AGRG3_HUMAN
ID AGRG3_HUMAN Reviewed; 549 AA.
AC Q86Y34; Q6ZMF4; Q86SL9; Q8IZF1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Adhesion G protein-coupled receptor G3 {ECO:0000303|PubMed:25713288};
DE AltName: Full=G-protein coupled receptor 97;
DE AltName: Full=G-protein coupled receptor PGR26;
DE Flags: Precursor;
GN Name=ADGRG3 {ECO:0000312|HGNC:HGNC:13728}; Synonyms=GPR97, PGR26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okaze H., Hayashi A., Kozuma S., Saito T.;
RT "A member of G-protein coupled receptor family.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12435584; DOI=10.1016/s0014-5793(02)03574-3;
RA Fredriksson R., Lagerstroem M.C., Hoeglund P.J., Schioeth H.B.;
RT "Novel human G protein-coupled receptors with long N-terminals containing
RT GPS domains and Ser/Thr-rich regions.";
RL FEBS Lett. 531:407-414(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PROTEIN SEQUENCE OF 21-35.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-387.
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22575658; DOI=10.1016/j.febslet.2012.03.014;
RA Gupte J., Swaminath G., Danao J., Tian H., Li Y., Wu X.;
RT "Signaling property study of adhesion G-protein-coupled receptors.";
RL FEBS Lett. 586:1214-1219(2012).
RN [8]
RP TISSUE SPECIFICITY, AND FUNCTION.
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).
RN [9]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
CC -!- FUNCTION: Orphan receptor that regulates migration of lymphatic
CC endothelial cells in vitro via the small GTPases RhoA and CDC42
CC (PubMed:24178298). Regulates B-cell development (By similarity). Seems
CC to signal through G-alpha(q)-proteins (PubMed:22575658).
CC {ECO:0000250|UniProtKB:Q8R0T6, ECO:0000269|PubMed:22575658,
CC ECO:0000269|PubMed:24178298}.
CC -!- INTERACTION:
CC Q86Y34; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-17979264, EBI-3904417;
CC Q86Y34; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-17979264, EBI-12003442;
CC Q86Y34; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-17979264, EBI-12019274;
CC Q86Y34; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-17979264, EBI-6166686;
CC Q86Y34; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-17979264, EBI-2820517;
CC Q86Y34; P60201-2: PLP1; NbExp=3; IntAct=EBI-17979264, EBI-12188331;
CC Q86Y34; Q9NS64: RPRM; NbExp=3; IntAct=EBI-17979264, EBI-1052363;
CC Q86Y34; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-17979264, EBI-8652744;
CC Q86Y34; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-17979264, EBI-10329860;
CC Q86Y34; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-17979264, EBI-10243654;
CC Q86Y34; O00526: UPK2; NbExp=3; IntAct=EBI-17979264, EBI-10179682;
CC Q86Y34; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-17979264, EBI-12190699;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22575658};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in cultured primary dermal lymphatic
CC endothelial cells. {ECO:0000269|PubMed:24178298}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18774.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB049169; BAC67700.1; -; mRNA.
DR EMBL; AY140959; AAN46673.1; -; mRNA.
DR EMBL; AK172801; BAD18774.1; ALT_FRAME; mRNA.
DR EMBL; BC064508; AAH64508.1; -; mRNA.
DR EMBL; AY255601; AAO85113.1; -; mRNA.
DR CCDS; CCDS10786.1; -.
DR RefSeq; NP_001295289.1; NM_001308360.1.
DR RefSeq; NP_740746.4; NM_170776.4.
DR PDB; 7D76; EM; 3.10 A; R=14-549.
DR PDB; 7D77; EM; 2.90 A; R=14-549.
DR PDBsum; 7D76; -.
DR PDBsum; 7D77; -.
DR AlphaFoldDB; Q86Y34; -.
DR SMR; Q86Y34; -.
DR BioGRID; 128799; 12.
DR IntAct; Q86Y34; 12.
DR STRING; 9606.ENSP00000332900; -.
DR ChEMBL; CHEMBL3559707; -.
DR GuidetoPHARMACOLOGY; 188; -.
DR MEROPS; P02.023; -.
DR GlyGen; Q86Y34; 4 sites.
DR iPTMnet; Q86Y34; -.
DR PhosphoSitePlus; Q86Y34; -.
DR BioMuta; ADGRG3; -.
DR DMDM; 50400483; -.
DR EPD; Q86Y34; -.
DR jPOST; Q86Y34; -.
DR MassIVE; Q86Y34; -.
DR PaxDb; Q86Y34; -.
DR PeptideAtlas; Q86Y34; -.
