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Protein

Adhesion G-protein coupled receptor G1

Gene

Adgrg1

Organism
Rattus norvegicus (Rat)
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. Binding to the COL3A1 ligand inhibits neuronal migration and activates the RhoA pathway by coupling to GNA13 and possibly GNA12. Plays a role in the maintenance of hematopoietic stem cells and/or leukemia stem cells in bone marrow niche. Plays an essential role in testis development. Plays a critical role in tumourigenesis.By similarity

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Cell adhesion, Differentiation, Neurogenesis

Keywords - Ligandi

Heparin-binding

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
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:Gpr56
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628617. 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25By similarityAdd BLAST25
ChainiPRO_000001288526 – 687Adhesion G-protein coupled receptor G1By similarityAdd BLAST662
ChainiPRO_000042309626 – ?382ADGRG1 N-terminal fragmentBy similarityAdd BLAST357
ChainiPRO_0000423097?383 – 687ADGRG1 C-terminal fragmentAdd BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...)Sequence analysis1
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi171N-linked (GlcNAc...)Sequence analysis1
Glycosylationi234N-linked (GlcNAc...)Sequence analysis1
Glycosylationi303N-linked (GlcNAc...)Sequence analysis1
Glycosylationi324N-linked (GlcNAc...)Sequence analysis1
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked. Shedding to yield the secreted ADGRG1 N-terminal fragment seems also to involve metalloprotease(s).1 Publication
N-glycosylated. Contains sialic acid residues.By similarity
Ubiquitinated. Undergoes polyubiquitination upon activation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei382 – 383Cleavage; by autolysisBy similarity2

Keywords - PTMi

Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8K3V3.
PRIDEiQ8K3V3.

PTM databases

iPTMnetiQ8K3V3.
PhosphoSitePlusiQ8K3V3.
UniCarbKBiQ8K3V3.

Interactioni

Subunit structurei

Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment (ADGRG1 NT) and the membrane-bound C-terminal fragment (ADGRG1 CT) predominantly remain associated and non-covalently linked. 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. Interacts with TGM2; TGM2 probably is not a ADGRG1 ligand and the interaction is reported controversial. 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. Interacts with heparin; leading to the reduction of ADGRG1 shedding.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020921.

Structurei

3D structure databases

ProteinModelPortaliQ8K3V3.
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

Contains 1 GPS domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
HOGENOMiHOG000015136.
HOVERGENiHBG051814.
InParanoidiQ8K3V3.
PhylomeDBiQ8K3V3.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR003910. GPR1/GPR3/GPR5.
IPR000203. GPS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01422. GPR56ORPHANR.
SMARTiSM00303. GPS. 1 hit.
[Graphical view]
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8K3V3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVQVLLQMV YFLLTLLFLV QGAHGASPRE DFRFCGQRNQ TQQSTLHYDQ
60 70 80 90 100
TSEPHIFVWN TDESLTIRAP FPAAPDIPYF FPEPRGLYHF CLYWSRHTGR
110 120 130 140 150
LHLRYGKNDY LLSSRASNLL CYRKQEESLK QGAPLVATSV SSWQSPQNTS
160 170 180 190 200
LPGAPSFIFS FHNAPHKVSH NASVNMCDLK KELQLLSKFL QHPHKASKRP
210 220 230 240 250
SAAFISQQLQ NLESKLTSVS FLGDTLSFEE NRVNATVWKL PPTAGLEDLQ
260 270 280 290 300
IHSQQEEEQS EVQAYSVLLP RAVFQQTRGR RRDAAKRLLV VDFSSQALFQ
310 320 330 340 350
DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV
360 370 380 390 400
EDPASSSTGS WSSEGCETVS RDTQTSCLCN HLTYFAVLMV SSMEVEATHK
410 420 430 440 450
HYLTLLSYVG CVISALACVF TIAAYLCTRR KSRDYTIKVH MNLLLAVFLL
460 470 480 490 500
DVSFLLSEPV ALMGSEAACR TSAMFLHFSL LACLSWMGLE GYNLYRLVVE
510 520 530 540 550
VFGTYVPGYL LKLSTVGWGF PVFLVTLVAL VDVNNYGPII LAVRRTPDHV
560 570 580 590 600
IYPSMCWIRD SVVSYVTNLG LFSLVFLFNM AMLATMVVQI LRLRPHSQKW
610 620 630 640 650
PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVIIYLFSIM TSFQGFLIFL
660 670 680
WYWSMRFQAQ GGPSPLKNNS DSAKLPISSG STSSSRI
Length:687
Mass (Da):77,252
Last modified:October 1, 2002 - v1
Checksum:i79C8A64FC572856D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529886 mRNA. Translation: AAM94855.1.
UniGeneiRn.1677.

Genome annotation databases

UCSCiRGD:628617. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF529886 mRNA. Translation: AAM94855.1.
UniGeneiRn.1677.

3D structure databases

ProteinModelPortaliQ8K3V3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000020921.

Protein family/group databases

MEROPSiP02.008.
GPCRDBiSearch...

PTM databases

iPTMnetiQ8K3V3.
PhosphoSitePlusiQ8K3V3.
UniCarbKBiQ8K3V3.

Proteomic databases

PaxDbiQ8K3V3.
PRIDEiQ8K3V3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:628617. rat.

Organism-specific databases

RGDi628617. Adgrg1.

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
HOGENOMiHOG000015136.
HOVERGENiHBG051814.
InParanoidiQ8K3V3.
PhylomeDBiQ8K3V3.

Miscellaneous databases

PROiQ8K3V3.

Family and domain databases

InterProiIPR017981. GPCR_2-like.
IPR000832. GPCR_2_secretin-like.
IPR003910. GPR1/GPR3/GPR5.
IPR000203. GPS.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01422. GPR56ORPHANR.
SMARTiSM00303. GPS. 1 hit.
[Graphical view]
PROSITEiPS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGRG1_RAT
AccessioniPrimary (citable) accession number: Q8K3V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

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.