ADGRG4
entrez
139378
canonical
uniprot
Q8IZF6
canonical
ensembl
ENSG00000156920
resolver
ensp
ENSP00000377697
resolver
ensp
ENSP00000377699
resolver
genesymbol
ADGRG4
resolver
genesymbol_syn
GPR112
resolver
hgnc
HGNC:18992
resolver
uniprot
A2A2J1
resolver
uniprot
A2A2J2
resolver
uniprot
Q5EGP2
resolver
uniprot
Q86SM6
resolver
uniprot_entry
AGRG4_HUMAN
resolver
uniprot_sec
A2A2J1
resolver
uniprot_sec
A2A2J2
resolver
uniprot_sec
Q5EGP2
resolver
uniprot_sec
Q86SM6
resolver
activity_regulation
ACTIVITY REGULATION: Forms a heterodimer of 2 chains generated by proteolytic processing that remain associated through non-covalent interactions mediated by the GAIN-B domain (By similarity). In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation (PubMed:35418677). On activation, the Stachel moves into the 7 transmembrane region and adopts a twisted hook-shaped configuration that forms contacts within the receptor, leading to coupling of a G-alpha protein, which activates signaling (PubMed:35418677). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:35418677). {ECO:0000255|PROSITE-ProRule:PRU00098, ECO:0000269|PubMed:35418677}.
uniprot
proteins
amino_acid_sequence
MKEHIIYQKLYGLILMSSFIFLSDTLSLKGKKLDFFGRGDTYVSLIDTIPELSRFTACIDLVFMDDNSRYWMAFSYITNNALLGREDIDLGLAGDHQQLILYRLGKTFSIRHHLASFQWHTICLIWDGVKGKLELFLNKERILEVTDQPHNLTPHGTLFLGHFLKNESSEVKSMMRSFPGSLYYFQLWDHILENEEFMKCLDGNIVSWEEDVWLVNKIIPTVDRTLRCFVPENMTIQEKSTTVSQQIDMTTPSQITGVKPQNTAHSSTLLSQSIPIFATDYTTISYSNTTSPPLETMTAQKILKTLVDETATFAVDVLSTSSAISLPTQSISIDNTTNSMKKTKSPSSESTKTTKMVEAMATEIFQPPTPSNFLSTSRFTKNSVVSTTSAIKSQSAVTKTTSLFSTIESTSMSTTPCLKQKSTNTGALPISTAGQEFIESTAAGTVPWFTVEKTSPASTHVGTASSFPPEPVLISTAAPVDSVFPRNQTAFPLATTDMKIAFTVHSLTLPTRLIETTPAPRTAETELTSTNFQDVSLPRVEDAMSTSMSKETSSKTFSFLTSFSFTGTESVQTVIDAEATRTALTPEITLASTVAETMLSSTITGRVYTQNTPTADGHLLTLMSTRSASTSKAPESGPTSTTDEAAHLFSSNETIWTSRPDQALLASMNTTTILTFVPNENFTSAFHENTTYTEYLSATTNITPLKASPEGKGTTANDATTARYTTAVSKLTSPWFANFSIVSGTTSITNMPEFKLTTLLLKTIPMSTKPANELPLTPRETVVPSVDIISTLACIQPNFSTEESASETTQTEINGAIVFGGTTTPVPKSATTQRLNATVTRKEATSHYLMRKSTIAAVAEVSPFSTMLEVTDESAQRVTASVTVSSFPDIEKLSTPLDNKTATTEVRESWLLTKLVKTTPRSSYNEMTEMFNFNHTYVAHWTSETSEGISAGSPTSGSTHIFGEPLGASTTRISETSFSTTPTDRTATSLSDGILPPQPTAAHSSATPVPVTHMFSLPVNGSSVVAEETEVTMSEPSTLARAFSTSVLSDVSNLSSTTMTTALVPPLDQTASTTIVIVPTHGDLIRTTSEATVISVRKTSMAVPSLTETPFHSLRLSTPVTAKAETTLFSTSVDTVTPSTHTLVCSKPPPDNIPPASSTHVISTTSTPEATQPISQVEETSTYALSFPYTFSGGGVVASLATGTTETSVVDETTPSHISANKLTTSVNSHISSSATYRVHTPVSIQLVTSTSVLSSDKDQMTISLGKTPRTMEVTEMSPSKNSFISYSRGTPSLEMTDTGFPETTKISSHQTHSPSEIPLGTPSDGNLASSPTSGSTQITPTLTSSNTVGVHIPEMSTSLGKTALPSQALTITTFLCPEKESTSALPAYTPRTVEMIVNSTYVTHSVSYGQDTSFVDTTTSSSTRISNPMDINTTFSHLHSLRTQPEVTSVASFISESTQTFPESLSLSTAGLYNDGFTVLSDRITTAFSVPNVPTMLPRESSMATSTPIYQMSSLPVNVTAFTSKKVSDTPPIVITKSSKTMHPGCLKSPCTATSGPMSEMSSIPVNNSAFTPATVSSDTSTRVGLFSTLLSSVTPRTTMTMQTSTLDVTPVIYAGATSKNKMVSSAFTTEMIEAPSRITPTTFLSPTEPTLPFVKTVPTTIMAGIVTPFVGTTAFSPLSSKSTGAISSIPKTTFSPFLSATQQSSQADEATTLGILSGITNRSLSTVNSGTGVALTDTYSRITVPENMLSPTHADSLHTSFNIQVSPSLTSFKSASGPTKNVKTTTNCFSSNTRKMTSLLEKTSLTNYATSLNTPVSYPPWTPSSATLPSLTSFVYSPHSTEAEISTPKTSPPPTSQMVEFPVLGTRMTSSNTQPLLMTSWNIPTAEGSQFPISTTINVPTSNEMETETLHLVPGPLSTFTASQTGLVSKDVMAMSSIPMSGILPNHGLSENPSLSTSLRAITSTLADVKHTFEKMTTSVTPGTTLPSILSGATSGSVISKSPILTWLLSSLPSGSPPATVSNAPHVMTSSTVEVSKSTFLTSDMISAHPFTNLTTLPSATMSTILTRTIPTPTLGGITTGFPTSLPMSINVTDDIVYISTHPEASSRTTITANPRTVSHPSSFSRKTMSPSTTDHTLSVGAMPLPSSTITSSWNRIPTASSPSTLIIPKPTLDSLLNIMTTTSTVPGASFPLISTGVTYPFTATVSSPISSFFETTWLDSTPSFLSTEASTSPTATKSTVSFYNVEMSFSVFVEEPRIPITSVINEFTENSLNSIFQNSEFSLATLETQIKSRDISEEEMVMDRAILEQREGQEMATISYVPYSCVCQVIIKASSSLASSELMRKIKSKIHGNFTHGNFTQDQLTLLVNCEHVAVKKLEPGNCKADETASKYKGTYKWLLTNPTETAQTRCIKNEDGNATRFCSISINTGKSQWEKPKFKQCKLLQELPDKIVDLANITISDENAEDVAEHILNLINESPALGKEETKIIVSKISDISQCDEISMNLTHVMLQIINVVLEKQNNSASDLHEISNEILRIIERTGHKMEFSGQIANLTVAGLALAVLRGDHTFDGMAFSIHSYEEGTDPEIFLGNVPVGGILASIYLPKSLTERIPLSNLQTILFNFFGQTSLFKTKNVTKALTTYVVSASISDDMFIQNLADPVVITLQHIGGNQNYGQVHCAFWDFENNNGLGGWNSSGCKVKETNVNYTICQCDHLTHFGVLMDLSRSTVDSVNEQILALITYTGCGISSIFLGVAVVTYIAFHKLRKDYPAKILINLCTALLMLNLVFLINSWLSSFQKVGVCITAAVALHYFLLVSFTWMGLEAVHMYLALVKVFNIYIPNYILKFCLVGWGIPAIMVAITVSVKKDLYGTLSPTTPFCWIKDDSIFYISVVAYFCLIFLMNLSMFCTVLVQLNSVKSQIQKTRRKMILHDLKGTMSLTFLLGLTWGFAFFAWGPMRNFFLYLFAIFNTLQGFFIFVFHCVMKESVREQWQIHLCCGWLRLDNSSDGSSRCQIKVGYKQEGLKKIFEHKLLTPSLKSTATSSTFKSLGSAQGTPSEISFPNDDFDKDPYCSSP
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR) (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (By similarity). ADGRG4 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:35418677). May be act as sensor of mechanical forces (PubMed:37863265). {ECO:0000250|UniProtKB:Q8CJ12, ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:37863265}.
uniprot
proteins
mass_dalton
333368
uniprot
proteins
mutagenesis
MUTAGEN 2660; /note="I->A: Increased basal G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2671; /note="L->A: Increased basal G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2683; /note="V->A: Increased basal G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2747; /note="T->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2794; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2820; /note="L->A: Decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2885; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2953; /note="W->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2957; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 2971; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.; PTM: N-glycosylated. {ECO:0000269|PubMed:37863265}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12435584
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
18953328
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
35418677
uniprot
proteins
pubmed
37863265
uniprot
proteins
sequence_length
3080
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000269|PubMed:35418677}.
uniprot
proteins
transmembrane_region
TRANSMEM 2741..2766; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2778..2800; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2807..2835; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2850..2870; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2893..2918; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2938..2961; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ"; TRANSMEM 2966..2989; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418677, ECO:0007744|PDB:7WUJ
uniprot
proteins