GP183_MOUSE
ID GP183_MOUSE Reviewed; 357 AA.
AC Q3U6B2; Q3U1F6; Q7TMV7; Q80T40;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=G-protein coupled receptor 183 {ECO:0000305};
DE AltName: Full=Epstein-Barr virus-induced G-protein coupled receptor 2 homolog {ECO:0000250|UniProtKB:P32249};
DE Short=EBI2 {ECO:0000250|UniProtKB:P32249};
DE Short=EBV-induced G-protein coupled receptor 2 homolog {ECO:0000250|UniProtKB:P32249};
GN Name=Gpr183 {ECO:0000312|MGI:MGI:2442034};
GN Synonyms=Ebi2 {ECO:0000250|UniProtKB:P32249};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-354.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19615922; DOI=10.1016/j.immuni.2009.06.016;
RA Gatto D., Paus D., Basten A., Mackay C.R., Brink R.;
RT "Guidance of B cells by the orphan G protein-coupled receptor EBI2 shapes
RT humoral immune responses.";
RL Immunity 31:259-269(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19597478; DOI=10.1038/nature08226;
RA Pereira J.P., Kelly L.M., Xu Y., Cyster J.G.;
RT "EBI2 mediates B cell segregation between the outer and centre follicle.";
RL Nature 460:1122-1126(2009).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=21673108; DOI=10.1074/jbc.m110.196345;
RA Benned-Jensen T., Smethurst C., Holst P.J., Page K.R., Sauls H.,
RA Sivertsen B., Schwartz T.W., Blanchard A., Jepras R., Rosenkilde M.M.;
RT "Ligand modulation of the Epstein-Barr virus-induced seven-transmembrane
RT receptor EBI2: identification of a potent and efficacious inverse
RT agonist.";
RL J. Biol. Chem. 286:29292-29302(2011).
RN [8]
RP FUNCTION.
RX PubMed=21844396; DOI=10.4049/jimmunol.1101262;
RA Kelly L.M., Pereira J.P., Yi T., Xu Y., Cyster J.G.;
RT "EBI2 guides serial movements of activated B cells and ligand activity is
RT detectable in lymphoid and nonlymphoid tissues.";
RL J. Immunol. 187:3026-3032(2011).
RN [9]
RP FUNCTION.
RX PubMed=21948984; DOI=10.4049/jimmunol.1101542;
RA Gatto D., Wood K., Brink R.;
RT "EBI2 operates independently of but in cooperation with CXCR5 and CCR7 to
RT direct B cell migration and organization in follicles and the germinal
RT center.";
RL J. Immunol. 187:4621-4628(2011).
RN [10]
RP IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.
RX PubMed=21796211; DOI=10.1038/nature10226;
RA Liu C., Yang X.V., Wu J., Kuei C., Mani N.S., Zhang L., Yu J., Sutton S.W.,
RA Qin N., Banie H., Karlsson L., Sun S., Lovenberg T.W.;
RT "Oxysterols direct B-cell migration through EBI2.";
RL Nature 475:519-523(2011).
RN [11]
RP IDENTIFICATION OF OXYSTEROLS AS ENDOGENOUS LIGANDS.
RX PubMed=21796212; DOI=10.1038/nature10280;
RA Hannedouche S., Zhang J., Yi T., Shen W., Nguyen D., Pereira J.P.,
RA Guerini D., Baumgarten B.U., Roggo S., Wen B., Knochenmuss R., Noel S.,
RA Gessier F., Kelly L.M., Vanek M., Laurent S., Preuss I., Miault C.,
RA Christen I., Karuna R., Li W., Koo D.I., Suply T., Schmedt C., Peters E.C.,
RA Falchetto R., Katopodis A., Spanka C., Roy M.O., Detheux M., Chen Y.A.,
RA Schultz P.G., Cho C.Y., Seuwen K., Cyster J.G., Sailer A.W.;
RT "Oxysterols direct immune cell migration via EBI2.";
RL Nature 475:524-527(2011).
RN [12]
RP FUNCTION.
