNASVMNLL VISFDRYFSI TRPLTYRAKR TTKRAGVMIG LAWVISFVLW
210 220 230 240 250
APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF YMPVTIMTIL
260 270 280 290 300
YWRIYKETEK RTKELAGLQA SGTEAETENF VHPTGSSRSC SSYELQQQSM
310 320 330 340 350
KRSNRRKYGR CHFWFTTKSW KPSSEQMDQD HSSSDSWNNN DAAASLENSA
360 370 380 390 400
SSDEEDIGSE TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGMVD
410 420 430 440 450
LERKADKLQA QKSVDDGGSF PKSFSKLPIQ LESAVDTAKT SDVNSSVGKS
460 470 480 490 500
TATLPLSFKE ATLAKRFALK TRSQITKRKR MSLVKEKKAA QTLSAILLAF
510 520 530 540 550
IITWTPYNIM VLVNTFCDSC IPKTFWNLGY WLCYINSTVN PVCYALCNKT
560 570 580 590
FRTTFKMLLL CQCDKKKRRK QQYQQRQSVI FHKRAPEQAL
Length:590
Mass (Da):66,128
Last modified:February 1, 1991 - v1
Checksum:i5CB473C57B9526E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti382 – 3843KLP → RLS in AAG30036 (PubMed:11238933).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651V → I.
Corresponds to variant rs2067481 [ dbSNP | Ensembl ].
VAR_033461
Natural varianti431 – 4311L → P.
Corresponds to variant rs16839102 [ dbSNP | Ensembl ].
VAR_049368

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15266 Genomic DNA. Translation: CAA33337.1.
U29589 Genomic DNA. Translation: AAA70337.1.
AB041395 Genomic DNA. Translation: BAA94480.1.
AF498917 mRNA. Translation: AAM18940.1.
AL356361 Genomic DNA. Translation: CAH72987.1.
BC096844 mRNA. Translation: AAH96844.1.
BC121026 mRNA. Translation: AAI21027.1.
AF279779 mRNA. Translation: AAG30036.1.
CCDSiCCDS1616.1.
PIRiS10128.
RefSeqiNP_000731.1. NM_000740.2.
XP_005273089.1. XM_005273032.2.
XP_005273091.1. XM_005273034.2.
UniGeneiHs.155736.
Hs.7138.

Genome annotation databases

EnsembliENST00000255380; ENSP00000255380; ENSG00000133019.
ENST00000615928; ENSP00000482377; ENSG00000133019.
GeneIDi1131.
KEGGihsa:1131.
UCSCiuc001hyp.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15266 Genomic DNA. Translation: CAA33337.1.
U29589 Genomic DNA. Translation: AAA70337.1.
AB041395 Genomic DNA. Translation: BAA94480.1.
AF498917 mRNA. Translation: AAM18940.1.
AL356361 Genomic DNA. Translation: CAH72987.1.
BC096844 mRNA. Translation: AAH96844.1.
BC121026 mRNA. Translation: AAI21027.1.
AF279779 mRNA. Translation: AAG30036.1.
CCDSiCCDS1616.1.
PIRiS10128.
RefSeqiNP_000731.1. NM_000740.2.
XP_005273089.1. XM_005273032.2.
XP_005273091.1. XM_005273034.2.
UniGeneiHs.155736.
Hs.7138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSANMR-A271-289[»]
ProteinModelPortaliP20309.
SMRiP20309. Positions 64-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107553. 62 interactions.
DIPiDIP-44291N.
IntActiP20309. 3 interactions.
MINTiMINT-4953628.
STRINGi9606.ENSP00000255380.

Chemistry

BindingDBiP20309.
ChEMBLiCHEMBL245.
DrugBankiDB08897. Aclidinium.
DB00321. Amitriptyline.
DB00543. Amoxapine.
DB00517. Anisotropine Methylbromide.
DB01238. Aripiprazole.
DB00572. Atropine.
DB00835. Brompheniramine.
DB00185. Cevimeline.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB00568. Cinnarizine.
DB00363. Clozapine.
DB00785. Cryptenamine.
DB00434. Cyproheptadine.
DB00496. Darifenacin.
DB01151. Desipramine.
DB00729. Diphemanil Methylsulfate.
DB01231. Diphenidol.
DB00280. Disopyramide.
DB01142. Doxepin.
DB06702. Fesoterodine.
DB00986. Glycopyrrolate.
DB00725. Homatropine Methylbromide.
DB00424. Hyoscyamine.
DB00458. Imipramine.
DB00332. Ipratropium bromide.
DB01625. Isopropamide.
DB01221. Ketamine.
DB00408. Loxapine.
DB00934. Maprotiline.
DB04843. Mepenzolate.
DB06709. Methacholine.
DB01403. Methotrimeprazine.
DB00462. Methylscopolamine bromide.
DB00340. Metixene.
DB01226. Mivacurium.
DB00622. Nicardipine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB01062. Oxybutynin.
DB00383. Oxyphencyclimine.
DB01337. Pancuronium.
DB00715. Paroxetine.
DB00454. Pethidine.
DB01085. Pilocarpine.
DB01338. Pipecuronium.
DB00387. Procyclidine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00747. Scopolamine.
DB01591. Solifenacin.
DB00202. Succinylcholine.
DB01409. Tiotropium.
DB01036. Tolterodine.
DB00193. Tramadol.
DB00376. Trihexyphenidyl.
DB00726. Trimipramine.
DB00809. Tropicamide.
DB00246. Ziprasidone.
GuidetoPHARMACOLOGYi15.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP20309.

