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Protein

Adhesion G-protein coupled receptor G1

Gene

Adgrg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor involved in cell adhesion and probably in cell-cell interactions. Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells. Receptor for collagen III/COL3A1 in the developing brain and involved in regulation of cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination (PubMed:21768377). Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12 (By similarity). Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche (PubMed:23478665). Plays a critical role in tumourigenesis (By similarity). Plays essential role in testis development (PubMed:20981830).By similarity7 Publications

Enzyme regulationi

ADGRG1 NT is proposed to inhibit receptor signaling; its interactions with extracellular ligands and /or homophilic ADGRG1 NT interactions may relieve the inhibition. Following ligand binding to the N-terminal fragment, the N-terminal fragment is released from the seven-transmembrane C-terminal fragment to unveil a new N-terminal stalk, which then stimulates G-protein-dependent signaling activity.By similarity

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • extracellular matrix binding Source: UniProtKB
  • G-protein coupled receptor activity Source: UniProtKB
  • heparin binding Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • brain development Source: MGI
  • cell adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell surface receptor signaling pathway Source: InterPro
  • cerebral cortex radial glia guided migration Source: UniProtKB
  • cerebral cortex regionalization Source: MGI
  • layer formation in cerebral cortex Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of neuron migration Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of neural precursor cell proliferation Source: MGI
  • positive regulation of Rho protein signal transduction Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • Rho protein signal transduction Source: UniProtKB
  • seminiferous tubule development Source: UniProtKB
  • vascular endothelial growth factor production Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, G-protein coupled receptor, Heparin-binding, Receptor, Transducer
Biological processCell adhesion, Differentiation, Neurogenesis

Protein family/group databases

MEROPSiP02.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G-protein coupled receptor G1
Alternative name(s):
G-protein coupled receptor 56
Serpentine receptor cyt28
Cleaved into the following 2 chains:
ADGRG1 N-terminal fragment
Short name:
ADGRG1 NT
Alternative name(s):
GPR56 N-terminal fragment
Short name:
GPR56 NT
Short name:
GPR56(N)
GPR56 extracellular subunit
GPR56 subunit alpha
ADGRG1 C-terminal fragment
Short name:
ADGRG1-CT
Alternative name(s):
GPR56 C-terminal fragment
Short name:
GPR56 CT
Short name:
GPR56(C)
GPR56 seven-transmembrane subunit
Short name:
GPR56 7TM
GPR56 subunit beta
Gene namesi
Name:Adgrg1Imported
Synonyms:Cyt28, Gpr56
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1340051. Adgrg1.

Subcellular locationi

ADGRG1 N-terminal fragment :
  • Secreted By similarity
ADGRG1 C-terminal fragment :
  • Membrane raft By similarity

  • Note: Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 402ExtracellularSequence analysisAdd BLAST377
Transmembranei403 – 423Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini424 – 442CytoplasmicSequence analysisAdd BLAST19
Transmembranei443 – 463Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini464 – 471ExtracellularSequence analysis8
Transmembranei472 – 492Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini493 – 512CytoplasmicSequence analysisAdd BLAST20
Transmembranei513 – 533Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini534 – 570ExtracellularSequence analysisAdd BLAST37
Transmembranei571 – 591Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini592 – 603CytoplasmicSequence analysisAdd BLAST12
Transmembranei604 – 624Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini625 – 630ExtracellularSequence analysis6
Transmembranei631 – 651Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini652 – 687CytoplasmicSequence analysisAdd BLAST36

