ID   AGRG1_MOUSE             Reviewed;         687 AA.
AC   Q8K209; Q3UR17; Q9QZT2;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Adhesion G-protein coupled receptor G1;
DE   AltName: Full=G-protein coupled receptor 56;
DE   AltName: Full=Serpentine receptor cyt28;
DE   Contains:
DE     RecName: Full=ADGRG1 N-terminal fragment;
DE              Short=ADGRG1 NT;
DE     AltName: Full=GPR56 N-terminal fragment;
DE              Short=GPR56 NT;
DE              Short=GPR56(N);
DE     AltName: Full=GPR56 extracellular subunit;
DE     AltName: Full=GPR56 subunit alpha;
DE   Contains:
DE     RecName: Full=ADGRG1 C-terminal fragment;
DE              Short=ADGRG1-CT;
DE     AltName: Full=GPR56 C-terminal fragment;
DE              Short=GPR56 CT;
DE              Short=GPR56(C);
DE     AltName: Full=GPR56 seven-transmembrane subunit;
DE              Short=GPR56 7TM;
DE     AltName: Full=GPR56 subunit beta;
DE   Flags: Precursor;
GN   Name=Adgrg1 {ECO:0000312|MGI:MGI:1340051}; Synonyms=Cyt28, Gpr56;
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 [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A.,
RA   Kingsley P.D., Sykes S., Palis J., Lemischka I.R.;
RT   "Identification of novel hematopoietic stem cell regulatory genes.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Lung, Pituitary, Placenta, and Spinal ganglion;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-39; ASN-148; ASN-171;
RP   ASN-234; ASN-303; ASN-324 AND ASN-341, AND MUTAGENESIS OF ARG-38; TYR-88;
RP   CYS-91; CYS-346 AND TRP-349.
RX   PubMed=17576745; DOI=10.1093/hmg/ddm144;
RA   Jin Z., Tietjen I., Bu L., Liu-Yesucevitz L., Gaur S.K., Walsh C.A.,
RA   Piao X.;
RT   "Disease-associated mutations affect GPR56 protein trafficking and cell
RT   surface expression.";
RL   Hum. Mol. Genet. 16:1972-1985(2007).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18509043; DOI=10.1523/jneurosci.0853-08.2008;
RA   Li S., Jin Z., Koirala S., Bu L., Xu L., Hynes R.O., Walsh C.A., Corfas G.,
RA   Piao X.;
RT   "GPR56 regulates pial basement membrane integrity and cortical
RT   lamination.";
RL   J. Neurosci. 28:5817-5826(2008).
RN   [6]
RP   FUNCTION.
RX   PubMed=18378689; DOI=10.1074/jbc.m708919200;
RA   Iguchi T., Sakata K., Yoshizaki K., Tago K., Mizuno N., Itoh H.;
RT   "Orphan G protein-coupled receptor GPR56 regulates neural progenitor cell
RT   migration via a G alpha 12/13 and Rho pathway.";
RL   J. Biol. Chem. 283:14469-14478(2008).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19515912; DOI=10.1523/jneurosci.1182-09.2009;
RA   Koirala S., Jin Z., Piao X., Corfas G.;
RT   "GPR56-regulated granule cell adhesion is essential for rostral cerebellar
RT   development.";
RL   J. Neurosci. 29:7439-7449(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20981830; DOI=10.1002/dvdy.22468;
RA   Chen G., Yang L., Begum S., Xu L.;
RT   "GPR56 is essential for testis development and male fertility in mice.";
RL   Dev. Dyn. 239:3358-3367(2010).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND LIGAND-BINDING.
RX   PubMed=21768377; DOI=10.1073/pnas.1104821108;
RA   Luo R., Jeong S.J., Jin Z., Strokes N., Li S., Piao X.;
RT   "G protein-coupled receptor 56 and collagen III, a receptor-ligand pair,
RT   regulates cortical development and lamination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12925-12930(2011).
