AGRG1_MOUSE
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 03-AUG-2022, entry version 158.
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; 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 -!- 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; 1.
DR STRING; 10090.ENSMUSP00000137520; -.
DR MEROPS; P02.008; -.
DR GlyConnect; 2362; 3 N-Linked glycans (3 sites).
DR GlyGen; Q8K209; 7 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q8K209; -.
DR PhosphoSitePlus; Q8K209; -.
DR MaxQB; Q8K209; -.
DR PaxDb; Q8K209; -.
DR PeptideAtlas; Q8K209; -.
DR PRIDE; Q8K209; -.
DR ProteomicsDB; 285772; -.
DR Antibodypedia; 15123; 331 antibodies from 34 providers.
DR DNASU; 14766; -.
DR Ensembl; ENSMUST00000093271; ENSMUSP00000090959; ENSMUSG00000031785.
DR Ensembl; ENSMUST00000179619; ENSMUSP00000137520; ENSMUSG00000031785.
DR Ensembl; ENSMUST00000212660; ENSMUSP00000148644; ENSMUSG00000031785.
DR GeneID; 14766; -.
DR KEGG; mmu:14766; -.
DR UCSC; uc009mxl.2; mouse.
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; NQKWPHV; -.
DR OrthoDB; 501343at2759; -.
DR PhylomeDB; Q8K209; -.
DR TreeFam; TF321769; -.
DR BioGRID-ORCS; 14766; 2 hits in 73 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 269 other tissues.
DR ExpressionAtlas; Q8K209; baseline and differential.
DR Genevisible; Q8K209; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0097451; C:glial limiting end-foot; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; 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 InterPro; IPR040950; GAIN_A.
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 InterPro; IPR040679; PLL.
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.
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
