Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3U6B2 (GP183_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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

Names and origin

Protein namesRecommended name:
G-protein coupled receptor 183
Alternative name(s):
Epstein-Barr virus-induced G-protein coupled receptor 2
Short name=EBI2
Short name=EBV-induced G-protein coupled receptor 2
Gene names
Name:Gpr183
Synonyms:Ebi2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols. Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses. Promotes activated B-cell localization in the outer follicle and interfollicular regions. Its specific expression during B-cell maturation helps position B-cells appropriately for mounting T-dependent antibody responses By similarity. Signals constitutively through G(i)-alpha, but not G(s)-alpha or G(q)-alpha. Signals constitutively also via MAPK1/3 (ERK1/2). Ref.5 Ref.6 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in mature B-cells and increases in expression early after activation, before being down-regulated in germinal center B-cells. Ref.6

Induction

Up-regulated during B-cell maturation in the bone marrow, and is expressed in mature recirculating B-cells in bone marrow, spleen and lymph nodes. Up-regulated in B-cells after BCR and CD40 engagement. Ref.6

Disruption phenotype

Mice display a reduction in the early antibody response to a T-dependent antigen. B-cells fail to move to the outer follicle at day 2 of activation, and instead are found in the follicle center. Mice have normal numbers of B and T cells and organized follicles and T-cell compartments are present. Ref.5 Ref.6

Miscellaneous

GSK682753A (8-[(2E)-3-(4-chlorophenyl)prop-2-enoyl]-3-[(3,4-dichlorophenyl)methyl]-1-oxa-3,8-diazaspiro[4.5]decan-2-one), an inverse agonist, selectively inhibits the constitutive activity of GPR183 with high potency and efficacy (Ref.7).

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357G-protein coupled receptor 183
PRO_0000303231

Regions

Topological domain1 – 2727Extracellular Potential
Transmembrane28 – 5326Helical; Name=1; Potential
Topological domain54 – 7320Cytoplasmic Potential
Transmembrane74 – 9118Helical; Name=2; Potential
Topological domain92 – 10110Extracellular Potential
Transmembrane102 – 12322Helical; Name=3; Potential
Topological domain124 – 14522Cytoplasmic Potential
Transmembrane146 – 16419Helical; Name=4; Potential
Topological domain165 – 18824Extracellular Potential
Transmembrane189 – 21123Helical; Name=5; Potential
Topological domain212 – 23726Cytoplasmic Potential
Transmembrane238 – 26124Helical; Name=6; Potential
Topological domain262 – 28322Extracellular Potential
Transmembrane284 – 30825Helical; Name=7; Potential
Topological domain309 – 35749Cytoplasmic Potential
Region122 – 1309Interaction with G proteins By similarity

Amino acid modifications

Modified residue3241Phosphoserine Ref.4
Modified residue3451Phosphoserine Ref.4
Glycosylation41N-linked (GlcNAc...) Potential
Disulfide bond100 ↔ 177 By similarity

Experimental info

Sequence conflict1631L → F in AAH52868. Ref.2
Sequence conflict2391L → P in BAE33542. Ref.1
Sequence conflict3381N → S in AAH52868. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3U6B2 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: D4B1C32C0C451993

FASTA35740,185
        10         20         30         40         50         60 
MANNFTTPLA TSHGNNCDLY AHHSTARVLM PLHYSLVFII GLVGNLLALV VIVQNRKKIN 

        70         80         90        100        110        120 
STTLYSMNLV ISDILFTTAL PTRIAYYALG FDWRIGDALC RVTALVFYIN TYAGVNFMTC 

       130        140        150        160        170        180 
LSIDRFFAVV HPLRYNKIKR IEYAKGVCLS VWILVFAQTL PLLLTPMSKE EGDKTTCMEY 

       190        200        210        220        230        240 
PNFEGTASLP WILLGACLLG YVLPITVILL CYSQICCKLF RTAKQNPLTE KSGVNKKALN 

