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AGRG3_MOUSE
ID   AGRG3_MOUSE             Reviewed;         542 AA.
AC   Q8R0T6; Q3U2Q3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Adhesion G protein-coupled receptor G3;
DE   AltName: Full=G-protein coupled receptor 97;
DE   Flags: Precursor;
GN   Name=Adgrg3; Synonyms=Gpr97;
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=NOD;
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/6J; TISSUE=Embryo, and Kidney;
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   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=24113187; DOI=10.1038/cddis.2013.346;
RA   Wang J.J., Zhang L.L., Zhang H.X., Shen C.L., Lu S.Y., Kuang Y., Wan Y.H.,
RA   Wang W.G., Yan H.M., Dang S.Y., Fei J., Jin X.L., Wang Z.G.;
RT   "Gpr97 is essential for the follicular versus marginal zone B-lymphocyte
RT   fate decision.";
RL   Cell Differ. 4:E853-E853(2013).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=24178298; DOI=10.1074/jbc.m113.512954;
RA   Valtcheva N., Primorac A., Jurisic G., Hollmen M., Detmar M.;
RT   "The orphan adhesion G protein-coupled receptor GPR97 regulates migration
RT   of lymphatic endothelial cells via the small GTPases RhoA and Cdc42.";
RL   J. Biol. Chem. 288:35736-35748(2013).
CC   -!- FUNCTION: Orphan receptor that regulates migration of lymphatic
CC       endothelial cells via the small GTPases RhoA and CDC42 (By similarity).
CC       Regulates B-cell development (PubMed:24113187). Seems to signal through
CC       G-alpha(q)-proteins (By similarity). {ECO:0000250|UniProtKB:Q86Y34,
CC       ECO:0000269|PubMed:24113187}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q86Y34}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in intestinal lymphatic
CC       endothelium. {ECO:0000269|PubMed:24178298}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mutant mice show altered
CC       follicular-versus-marginal zone B-lymphocyte fate decision in the
CC       spleen and decreased numbers of B220+ lymphocytes in the bone marrow.
CC       {ECO:0000269|PubMed:24113187}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR   EMBL; AK155164; BAE33087.1; -; mRNA.
DR   EMBL; BC026426; AAH26426.1; -; mRNA.
DR   EMBL; BC064726; AAH64726.1; -; mRNA.
DR   CCDS; CCDS22554.1; -.
DR   RefSeq; NP_766624.3; NM_173036.3.
DR   AlphaFoldDB; Q8R0T6; -.
DR   SMR; Q8R0T6; -.
DR   IntAct; Q8R0T6; 1.
DR   STRING; 10090.ENSMUSP00000051079; -.
DR   MEROPS; P02.024; -.
DR   GlyGen; Q8R0T6; 4 sites.
DR   iPTMnet; Q8R0T6; -.
DR   PhosphoSitePlus; Q8R0T6; -.
DR   jPOST; Q8R0T6; -.
DR   MaxQB; Q8R0T6; -.
DR   PaxDb; Q8R0T6; -.
DR   PRIDE; Q8R0T6; -.
DR   ProteomicsDB; 285773; -.
DR   Antibodypedia; 15147; 163 antibodies from 27 providers.
DR   DNASU; 54672; -.
DR   Ensembl; ENSMUST00000051259; ENSMUSP00000051079; ENSMUSG00000060470.
DR   GeneID; 54672; -.
DR   KEGG; mmu:54672; -.
DR   UCSC; uc009mxp.2; mouse.
DR   CTD; 222487; -.
DR   MGI; MGI:1859670; Adgrg3.
DR   VEuPathDB; HostDB:ENSMUSG00000060470; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   GeneTree; ENSGT00940000154285; -.
DR   HOGENOM; CLU_002753_3_9_1; -.
DR   InParanoid; Q8R0T6; -.
DR   OMA; TLFKGPQ; -.
DR   OrthoDB; 501343at2759; -.
DR   PhylomeDB; Q8R0T6; -.
DR   TreeFam; TF321769; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 54672; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Adgrg3; mouse.
DR   PRO; PR:Q8R0T6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8R0T6; protein.
DR   Bgee; ENSMUSG00000060470; Expressed in granulocyte and 79 other tissues.
DR   ExpressionAtlas; Q8R0T6; baseline and differential.
DR   Genevisible; Q8R0T6; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032792; P:negative regulation of CREB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   Gene3D; 2.60.220.50; -; 1.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR003910; GPR1/GPR3/GPR5.
DR   InterPro; IPR000203; GPS.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01422; GPR56ORPHANR.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..542
FT                   /note="Adhesion G protein-coupled receptor G3"
FT                   /id="PRO_0000012890"
FT   TOPO_DOM        19..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        268..288
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..302
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        303..323
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..342
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        343..363
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        373..393
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..426
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        427..447
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..467
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        468..488
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..494
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        495..515
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        516..542
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          210..256
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        295
FT                   /note="F -> L (in Ref. 2; AAH64726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   542 AA;  60072 MW;  E37A23B108BA1CB3 CRC64;
     MATARSLGLL FFLLLTSDEE TTEEPRNVCR RLQEGHEYDT FDLNDTAQCF TKCGQSEHSP
     CDVGNLQRYW LNYESYLLEN SMETVDMPFV KALIQNISTD VSEDLLYSLM LSQIPRQVMQ
     GEDEPADGVR LPKSLFGALP GNRSAVRLAI TVLDIGAGNV FKGPKLLEDK GSSVLNNRMV
     GLSVGQMHAT GLSEPVEITF SHERQPPNVI LTCVFWDMAK GDWDSHGCST VPGDGRTVCR
     CDHLTFFALL LRPILDLATA QTLTRISQAG SAVSMIFLAF TMVLYVAFRF SLQRFKSEDA
     PKIHMALSIS LFLLNLTFLI NVGSSSQGPP ASCWVRAAIF HYFLLCVFTW MGLEAFHLYL
     LAIRVFNTYF GHYFLKLSLL AWGLPVLVVI GAGSSNSYGV YTIRDQENRT SLELCWFQKE
     PALYATVHGY FLVTFLFGAV VLALVAWKIF TLPSVTAGKG QGPTWKSVLT VLGLSSLVGM
     TWGLAVLTPL GLSTIYVFTL LNSLQGLFIF CWFIILYFPT QSTTASSSGT ARLDQAHSVS
     QE
 
 
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