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Cobblestone-like cortical malformation with defective pial basement membrane (BM), abnormal anchorage of radial glial endfeet, mislocalized Cajal-Retzius cells and neuronal overmigration. Severe malformation of the rostral cerebellum that develops perinatally. Granule cells from the rostral region show loss of adhesion to extracellular matrix molecules of the pial basement membrane. In ADGRG1 knockout mice, neurons overmigrate through breached pial basement membrane or undermigrate forming irregular cortical layers. Deficient mice shown disruption of seminiferous tubule formation and increased sterility (PubMed:20981830).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38R → Q or W: Reduced cell surface localization. 2 Publications1
Mutagenesisi88Y → C: Reduced cell surface localization. 2 Publications1
Mutagenesisi91C → S: Reduced cell surface localization. 2 Publications1
Mutagenesisi346C → S: Abolishes proteolytic cleavage and cell surface localization. 1 Publication1
Mutagenesisi349W → S: Abolishes proteolytic cleavage and cell surface localization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25By similarityAdd BLAST25
ChainiPRO_000001288226 – 687Adhesion G-protein coupled receptor G1Add BLAST662
ChainiPRO_000043650526 – ?382ADGRG1 N-terminal fragmentBy similarityAdd BLAST357
ChainiPRO_0000436506?383 – 687ADGRG1 C-terminal fragmentBy similarityAdd BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi148N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi171N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi234N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi303N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi324N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi341N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membroune-bound C-terminal fragment predominantly remain associated and non-covalently linked.1 Publication
N-glycosylated. The secreted ADGRG1 N-terminal fragment is heavily glycosylated.1 Publication
Ubiquitinated. Undergoes polyubiquitination upon activation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei382 – 383Cleavage; by autolysis2

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8K209.
PaxDbiQ8K209.
PeptideAtlasiQ8K209.
PRIDEiQ8K209.

PTM databases

iPTMnetiQ8K209.
PhosphoSitePlusiQ8K209.

Expressioni

Tissue specificityi

Expressed in neural progenitor cells in fetal forbrain. Expressed in migrating neurons. Expressed in radial glial endfeet (at protein level) (PubMed:21768377). Expressed in peritubular myoid cells, Sertoli cells, and germ cells of the testis (PubMed:20981830).2 Publications

Gene expression databases

BgeeiENSMUSG00000031785.
CleanExiMM_GPR56.
ExpressionAtlasiQ8K209. baseline and differential.
GenevisibleiQ8K209. MM.

Interactioni

Subunit structurei

Predominantly non-covalently linked heterodimer of the N-terminal and the C-terminal fragment. ADGRG1 NT self-associates in a trans-trans manner; the homophilic interaction enhances receptor signaling. ADGRG1 CT interacts with ARRB2; the interaction is impaired by ADGRG1 NT. Part of a GPCR-tetraspanin complex at least consisting of ADGRG1, CD81, eventually CD9, and GNA11 in which CD81 is enhancing the association of ADGRG1 with GNA11 (By similarity). Interacts with heparin; leading to the reduction of ADGRG1 shedding (PubMed:27068534).By similarity1 Publication

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ8K209. 1 interactor.
STRINGi10090.ENSMUSP00000090959.

Structurei

Secondary structure

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 40Combined sources10
Beta strandi45 – 50Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi56 – 60Combined sources5
Beta strandi62 – 71Combined sources10
Beta strandi86 – 95Combined sources10
Turni96 – 99Combined sources4
Beta strandi100 – 105Combined sources6
Beta strandi108 – 114Combined sources7
Beta strandi124 – 126Combined sources3
Beta strandi136 – 145Combined sources10
Beta strandi155 – 160Combined sources6
Helixi176 – 191Combined sources16
Helixi193 – 195Combined sources3
Beta strandi196 – 198Combined sources3
Helixi202 – 218Combined sources17
Beta strandi222 – 230Combined sources9
Beta strandi233 – 239Combined sources7
Helixi242 – 246Combined sources5
Beta strandi249 – 252Combined sources4
Beta strandi259 – 269Combined sources11
Helixi271 – 274Combined sources4
Beta strandi287 – 294Combined sources8
Helixi308 – 310Combined sources3
Beta strandi311 – 317Combined sources7
Beta strandi329 – 335Combined sources7
Beta strandi343 – 350Combined sources8
Turni353 – 355Combined sources3
Beta strandi360 – 362Combined sources3
Beta strandi366 – 370Combined sources5
Beta strandi372 – 381Combined sources10
Beta strandi384 – 390Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KVMX-ray2.45A28-382[»]
B383-391[»]
ProteinModelPortaliQ8K209.
SMRiQ8K209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini343 – 394GPSPROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 33Heparin-bindingBy similarity8
Regioni190 – 200Heparin-bindingBy similarityAdd BLAST11