RX PubMed=22913878; DOI=10.1096/fj.12-208876;
RA Barroso R., Martinez Munoz L., Barrondo S., Vega B., Holgado B.L.,
RA Lucas P., Baillo A., Salles J., Rodriguez-Frade J.M., Mellado M.;
RT "EBI2 regulates CXCL13-mediated responses by heterodimerization with
RT CXCR5.";
RL FASEB J. 26:4841-4854(2012).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23682316; DOI=10.7554/elife.00757;
RA Yi T., Cyster J.G.;
RT "EBI2-mediated bridging channel positioning supports splenic dendritic cell
RT homeostasis and particulate antigen capture.";
RL Elife 2:E00757-E00757(2013).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23502855; DOI=10.1038/ni.2555;
RA Gatto D., Wood K., Caminschi I., Murphy-Durland D., Schofield P.,
RA Christ D., Karupiah G., Brink R.;
RT "The chemotactic receptor EBI2 regulates the homeostasis, localization and
RT immunological function of splenic dendritic cells.";
RL Nat. Immunol. 14:446-453(2013).
RN [15]
RP INDUCTION.
RX PubMed=25176650; DOI=10.1016/j.celrep.2014.07.059;
RA Huang C., Gonzalez D.G., Cote C.M., Jiang Y., Hatzi K., Teater M., Dai K.,
RA Hla T., Haberman A.M., Melnick A.;
RT "The BCL6 RD2 domain governs commitment of activated B cells to form
RT germinal centers.";
RL Cell Rep. 8:1497-1508(2014).
RN [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25297897; DOI=10.1002/glia.22757;
RA Rutkowska A., Preuss I., Gessier F., Sailer A.W., Dev K.K.;
RT "EBI2 regulates intracellular signaling and migration in human astrocyte.";
RL Glia 63:341-351(2015).
RN [17]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26438360; DOI=10.1084/jem.20150088;
RA Nevius E., Pinho F., Dhodapkar M., Jin H., Nadrah K., Horowitz M.C.,
RA Kikuta J., Ishii M., Pereira J.P.;
RT "Oxysterols and EBI2 promote osteoclast precursor migration to bone
RT surfaces and regulate bone mass homeostasis.";
RL J. Exp. Med. 212:1931-1946(2015).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27147029; DOI=10.1038/nature17947;
RA Li J., Lu E., Yi T., Cyster J.G.;
RT "EBI2 augments Tfh cell fate by promoting interaction with IL-2-quenching
RT dendritic cells.";
RL Nature 533:110-114(2016).
RN [19]
RP FUNCTION, AND INDUCTION.
RX PubMed=27166278; DOI=10.1038/srep25520;
RA Rutkowska A., O'Sullivan S.A., Christen I., Zhang J., Sailer A.W.,
RA Dev K.K.;
RT "The EBI2 signalling pathway plays a role in cellular crosstalk between
RT astrocytes and macrophages.";
RL Sci. Rep. 6:25520-25520(2016).
CC -!- FUNCTION: G-protein coupled receptor expressed in lymphocytes that acts
CC as a chemotactic receptor for B-cells, T-cells, splenic dendritic
CC cells, monocytes/macrophages and astrocytes (PubMed:19597478,
CC PubMed:19615922, PubMed:21844396, PubMed:21796211, PubMed:21796212,
CC PubMed:27147029). Receptor for oxysterol 7-alpha,25-
CC dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols
CC (PubMed:21796211, PubMed:21796212). Mediates cell positioning and
CC movement of a number of cells by binding the 7-alpha,25-OHC ligand that
CC forms a chemotactic gradient (PubMed:21796211, PubMed:21796212,
CC PubMed:27147029). Binding of 7-alpha,25-OHC mediates the correct
CC localization of B-cells during humoral immune responses
CC (PubMed:21796211, PubMed:21796212). Collaborates with CXCR5 to mediate
CC B-cell migration; probably by forming a heterodimer with CXCR5 that
CC affects the interaction between of CXCL13 and CXCR5 (PubMed:21948984,
CC PubMed:22913878). Guides B-cell movement along the B-cell zone-T-cell
CC zone boundary and later to interfollicular and outer follicular regions
CC (PubMed:19615922, PubMed:19597478, PubMed:21844396). Its specific
CC expression during B-cell maturation helps position B-cells
CC appropriately for mounting T-dependent antibody responses
CC (PubMed:19615922). Also acts as a chemotactic receptor for some T-cells
CC upon binding to 7-alpha,25-OHC ligand (PubMed:27147029). Promotes
CC follicular helper T (Tfh) cells differentiation by positioning
CC activated T-cells at the follicle-T-zone interface, promoting contact
CC of newly activated CD4 T-cells with activated dendritic cells and
CC exposing them to Tfh-cell-promoting inducible costimulator (ICOS)
CC ligand (PubMed:27147029). Expression in splenic dendritic cells is
CC required for their homeostasis, localization and ability to induce
CC B- and T-cell responses: GPR183 acts as a chemotactic receptor in
CC dendritic cells that mediates the accumulation of CD4(+) dendritic
CC cells in bridging channels (PubMed:23682316, PubMed:23502855).