DR PRIDE; Q86Y34; -.
DR ProteomicsDB; 70366; -.
DR Antibodypedia; 15147; 163 antibodies from 27 providers.
DR DNASU; 222487; -.
DR Ensembl; ENST00000333493.9; ENSP00000332900.4; ENSG00000182885.17.
DR GeneID; 222487; -.
DR KEGG; hsa:222487; -.
DR MANE-Select; ENST00000333493.9; ENSP00000332900.4; NM_170776.5; NP_740746.4.
DR UCSC; uc002emh.4; human.
DR CTD; 222487; -.
DR DisGeNET; 222487; -.
DR GeneCards; ADGRG3; -.
DR HGNC; HGNC:13728; ADGRG3.
DR HPA; ENSG00000182885; Tissue enriched (bone).
DR MIM; 618441; gene.
DR neXtProt; NX_Q86Y34; -.
DR OpenTargets; ENSG00000182885; -.
DR PharmGKB; PA28936; -.
DR VEuPathDB; HostDB:ENSG00000182885; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000154285; -.
DR InParanoid; Q86Y34; -.
DR OMA; TLFKGPQ; -.
DR OrthoDB; 501343at2759; -.
DR PhylomeDB; Q86Y34; -.
DR TreeFam; TF321769; -.
DR PathwayCommons; Q86Y34; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q86Y34; -.
DR BioGRID-ORCS; 222487; 11 hits in 1071 CRISPR screens.
DR ChiTaRS; ADGRG3; human.
DR GeneWiki; GPR97; -.
DR GenomeRNAi; 222487; -.
DR Pharos; Q86Y34; Tchem.
DR PRO; PR:Q86Y34; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q86Y34; protein.
DR Bgee; ENSG00000182885; Expressed in blood and 99 other tissues.
DR ExpressionAtlas; Q86Y34; baseline and differential.
DR Genevisible; Q86Y34; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
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; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0032792; P:negative regulation of CREB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP: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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 21..549
FT /note="Adhesion G protein-coupled receptor G3"
FT /id="PRO_0000012889"
FT TOPO_DOM 21..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 308..328
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..347
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 375..395
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..434
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 435..455
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 489..509
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..513
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 514..534
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 212..261
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 430
FT /note="A -> T (in dbSNP:rs2290178)"
FT /id="VAR_055927"
FT CONFLICT 8
FT /note="G -> W (in Ref. 2; AAN46673)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="P -> S (in Ref. 3; BAD18774)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="K -> R (in Ref. 3; BAD18774)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="I -> V (in Ref. 3; BAD18774)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="A -> V (in Ref. 4; AAH64508)"
FT /evidence="ECO:0000305"
FT HELIX 264..296
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 305..328
FT /evidence="ECO:0007829|PDB:7D77"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 335..367
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 378..399
FT /evidence="ECO:0007829|PDB:7D77"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:7D77"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 436..460
FT /evidence="ECO:0007829|PDB:7D77"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 472..494
FT /evidence="ECO:0007829|PDB:7D77"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:7D77"
FT HELIX 503..524
FT /evidence="ECO:0007829|PDB:7D77"
SQ SEQUENCE 549 AA; 60861 MW; C9AB0D95B2F26DDA CRC64;
MATPRGLGAL LLLLLLPTSG QEKPTEGPRN TCLGSNNMYD IFNLNDKALC FTKCRQSGSD
SCNVENLQRY WLNYEAHLMK EGLTQKVNTP FLKALVQNLS TNTAEDFYFS LEPSQVPRQV
MKDEDKPPDR VRLPKSLFRS LPGNRSVVRL AVTILDIGPG TLFKGPRLGL GDGSGVLNNR
LVGLSVGQMH VTKLAEPLEI VFSHQRPPPN MTLTCVFWDV TKGTTGDWSS EGCSTEVRPE
GTVCCCDHLT FFALLLRPTL DQSTVHILTR ISQAGCGVSM IFLAFTIILY AFLRLSRERF
KSEDAPKIHV ALGGSLFLLN LAFLVNVGSG SKGSDAACWA RGAVFHYFLL CAFTWMGLEA
FHLYLLAVRV FNTYFGHYFL KLSLVGWGLP ALMVIGTGSA NSYGLYTIRD RENRTSLELC
WFREGTTMYA LYITVHGYFL ITFLFGMVVL ALVVWKIFTL SRATAVKERG KNRKKVLTLL
GLSSLVGVTW GLAIFTPLGL STVYIFALFN SLQGVFICCW FTILYLPSQS TTVSSSTARL
DQAHSASQE
