Skip Header

Contribute Send feedback
Read comments (?) or add your own

P47746 (CNR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. 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:
Cannabinoid receptor 1
Short name=CB-R
Short name=CB1
Alternative name(s):
Brain-type cannabinoid receptor
Gene names
Name:Cnr1
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 length473 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in cannabinoid-induced CNS effects. Acts by inhibiting adenylate cyclase. Could be a receptor for anandamide. Inhibits L-type Ca2+ channel current.

Subunit structure

Interacts (via C-terminus) with CNRIP1 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Palmitoylation at Cys-416 is important for recruitment at both plasma membrane and lipid rafts By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Cannabinoid receptor 1
PRO_0000069316

Regions

Topological domain1 – 117117Extracellular Potential
Transmembrane118 – 14326Helical; Name=1; Potential
Topological domain144 – 15512Cytoplasmic Potential
Transmembrane156 – 17621Helical; Name=2; Potential
Topological domain177 – 18812Extracellular Potential
Transmembrane189 – 21325Helical; Name=3; Potential
Topological domain214 – 23320Cytoplasmic Potential
Transmembrane234 – 25623Helical; Name=4; Potential
Topological domain257 – 27418Extracellular Potential
Transmembrane275 – 30026Helical; Name=5; Potential
Topological domain301 – 34545Cytoplasmic Potential
Transmembrane346 – 36621Helical; Name=6; Potential
Topological domain367 – 37812Extracellular Potential
Transmembrane379 – 40022Helical; Name=7; Potential
Topological domain401 – 47373Cytoplasmic Potential

Amino acid modifications

Lipidation4161S-palmitoyl cysteine By similarity
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict91A → G in AAA57202. Ref.1
Sequence conflict1151S → R in AAA57202. Ref.1
Sequence conflict2111T → R in AAA57202. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47746 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: E504168191CB6429

FASTA47352,831
        10         20         30         40         50         60 
MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDIKGDMASK LGYFPQKFPL TSFRGSPFQE 

        70         80         90        100        110        120 
KMTAGDNSPL VPAGDTTNIT EFYNKSLSSF KENEDNIQCG ENFMDMECFM ILNPSQQLAI 

       130        140        150        160        170        180 
AVLSLTLGTF TVLENLLVLC VILHSRSLRC RPSYHFIGSL AVADLLGSVI FVYSFVDFHV 

       190        200        210        220        230        240 
FHRKDSPNVF LFKLGGVTAS FTASVGSLFL TAIDRYISIH RPLAYKRIVT RPKAVVAFCL 

       250        260        270        280        290        300 
MWTIAIVIAV LPLLGWNCKK LQSVCSDIFP LIDETYLMFW IGVTSVLLLF IVYAYMYILW 

       310        320        330        340        350        360 
KAHSHAVRMI QRGTQKSIII HTSEDGKVQV TRPDQARMDI RLAKTLVLIL VVLIICWGPL 

       370        380        390        400        410        420 
LAIMVYDVFG KMNKLIKTVF AFCSMLCLLN STVNPIIYAL RSKDLRHAFR SMFPSCEGTA 

       430        440        450        460        470 
QPLDNSMGDS DCLHKHANNT ASMHRAAESC IKSTVKIAKV TMSVSTDTSA EAL

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a cDNA encoding the mouse brain-type cannabinoid receptor protein."
Chakrabarti A., Onaivi E.S., Chaudhuri G.
DNA Seq. 5:385-388(1995) [PubMed: 8777318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"Determination of the cannabinoid receptors in mouse x rat hybridoma NG108-15 cells and rat GH4C1 cells."
Ho B.Y., Zhao J.
Neurosci. Lett. 212:123-126(1996) [PubMed: 8832654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Unresponsiveness to cannabinoids and reduced addictive effects of opiates in CB1 receptor knockout mice."
Ledent C., Valverde O., Cossu G., Petitet F., Aubert J.F., Beslot F., Boehme G.A., Imperato A., Pedrazzini T., Roques B.P., Vassart G., Fratta W., Parmentier M.
Science 283:401-404(1999) [PubMed: 9888857] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[4]"Structure, expression and regulation of the cannabinoid receptor gene (CB1) in Huntington's disease transgenic mice."
McCaw E.A., Hu H., Gomez G.T., Hebb A.L., Kelly M.E., Denovan-Wright E.M.
Eur. J. Biochem. 271:4909-4920(2004) [PubMed: 15606779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: C57BL/6 X CBA.
[5]Bonner T.I.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
[6]"cDNA cloning and expression analysis of mouse cannabinoid receptor (CB1) gene."
Yuan Z.-Q., Li L., Qiu B.-S., Song D.-K.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"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: Brain cortex.
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U17985 mRNA. Translation: AAA57202.1.
U40709 mRNA. Translation: AAA91176.1.
Y18374 Genomic DNA. Translation: CAB42647.1.
AY522555 Genomic DNA. Translation: AAS91801.1.
AY522554 mRNA. Translation: AAS91800.1.
U22948 Genomic DNA. Translation: AAA64413.1.
AF153345 mRNA. Translation: AAD34624.1.
AK139417 mRNA. Translation: BAE24003.1.
BC070447 mRNA. Translation: AAH70447.1.
BC079564 mRNA. Translation: AAH79564.1.
IPIIPI00111245.
RefSeqNP_031752.1. NM_007726.3.
UniGeneMm.7992.

3D structure databases

ProteinModelPortalP47746.
SMRP47746. Positions 111-417.
ModBaseSearch...

Protein-protein interaction databases

STRINGP47746.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP47746.

Proteomic databases

PRIDEP47746.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057188; ENSMUSP00000055797; ENSMUSG00000044288.
ENSMUST00000084736; ENSMUSP00000081787; ENSMUSG00000044288.
GeneID12801.
KEGGmmu:12801.
NMPDRfig|10090.3.peg.9375.

Organism-specific databases

CTD1268.
MGIMGI:104615. Cnr1.

Phylogenomic databases

eggNOGroNOG10571.
HOGENOMHBG716518.
HOVERGENHBG051045.
InParanoidP47746.
OMAFVYSFVD.
OrthoDBEOG41ZF9S.
PhylomeDBP47746.

Gene expression databases

ArrayExpressP47746.
BgeeP47746.
CleanExMM_CNR1.
GenevestigatorP47746.
GermOnlineENSMUSG00000044288. Mus musculus.

Family and domain databases

InterProIPR000276. 7TM_GPCR_Rhodpsn.
IPR002230. Cnbnoid_rcpt.
IPR000810. Cnoid_rcpt_1.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]
KOK04277.
PANTHERPTHR22750:SF10. Cnoid_rcpt_1. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PIRSFPIRSF037995. Cnoid_rcpt_1. 1 hit.
PRINTSPR00522. CANABINOID1R.
PR00362. CANNABINOIDR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282226.
SOURCESearch...

Entry information

Entry nameCNR1_MOUSE
AccessionPrimary (citable) accession number: P47746
Secondary accession number(s): Q5SF33
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 96 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