CC Regulates migration of astrocytes and is involved in communication
CC between astrocytes and macrophages (PubMed:25297897, PubMed:27166278).
CC Promotes osteoclast precursor migration to bone surfaces
CC (PubMed:26438360). Signals constitutively through G(i)-alpha, but not
CC G(s)-alpha or G(q)-alpha (By similarity). Signals constitutively also
CC via MAPK1/3 (ERK1/2) (By similarity). {ECO:0000250|UniProtKB:P32249,
CC ECO:0000269|PubMed:19597478, ECO:0000269|PubMed:19615922,
CC ECO:0000269|PubMed:21796211, ECO:0000269|PubMed:21796212,
CC ECO:0000269|PubMed:21844396, ECO:0000269|PubMed:21948984,
CC ECO:0000269|PubMed:22913878, ECO:0000269|PubMed:23502855,
CC ECO:0000269|PubMed:23682316, ECO:0000269|PubMed:25297897,
CC ECO:0000269|PubMed:26438360, ECO:0000269|PubMed:27147029,
CC ECO:0000269|PubMed:27166278}.
CC -!- SUBUNIT: Homodimer and heterodimer. Heterodimerizes with CXCR5; leading
CC to modulate the interaction between of CXCL13 and CXCR5.
CC {ECO:0000250|UniProtKB:P32249}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32249};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in mature B-cells and increases in
CC expression early after activation, before being down-regulated in
CC germinal center B-cells (PubMed:19597478). Expressed in astrocytes
CC (PubMed:25297897). Specifically expressed in CD4(+) dendritic cells but
CC not in CD8(+) dendritic cells (PubMed:23682316, PubMed:23502855).
CC Expressed in monocyte/osteoclasts precursors and mature osteoclasts
CC (PubMed:26438360). {ECO:0000269|PubMed:19597478,
CC ECO:0000269|PubMed:23502855, ECO:0000269|PubMed:23682316,
CC ECO:0000269|PubMed:25297897, ECO:0000269|PubMed:26438360}.
CC -!- INDUCTION: Up-regulated during B-cell maturation in the bone marrow,
CC and is expressed in mature recirculating B-cells in bone marrow, spleen
CC and lymph nodes (PubMed:19597478). Up-regulated in B-cells after BCR
CC and CD40 engagement (PubMed:19597478). Down-regulated by
CC lipopolysaccharide (LPS) in astrocytes (PubMed:27166278). Expression is
CC directly down-regulated by BCL6 (PubMed:25176650).
CC {ECO:0000269|PubMed:19597478, ECO:0000269|PubMed:25176650,
CC ECO:0000269|PubMed:27166278}.
CC -!- DISRUPTION PHENOTYPE: Mice display a reduction in the early antibody
CC response to a T-dependent antigen (PubMed:19597478). B-cells fail to
CC move to the outer follicle at day 2 of activation, and instead are
CC found in the follicle center (PubMed:19615922). Mice have normal
CC numbers of B- and T-cells and organized follicles and T-cell
CC compartments are present (PubMed:19615922). Mice show a decreased
CC number of splenic CD4(+) dendritic cells and defective priming of
CC T- and B-cell response (PubMed:23682316, PubMed:23502855). Reduced
CC follicular helper T (Tfh) cells (PubMed:27147029). T-cells fail to
CC accumulate in the outer T zone at either time point and instead remain
CC dispersed throughout the T zone (PubMed:27147029).
CC {ECO:0000269|PubMed:19597478, ECO:0000269|PubMed:19615922,
CC ECO:0000269|PubMed:23502855, ECO:0000269|PubMed:27147029}.