RN   [11]
RP   LIGAND-BINDING, AND MUTAGENESIS OF ARG-38; TYR-88 AND CYS-91.
RX   PubMed=22238662; DOI=10.1371/journal.pone.0029818;
RA   Luo R., Jin Z., Deng Y., Strokes N., Piao X.;
RT   "Disease-associated mutations prevent GPR56-collagen III interaction.";
RL   PLoS ONE 7:E29818-E29818(2012).
RN   [12]
RP   FUNCTION.
RX   PubMed=23478665; DOI=10.1038/leu.2013.75;
RA   Saito Y., Kaneda K., Suekane A., Ichihara E., Nakahata S., Yamakawa N.,
RA   Nagai K., Mizuno N., Kogawa K., Miura I., Itoh H., Morishita K.;
RT   "Maintenance of the hematopoietic stem cell pool in bone marrow niches by
RT   EVI1-regulated GPR56.";
RL   Leukemia 27:1637-1649(2013).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24531968; DOI=10.1126/science.1244392;
RA   Bae B.I., Tietjen I., Atabay K.D., Evrony G.D., Johnson M.B., Asare E.,
RA   Wang P.P., Murayama A.Y., Im K., Lisgo S.N., Overman L., Sestan N.,
RA   Chang B.S., Barkovich A.J., Grant P.E., Topcu M., Politsky J., Okano H.,
RA   Piao X., Walsh C.A.;
RT   "Evolutionarily dynamic alternative splicing of GPR56 regulates regional
RT   cerebral cortical patterning.";
RL   Science 343:764-768(2014).
RN   [14]
RP   INTERACTION WITH HEPARIN.
RX   PubMed=27068534; DOI=10.1242/jcs.174458;
RA   Chiang N.Y., Chang G.W., Huang Y.S., Peng Y.M., Hsiao C.C., Kuo M.L.,
RA   Lin H.H.;
RT   "Heparin interacts with adhesion-GPCR GPR56/ADGRG1, reduces receptor
RT   shedding, and promotes cell adhesion and motility.";
RL   J. Cell Sci. 129:2156-2169(2016).
CC   -!- FUNCTION: Receptor involved in cell adhesion and probably in cell-cell
CC       interactions. Mediates cell matrix adhesion in developing neurons and
CC       hematopoietic stem cells. Receptor for collagen III/COL3A1 in the
CC       developing brain and involved in regulation of cortical development,
CC       specifically in maintenance of the pial basement membrane integrity and
CC       in cortical lamination (PubMed:21768377). Binding to the COL3A1 ligand
CC       inhibits neuronal migration and activates the RhoA pathway by coupling
CC       to GNA13 and possibly GNA12 (By similarity). Plays a role in the
CC       maintenance of hematopoietic stem cells and/or leukemia stem cells in
CC       bone marrow niche (PubMed:23478665). Plays a critical role in
CC       tumourigenesis (By similarity). Plays essential role in testis
CC       development (PubMed:20981830). {ECO:0000250|UniProtKB:Q9Y653,
CC       ECO:0000269|PubMed:18378689, ECO:0000269|PubMed:18509043,
CC       ECO:0000269|PubMed:19515912, ECO:0000269|PubMed:20981830,
CC       ECO:0000269|PubMed:21768377, ECO:0000269|PubMed:23478665,
CC       ECO:0000269|PubMed:24531968}.
CC   -!- ACTIVITY REGULATION: ADGRG1 NT is proposed to inhibit receptor
CC       signaling; its interactions with extracellular ligands and /or
CC       homophilic ADGRG1 NT interactions may relieve the inhibition. Following
CC       ligand binding to the N-terminal fragment, the N-terminal fragment is
CC       released from the seven-transmembrane C-terminal fragment to unveil a
CC       new N-terminal stalk, which then stimulates G-protein-dependent
CC       signaling activity. The N-terminal stalk has also been shown to be
CC       dispensable for at least some G-protein-dependent signaling.