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128227.
HOGENOMiHOG000015136.
HOVERGENiHBG051814.
InParanoidiQ8K209.
KOiK08450.
OMAiSMCWIRD.
OrthoDBiEOG091G02U6.
PhylomeDBiQ8K209.
TreeFamiTF321769.

Family and domain databases

InterProiView protein in InterPro
IPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR003910. GPR1/GPR3/GPR5.
IPR000203. GPS.
PfamiView protein in Pfam
PF00002. 7tm_2. 1 hit.
PF01825. GPS. 1 hit.
PRINTSiPR00249. GPCRSECRETIN.
PR01422. GPR56ORPHANR.
SMARTiView protein in SMART
SM00303. GPS. 1 hit.
PROSITEiView protein in PROSITE
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K209-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ
60 70 80 90 100
SSEPHIFVWN TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR
110 120 130 140 150
LHLRYGKHDY LLSSQASRLL CFQKQEQSLK QGAPLIATSV SSWQIPQNTS
160 170 180 190 200
LPGAPSFIFS FHNAPHKVSH NASVDMCDLK KELQQLSRYL QHPQKAAKRP
210 220 230 240 250
TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL PPTAGLEDLH
260 270 280 290 300
IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ
310 320 330 340 350
DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV
360 370 380 390 400
EDPASSSTGS WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK
410 420 430 440 450
HYLTLLSYVG CVISALACVF TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL
460 470 480 490 500
DVSFLLSEPV ALTGSEAACR TSAMFLHFSL LACLSWMGLE GYNLYRLVVE
510 520 530 540 550
VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII LAVRRTPERV
560 570 580 590 600
TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW
610 620 630 640 650
PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL
660 670 680
WYWSMRFQAQ GGPSPLKNNS DSAKLPISSG STSSSRI
Length:687
Mass (Da):77,255
Last modified:October 1, 2002 - v1
Checksum:iB5315D70B66C9A9A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti643F → Y in AAF00617 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF166382 mRNA. Translation: AAF00617.1.
AK087268 mRNA. Translation: BAC39835.1.
AK133678 mRNA. Translation: BAE21780.1.
AK141886 mRNA. Translation: BAE24871.1.
AK141894 mRNA. Translation: BAE24874.1.
AK167547 mRNA. Translation: BAE39613.1.
BC034678 mRNA. Translation: AAH34678.1.
CCDSiCCDS22553.1.
RefSeqiNP_001185823.1. NM_001198894.1.
NP_061370.2. NM_018882.3.
XP_006530755.1. XM_006530692.2.
XP_006530756.1. XM_006530693.2.
XP_006530757.1. XM_006530694.2.
XP_006530758.1. XM_006530695.2.
XP_006530759.1. XM_006530696.3.
XP_006530760.1. XM_006530697.2.
UniGeneiMm.290834.

Genome annotation databases

EnsembliENSMUST00000093271; ENSMUSP00000090959; ENSMUSG00000031785.
ENSMUST00000179619; ENSMUSP00000137520; ENSMUSG00000031785.
ENSMUST00000212660; ENSMUSP00000148644; ENSMUSG00000031785.
GeneIDi14766.
KEGGimmu:14766.
UCSCiuc009mxl.2. mouse.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAGRG1_MOUSE
AccessioniPrimary (citable) accession number: Q8K209
Secondary accession number(s): Q3UR17, Q9QZT2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: July 5, 2017
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families