CC -!- MISCELLANEOUS: GSK682753A (8-[(2E)-3-(4-chlorophenyl)prop-2-enoyl]-3-
CC [(3,4-dichlorophenyl)methyl]-1-oxa-3,8-diazaspiro[4.5]decan-2-one), an
CC inverse agonist, selectively inhibits the constitutive activity of
CC GPR183 with high potency and efficacy. {ECO:0000305|PubMed:21673108}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK138693; BAE23750.1; -; mRNA.
DR EMBL; AK153216; BAE31813.1; -; mRNA.
DR EMBL; AK156005; BAE33542.1; -; mRNA.
DR EMBL; BC052868; AAH52868.1; -; mRNA.
DR EMBL; AY255606; AAO85118.1; -; mRNA.
DR CCDS; CCDS27343.1; -.
DR RefSeq; NP_898852.2; NM_183031.2.
DR AlphaFoldDB; Q3U6B2; -.
DR SMR; Q3U6B2; -.
DR STRING; 10090.ENSMUSP00000052404; -.
DR BindingDB; Q3U6B2; -.
DR ChEMBL; CHEMBL3259471; -.
DR GlyGen; Q3U6B2; 1 site.
DR iPTMnet; Q3U6B2; -.
DR PhosphoSitePlus; Q3U6B2; -.
DR SwissPalm; Q3U6B2; -.
DR EPD; Q3U6B2; -.
DR jPOST; Q3U6B2; -.
DR PaxDb; Q3U6B2; -.
DR PRIDE; Q3U6B2; -.
DR ProteomicsDB; 267752; -.
DR Antibodypedia; 10905; 236 antibodies from 32 providers.
DR DNASU; 321019; -.
DR Ensembl; ENSMUST00000049872; ENSMUSP00000052404; ENSMUSG00000051212.
DR GeneID; 321019; -.
DR KEGG; mmu:321019; -.
DR UCSC; uc007vaq.1; mouse.
DR CTD; 1880; -.
DR MGI; MGI:2442034; Gpr183.
DR VEuPathDB; HostDB:ENSMUSG00000051212; -.
DR eggNOG; ENOG502QWD9; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q3U6B2; -.
DR OMA; HYTVFLM; -.
DR OrthoDB; 760173at2759; -.
DR PhylomeDB; Q3U6B2; -.
DR TreeFam; TF350009; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 321019; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Gpr183; mouse.
DR PRO; PR:Q3U6B2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3U6B2; protein.
DR Bgee; ENSMUSG00000051212; Expressed in mesenteric lymph node and 125 other tissues.
DR ExpressionAtlas; Q3U6B2; baseline and differential.
DR Genevisible; Q3U6B2; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008142; F:oxysterol binding; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IMP:UniProtKB.
DR GO; GO:0002312; P:B cell activation involved in immune response; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0002407; P:dendritic cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0036145; P:dendritic cell homeostasis; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR GO; GO:0002313; P:mature B cell differentiation involved in immune response; IMP:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:2000458; P:regulation of astrocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0010818; P:T cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0061470; P:T follicular helper cell differentiation; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunity; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="G-protein coupled receptor 183"
FT /id="PRO_0000303231"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..261
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 122..130
FT /note="Interaction with G proteins"
FT /evidence="ECO:0000250"
FT REGION 336..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 108
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 112
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT BINDING 256
FT /ligand="7alpha,25-dihydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:37623"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P32249"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 163
FT /note="L -> F (in Ref. 2; AAH52868)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> P (in Ref. 1; BAE33542)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="N -> S (in Ref. 2; AAH52868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40185 MW; D4B1C32C0C451993 CRC64;
MANNFTTPLA TSHGNNCDLY AHHSTARVLM PLHYSLVFII GLVGNLLALV VIVQNRKKIN
STTLYSMNLV ISDILFTTAL PTRIAYYALG FDWRIGDALC RVTALVFYIN TYAGVNFMTC
LSIDRFFAVV HPLRYNKIKR IEYAKGVCLS VWILVFAQTL PLLLTPMSKE EGDKTTCMEY
PNFEGTASLP WILLGACLLG YVLPITVILL CYSQICCKLF RTAKQNPLTE KSGVNKKALN
TIILIIVVFI LCFTPYHVAI IQHMIKMLCS PGALECGARH SFQISLHFTV CLMNFNCCMD
PFIYFFACKG YKRKVMKMLK RQVSVSISSA VRSAPEENSR EMTESQMMIH SKASNGR
