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Q8BZR0 (GPR82_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. 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:
Probable G-protein coupled receptor 82
Gene names
Name:Gpr82
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Orphan receptor.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Probable G-protein coupled receptor 82
PRO_0000303082

Regions

Topological domain1 – 1111Extracellular Potential
Transmembrane12 – 3221Helical; Name=1; Potential
Topological domain33 – 5523Cytoplasmic Potential
Transmembrane56 – 7621Helical; Name=2; Potential
Topological domain77 – 9216Extracellular Potential
Transmembrane93 – 11523Helical; Name=3; Potential
Topological domain116 – 15641Cytoplasmic Potential
Transmembrane157 – 17721Helical; Name=4; Potential
Topological domain178 – 19720Extracellular Potential
Transmembrane198 – 21821Helical; Name=5; Potential
Topological domain219 – 25133Cytoplasmic Potential
Transmembrane252 – 27221Helical; Name=6; Potential
Topological domain273 – 32856Extracellular Potential

Amino acid modifications

Glycosylation31N-linked (GlcNAc...) Potential
Glycosylation41N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8BZR0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 324C3AED267FCE53

FASTA32837,555
        10         20         30         40         50         60 
MTNNSTCIQP SVISTTALPV TYIFLFIIGL FGNSLAQWVF LTKIGKKTST HIYLANLVTA 

        70         80         90        100        110        120 
NLLVCTAMPF MGIYFLRGFY WKYQSVQCRL VNFLGTLSMH VSMFVSLLIL SWIAISRYAT 

       130        140        150        160        170        180 
LMKKESKQEA TSCYERMFYG HVLKRFRQPN FARTMCIYIW GVVLVIIIPV TLYYSVVEAT 

       190        200        210        220        230        240 
EEGQSQCYNR QMELGARPSQ IAGLIGTTFI GFSFLVVVTS YYSLVSHLRR VRTCTSITEK 

       250        260        270        280        290        300 
DLTYRSVKRH LLIIQVLLVV CFLPYSIFKP IFYVLHQREG DCQQLNYLIE AKNILTCLAS 

       310        320 
ARSSTDPIIF LLLDKTFKKT LYGLLTKS

« Hide

References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Epididymis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
[4]"The G protein-coupled receptor repertoires of human and mouse."
Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E., Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C., Bergmann J.E., Gaitanaris G.A.
Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK033761 mRNA. Translation: BAC28466.1.
AL671117 Genomic DNA. Translation: CAM19449.1.
BC116704 mRNA. Translation: AAI16705.1.
AY255571 mRNA. Translation: AAO85083.1.
IPIIPI00227660.
RefSeqNP_783600.1. NM_175669.3.
UniGeneMm.383294.

3D structure databases

ProteinModelPortalQ8BZR0.
SMRQ8BZR0. Positions 13-172.
ModBaseSearch...

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ8BZR0.

Proteomic databases

PRIDEQ8BZR0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053659; ENSMUSP00000062535; ENSMUSG00000047678.
GeneID319200.
KEGGmmu:319200.
UCSCuc009srv.1. mouse.

Organism-specific databases

CTD27197.
MGIMGI:2441734. Gpr82.

Phylogenomic databases

eggNOGNOG151131.
GeneTreeENSGT00640000091213.
HOGENOMHOG000112792.
HOVERGENHBG097852.
InParanoidQ8BZR0.
KOK08420.
OrthoDBEOG41ZFB8.

Gene expression databases

BgeeQ8BZR0.
CleanExMM_GPR82.
GenevestigatorQ8BZR0.

Family and domain databases

InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. False negative.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio394366.
SOURCESearch...

Entry information

Entry nameGPR82_MOUSE
AccessionPrimary (citable) accession number: Q8BZR0
Secondary accession number(s): Q80UB1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: May 1, 2013
This is version 80 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