       250        260        270        280        290        300 
TIILIIVVFI LCFTPYHVAI IQHMIKMLCS PGALECGARH SFQISLHFTV CLMNFNCCMD 

       310        320        330        340        350 
PFIYFFACKG YKRKVMKMLK RQVSVSISSA VRSAPEENSR EMTESQMMIH SKASNGR 

« Hide

References

« Hide 'large scale' 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 and NOD.
Tissue: Bone marrow, Spleen and Thymus.
[2]"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].
Strain: C57BL/6NCr.
Tissue: Hematopoietic stem cell.
[3]"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 250-354.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-345, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Guidance of B cells by the orphan G protein-coupled receptor EBI2 shapes humoral immune responses."
Gatto D., Paus D., Basten A., Mackay C.R., Brink R.
Immunity 31:259-269(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"EBI2 mediates B cell segregation between the outer and centre follicle."
Pereira J.P., Kelly L.M., Xu Y., Cyster J.G.
Nature 460:1122-1126(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
[7]"Ligand modulation of the Epstein-Barr virus-induced seven-transmembrane receptor EBI2: identification of a potent and efficacious inverse agonist."
Benned-Jensen T., Smethurst C., Holst P.J., Page K.R., Sauls H., Sivertsen B., Schwartz T.W., Blanchard A., Jepras R., Rosenkilde M.M.
J. Biol. Chem. 286:29292-29302(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Oxysterols direct B-cell migration through EBI2."
Liu C., Yang X.V., Wu J., Kuei C., Mani N.S., Zhang L., Yu J., Sutton S.W., Qin N., Banie H., Karlsson L., Sun S., Lovenberg T.W.
Nature 475:519-523(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.
[9]"Oxysterols direct immune cell migration via EBI2."
Hannedouche S., Zhang J., Yi T., Shen W., Nguyen D., Pereira J.P., Guerini D., Baumgarten B.U., Roggo S., Wen B., Knochenmuss R., Noel S., Gessier F., Kelly L.M., Vanek M., Laurent S., Preuss I., Miault C. expand/collapse author list , Christen I., Karuna R., Li W., Koo D.I., Suply T., Schmedt C., Peters E.C., Falchetto R., Katopodis A., Spanka C., Roy M.O., Detheux M., Chen Y.A., Schultz P.G., Cho C.Y., Seuwen K., Cyster J.G., Sailer A.W.
Nature 475:524-527(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK138693 mRNA. Translation: BAE23750.1.
AK153216 mRNA. Translation: BAE31813.1.
AK156005 mRNA. Translation: BAE33542.1.
BC052868 mRNA. Translation: AAH52868.1.
AY255606 mRNA. Translation: AAO85118.1.
RefSeqNP_898852.2. NM_183031.2.
UniGeneMm.265618.

3D structure databases

ProteinModelPortalQ3U6B2.
SMRQ3U6B2. Positions 20-319.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY81.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ3U6B2.

Proteomic databases

PRIDEQ3U6B2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049872; ENSMUSP00000052404; ENSMUSG00000051212.
GeneID321019.
KEGGmmu:321019.
UCSCuc007vaq.1. mouse.

Organism-specific databases

CTD1880.
MGIMGI:2442034. Gpr183.

Phylogenomic databases

eggNOGNOG145860.
GeneTreeENSGT00750000117626.
HOGENOMHOG000043070.
HOVERGENHBG101355.
InParanoidQ3U6B2.
KOK04305.
OMALVFYINT.
OrthoDBEOG7VDXPF.
PhylomeDBQ3U6B2.
TreeFamTF350009.

Gene expression databases

BgeeQ3U6B2.
GenevestigatorQ3U6B2.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio397884.
PROQ3U6B2.
SOURCESearch...

Entry information

Entry nameGP183_MOUSE
AccessionPrimary (citable) accession number: Q3U6B2
Secondary accession number(s): Q3U1F6, Q7TMV7, Q80T40
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries