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Q3U6B2

- GP183_MOUSE

UniProt

Q3U6B2 - GP183_MOUSE

Protein

G-protein coupled receptor 183

Gene

Gpr183

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    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).By similarity3 Publications

    GO - Molecular functioni

    1. G-protein coupled receptor activity Source: UniProtKB-KW
    2. oxysterol binding Source: UniProtKB

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: UniProtKB
    2. humoral immune response Source: UniProtKB
    3. mature B cell differentiation involved in immune response Source: UniProtKB
    4. positive regulation of B cell proliferation Source: UniProtKB
    5. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Gpr183
    Synonyms:Ebi2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:2442034. Gpr183.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 357357G-protein coupled receptor 183PRO_0000303231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi100 ↔ 177PROSITE-ProRule annotation
    Modified residuei324 – 3241Phosphoserine1 Publication
    Modified residuei345 – 3451Phosphoserine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiQ3U6B2.

    PTM databases

    PhosphoSiteiQ3U6B2.

    Expressioni

    Tissue specificityi

    Expressed in mature B-cells and increases in expression early after activation, before being down-regulated in germinal center B-cells.1 Publication

    Inductioni

    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.1 Publication

    Gene expression databases

    BgeeiQ3U6B2.
    GenevestigatoriQ3U6B2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3U6B2.
    SMRiQ3U6B2. Positions 20-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini54 – 7320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini92 – 10110ExtracellularSequence Analysis
    Topological domaini124 – 14522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini165 – 18824ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini212 – 23726CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini262 – 28322ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini309 – 35749CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 5326Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei74 – 9118Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei102 – 12322Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei146 – 16419Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei189 – 21123Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei238 – 26124Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei284 – 30825Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1309Interaction with G proteinsBy similarity

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG145860.
    GeneTreeiENSGT00750000117626.
    HOGENOMiHOG000043070.
    HOVERGENiHBG101355.
    InParanoidiQ3U6B2.
    KOiK04305.
    OMAiLVFYINT.
    OrthoDBiEOG7VDXPF.
    PhylomeDBiQ3U6B2.
    TreeFamiTF350009.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3U6B2-1 [UniParc]FASTAAdd to Basket

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    MANNFTTPLA TSHGNNCDLY AHHSTARVLM PLHYSLVFII GLVGNLLALV    50
    VIVQNRKKIN STTLYSMNLV ISDILFTTAL PTRIAYYALG FDWRIGDALC 100
    RVTALVFYIN TYAGVNFMTC LSIDRFFAVV HPLRYNKIKR IEYAKGVCLS 150
    VWILVFAQTL PLLLTPMSKE EGDKTTCMEY PNFEGTASLP WILLGACLLG 200
    YVLPITVILL CYSQICCKLF RTAKQNPLTE KSGVNKKALN TIILIIVVFI 250
    LCFTPYHVAI IQHMIKMLCS PGALECGARH SFQISLHFTV CLMNFNCCMD 300
    PFIYFFACKG YKRKVMKMLK RQVSVSISSA VRSAPEENSR EMTESQMMIH 350
    SKASNGR 357
    Length:357
    Mass (Da):40,185
    Last modified:October 11, 2005 - v1
    Checksum:iD4B1C32C0C451993
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1631L → F in AAH52868. (PubMed:15489334)Curated
    Sequence conflicti239 – 2391L → P in BAE33542. (PubMed:16141072)Curated
    Sequence conflicti338 – 3381N → S in AAH52868. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS27343.1.
    RefSeqiNP_898852.2. NM_183031.2.
    UniGeneiMm.265618.

    Genome annotation databases

    EnsembliENSMUST00000049872; ENSMUSP00000052404; ENSMUSG00000051212.
    GeneIDi321019.
    KEGGimmu:321019.
    UCSCiuc007vaq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS27343.1.
    RefSeqi NP_898852.2. NM_183031.2.
    UniGenei Mm.265618.

    3D structure databases

    ProteinModelPortali Q3U6B2.
    SMRi Q3U6B2. Positions 20-319.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    GuidetoPHARMACOLOGYi 81.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q3U6B2.

    Proteomic databases

    PRIDEi Q3U6B2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049872 ; ENSMUSP00000052404 ; ENSMUSG00000051212 .
    GeneIDi 321019.
    KEGGi mmu:321019.
    UCSCi uc007vaq.1. mouse.

    Organism-specific databases

    CTDi 1880.
    MGIi MGI:2442034. Gpr183.

    Phylogenomic databases

    eggNOGi NOG145860.
    GeneTreei ENSGT00750000117626.
    HOGENOMi HOG000043070.
    HOVERGENi HBG101355.
    InParanoidi Q3U6B2.
    KOi K04305.
    OMAi LVFYINT.
    OrthoDBi EOG7VDXPF.
    PhylomeDBi Q3U6B2.
    TreeFami TF350009.

    Miscellaneous databases

    NextBioi 397884.
    PROi Q3U6B2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3U6B2.
    Genevestigatori Q3U6B2.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.
    9. Cited for: IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.

    Entry informationi

    Entry nameiGP183_MOUSE
    AccessioniPrimary (citable) accession number: Q3U6B2
    Secondary accession number(s): Q3U1F6, Q7TMV7, Q80T40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3