CC       {ECO:0000250|UniProtKB:Q9Y653}.
CC   -!- SUBUNIT: Predominantly non-covalently linked heterodimer of the N-
CC       terminal and the C-terminal fragment. ADGRG1 NT self-associates in a
CC       trans-trans manner; the homophilic interaction enhances receptor
CC       signaling. ADGRG1 CT interacts with ARRB2; the interaction is impaired
CC       by ADGRG1 NT. Part of a GPCR-tetraspanin complex at least consisting of
CC       ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the
CC       association of ADGRG1 with GNA11 (By similarity). Interacts with
CC       heparin; leading to the reduction of ADGRG1 shedding (PubMed:27068534).
CC       Interacts with COL3A1 (By similarity). {ECO:0000250|UniProtKB:Q9Y653,
CC       ECO:0000269|PubMed:27068534}.
CC   -!- INTERACTION:
CC       Q8K209; Q80TR1: Adgrl1; NbExp=2; IntAct=EBI-6856929, EBI-770649;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17576745,
CC       ECO:0000269|PubMed:22238662}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [ADGRG1 N-terminal fragment]: Secreted
CC       {ECO:0000250|UniProtKB:Q9Y653}.
CC   -!- SUBCELLULAR LOCATION: [ADGRG1 C-terminal fragment]: Membrane raft
CC       {ECO:0000250|UniProtKB:Q9Y653}. Note=Interaction with its ligand COL3A1
CC       leads to the release of ADGRG1 NT from the membrane and triggers the
CC       association of ADGRG1 CT with lipid rafts.
CC       {ECO:0000250|UniProtKB:Q9Y653}.
CC   -!- TISSUE SPECIFICITY: Expressed in neural progenitor cells in fetal
CC       forbrain. Expressed in migrating neurons. Expressed in radial glial
CC       endfeet (at protein level) (PubMed:21768377). Expressed in peritubular
CC       myoid cells, Sertoli cells, and germ cells of the testis
CC       (PubMed:20981830). {ECO:0000269|PubMed:20981830,
CC       ECO:0000269|PubMed:21768377}.
CC   -!- PTM: Autoproteolytically cleaved into 2 fragments; the large
CC       extracellular N-terminal fragment and the membroune-bound C-terminal
CC       fragment predominantly remain associated and non-covalently linked.
CC       {ECO:0000269|PubMed:22238662}.
CC   -!- PTM: N-glycosylated. The secreted ADGRG1 N-terminal fragment is heavily
CC       glycosylated. {ECO:0000269|PubMed:17576745}.
CC   -!- PTM: Ubiquitinated. Undergoes polyubiquitination upon activation.
CC       {ECO:0000250|UniProtKB:Q9Y653}.
CC   -!- DISRUPTION PHENOTYPE: Cobblestone-like cortical malformation with
CC       defective pial basement membrane (BM), abnormal anchorage of radial
CC       glial endfeet, mislocalized Cajal-Retzius cells and neuronal
CC       overmigration. Severe malformation of the rostral cerebellum that
CC       develops perinatally. Granule cells from the rostral region show loss
CC       of adhesion to extracellular matrix molecules of the pial basement
CC       membrane. In ADGRG1 knockout mice, neurons overmigrate through breached
CC       pial basement membrane or undermigrate forming irregular cortical
CC       layers. Deficient mice shown disruption of seminiferous tubule
CC       formation and increased sterility (PubMed:20981830).
CC       {ECO:0000269|PubMed:18509043, ECO:0000269|PubMed:20981830,
CC       ECO:0000269|PubMed:24531968}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF166382; AAF00617.1; -; mRNA.
DR   EMBL; AK087268; BAC39835.1; -; mRNA.
DR   EMBL; AK133678; BAE21780.1; -; mRNA.