Polymorphism and mutation databases

BioMutaiCHRM3.
DMDMi113125.

Proteomic databases

MaxQBiP20309.
PaxDbiP20309.
PRIDEiP20309.

Protocols and materials databases

DNASUi1131.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255380; ENSP00000255380; ENSG00000133019.
ENST00000615928; ENSP00000482377; ENSG00000133019.
GeneIDi1131.
KEGGihsa:1131.
UCSCiuc001hyp.3. human.

Organism-specific databases

CTDi1131.
GeneCardsiGC01P239549.
HGNCiHGNC:1952. CHRM3.
HPAiCAB010409.
HPA024106.
MIMi100100. phenotype.
118494. gene.
neXtProtiNX_P20309.
Orphaneti2970. Prune belly syndrome.
PharmGKBiPA112.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250863.
GeneTreeiENSGT00780000121874.
HOGENOMiHOG000231484.
HOVERGENiHBG105720.
InParanoidiP20309.
KOiK04131.
OMAiCDKKKRR.
OrthoDBiEOG7V49Z7.
PhylomeDBiP20309.
TreeFamiTF320495.

Enzyme and pathway databases

ReactomeiREACT_16943. Muscarinic acetylcholine receptors.
REACT_18283. G alpha (q) signalling events.
REACT_18405. Acetylcholine regulates insulin secretion.
SignaLinkiP20309.

Miscellaneous databases

ChiTaRSiCHRM3. human.
EvolutionaryTraceiP20309.
GeneWikiiMuscarinic_acetylcholine_receptor_M3.
GenomeRNAii1131.
NextBioi4702.
PROiP20309.
SOURCEiSearch...

Gene expression databases

BgeeiP20309.
CleanExiHS_CHRM3.
ExpressionAtlasiP20309. baseline and differential.
GenevestigatoriP20309.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001183. Musac_Ach_M3_rcpt.
IPR000995. Musac_Ach_rcpt.
[Graphical view]
PANTHERiPTHR24249:SF61. PTHR24249:SF61. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00243. MUSCARINICR.
PR00540. MUSCRINICM3R.
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. "Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors."
    Peralta E.G., Ashkenazi A., Winslow J.W., Smith D.H., Ramachandran J., Capon D.J.
    EMBO J. 6:3923-3929(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes."
    Bonner T.I., Young A.C., Brann M.R., Buckley N.J.
    Neuron 1:403-410(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human-specific amino acid changes found in 103 protein-coding genes."
    Kitano T., Liu Y.-H., Ueda S., Saitou N.
    Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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].
  7. "Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes."
    Speek M.
    Mol. Cell. Biol. 21:1973-1985(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-384.
    Tissue: Teratocarcinoma.
  8. "Mutation of carboxyl-terminal threonine residues in human M3 muscarinic acetylcholine receptor modulates the extent of sequestration and desensitization."
    Yang J., Williams J.A., Yule D.I., Logsdon C.D.
    Mol. Pharmacol. 48:477-485(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: INVOLVEMENT IN EGBRS.
  10. "The muscarinic M3 acetylcholine receptor exists as two differently sized complexes at the plasma membrane."
    Patowary S., Alvarez-Curto E., Xu T.R., Holz J.D., Oliver J.A., Milligan G., Raicu V.
    Biochem. J. 452:303-312(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  11. "Identification and structural determination of the M(3) muscarinic acetylcholine receptor basolateral sorting signal."
    Iverson H.A., Fox D. III, Nadler L.S., Klevit R.E., Nathanson N.M.
    J. Biol. Chem. 280:24568-24575(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 271-289, MUTAGENESIS OF GLU-276; PHE-280 AND VAL-281, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACM3_HUMAN
AccessioniPrimary (citable) accession number: P20309
Secondary accession number(s): Q0VAJ8
, Q4QRI3, Q5VXY2, Q9HB60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 29, 2015
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.