DR   EMBL; AK141886; BAE24871.1; -; mRNA.
DR   EMBL; AK141894; BAE24874.1; -; mRNA.
DR   EMBL; AK167547; BAE39613.1; -; mRNA.
DR   EMBL; BC034678; AAH34678.1; -; mRNA.
DR   CCDS; CCDS22553.1; -.
DR   RefSeq; NP_001185823.1; NM_001198894.1.
DR   RefSeq; NP_061370.2; NM_018882.3.
DR   RefSeq; XP_006530755.1; XM_006530692.2.
DR   RefSeq; XP_006530756.1; XM_006530693.2.
DR   RefSeq; XP_006530757.1; XM_006530694.2.
DR   RefSeq; XP_006530758.1; XM_006530695.2.
DR   RefSeq; XP_006530759.1; XM_006530696.3.
DR   RefSeq; XP_006530760.1; XM_006530697.2.
DR   PDB; 5KVM; X-ray; 2.45 A; A=28-382, B=383-391.
DR   PDBsum; 5KVM; -.
DR   AlphaFoldDB; Q8K209; -.
DR   SMR; Q8K209; -.
DR   IntAct; Q8K209; 2.
DR   MINT; Q8K209; -.
DR   STRING; 10090.ENSMUSP00000137520; -.
DR   MEROPS; P02.008; -.
DR   GlyConnect; 2362; 3 N-Linked glycans (3 sites).
DR   GlyCosmos; Q8K209; 7 sites, 3 glycans.
DR   GlyGen; Q8K209; 8 sites, 3 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K209; -.
DR   PhosphoSitePlus; Q8K209; -.
DR   SwissPalm; Q8K209; -.
DR   MaxQB; Q8K209; -.
DR   PaxDb; 10090-ENSMUSP00000137520; -.
DR   PeptideAtlas; Q8K209; -.
DR   ProteomicsDB; 285772; -.
DR   Antibodypedia; 15123; 365 antibodies from 34 providers.
DR   DNASU; 14766; -.
DR   Ensembl; ENSMUST00000093271.8; ENSMUSP00000090959.7; ENSMUSG00000031785.17.
DR   Ensembl; ENSMUST00000179619.9; ENSMUSP00000137520.2; ENSMUSG00000031785.17.
DR   Ensembl; ENSMUST00000212660.2; ENSMUSP00000148644.2; ENSMUSG00000031785.17.
DR   GeneID; 14766; -.
DR   KEGG; mmu:14766; -.
DR   UCSC; uc009mxl.2; mouse.
DR   AGR; MGI:1340051; -.
DR   CTD; 9289; -.
DR   MGI; MGI:1340051; Adgrg1.
DR   VEuPathDB; HostDB:ENSMUSG00000031785; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   GeneTree; ENSGT00940000160843; -.
DR   HOGENOM; CLU_002753_3_9_1; -.
DR   InParanoid; Q8K209; -.
DR   OMA; NLLWAIF; -.
DR   OrthoDB; 5477252at2759; -.
DR   PhylomeDB; Q8K209; -.
DR   TreeFam; TF321769; -.
DR   BioGRID-ORCS; 14766; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Adgrg1; mouse.
DR   PRO; PR:Q8K209; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8K209; Protein.
DR   Bgee; ENSMUSG00000031785; Expressed in mouth mucosa and 272 other cell types or tissues.
DR   ExpressionAtlas; Q8K209; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0097451; C:glial limiting end-foot; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR   GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0021801; P:cerebral cortex radial glia-guided migration; IMP:UniProtKB.
DR   GO; GO:0021796; P:cerebral cortex regionalization; IMP:MGI.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR   GO; GO:0021819; P:layer formation in cerebral cortex; IMP:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:2001223; P:negative regulation of neuron migration; IMP:UniProtKB.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IMP:UniProtKB.
DR   GO; GO:0070528; P:protein kinase C signaling; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0072520; P:seminiferous tubule development; IMP:UniProtKB.
DR   GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR040950; ADGRG1_GAIN_A.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR003910; GPR1/GPR3/GPR5.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR040679; PLL.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR12011:SF318; ADHESION G-PROTEIN COUPLED RECEPTOR G1; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF18619; GAIN_A; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF18587; PLL; 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.
DR   Genevisible; Q8K209; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell membrane; Developmental protein;
KW   Differentiation; G-protein coupled receptor; Glycoprotein; Heparin-binding;
KW   Membrane; Neurogenesis; Receptor; Reference proteome; Secreted; Signal;
KW   Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y653"
FT   CHAIN           26..687
FT                   /note="Adhesion G-protein coupled receptor G1"
FT                   /id="PRO_0000012882"
FT   CHAIN           26..?382
FT                   /note="ADGRG1 N-terminal fragment"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y653"
FT                   /id="PRO_0000436505"
FT   CHAIN           ?383..687
FT                   /note="ADGRG1 C-terminal fragment"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y653"
FT                   /id="PRO_0000436506"
FT   TOPO_DOM        26..402
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..442
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        464..471
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..492
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        534..570
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        571..591
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        592..603
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        625..630
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..651
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        652..687
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          343..394
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          664..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..33
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y653"
FT   BINDING         190..200
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y653"
FT   SITE            382..383
FT                   /note="Cleavage; by autolysis"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        324
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   MUTAGEN         38
FT                   /note="R->Q,W: Reduced cell surface localization."
FT                   /evidence="ECO:0000269|PubMed:17576745,
FT                   ECO:0000269|PubMed:22238662"
FT   MUTAGEN         88
FT                   /note="Y->C: Reduced cell surface localization."
FT                   /evidence="ECO:0000269|PubMed:17576745,
FT                   ECO:0000269|PubMed:22238662"
FT   MUTAGEN         91
FT                   /note="C->S: Reduced cell surface localization."
FT                   /evidence="ECO:0000269|PubMed:17576745,
FT                   ECO:0000269|PubMed:22238662"
FT   MUTAGEN         346
FT                   /note="C->S: Abolishes proteolytic cleavage and cell
FT                   surface localization."
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   MUTAGEN         349
FT                   /note="W->S: Abolishes proteolytic cleavage and cell
FT                   surface localization."
FT                   /evidence="ECO:0000269|PubMed:17576745"
FT   CONFLICT        643
FT                   /note="F -> Y (in Ref. 1; AAF00617)"
FT                   /evidence="ECO:0000305"
FT   STRAND          31..40
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          86..95
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   TURN            96..99
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          136..145
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          155..160
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           176..191
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           202..218
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          233..239
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           242..246
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          259..269
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          287..294
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          311..317
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          329..335
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          343..350
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   TURN            353..355
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          372..381
FT                   /evidence="ECO:0007829|PDB:5KVM"
FT   STRAND          384..390
FT                   /evidence="ECO:0007829|PDB:5KVM"
SQ   SEQUENCE   687 AA;  77255 MW;  B5315D70B66C9A9A CRC64;
     MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ SSEPHIFVWN
     TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR LHLRYGKHDY LLSSQASRLL
     CFQKQEQSLK QGAPLIATSV SSWQIPQNTS LPGAPSFIFS FHNAPHKVSH NASVDMCDLK
     KELQQLSRYL QHPQKAAKRP TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL
     PPTAGLEDLH IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ
     DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV EDPASSSTGS
     WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK HYLTLLSYVG CVISALACVF
     TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL DVSFLLSEPV ALTGSEAACR TSAMFLHFSL
     LACLSWMGLE GYNLYRLVVE VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII
     LAVRRTPERV TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW
     PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL WYWSMRFQAQ
     GGPSPLKNNS DSAKLPISSG STSSSRI
//