GRM4_MACFA
ID GRM4_MACFA Reviewed; 912 AA.
AC Q1ZZH0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Metabotropic glutamate receptor 4;
DE Short=mGluR4;
DE Flags: Precursor;
GN Name=GRM4;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=16943768;
RA Hanna M.C., Calkins D.J.;
RT "Expression and sequences of genes encoding glutamate receptors and
RT transporters in primate retina determined using 3'-end amplification
RT polymerase chain reaction.";
RL Mol. Vis. 12:961-976(2006).
CC -!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors. Signaling inhibits adenylate cyclase activity
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PICK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; DQ417735; ABD74420.1; -; mRNA.
DR RefSeq; NP_001271577.1; NM_001284648.1.
DR AlphaFoldDB; Q1ZZH0; -.
DR SMR; Q1ZZH0; -.
DR STRING; 9541.XP_005553328.1; -.
DR GeneID; 102144159; -.
DR CTD; 2914; -.
DR eggNOG; KOG1056; Eukaryota.
DR OrthoDB; 483746at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR001786; GPCR_3_mGluR4.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01054; MTABOTROPC4R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..912
FT /note="Metabotropic glutamate receptor 4"
FT /id="PRO_0000250700"
FT TOPO_DOM 33..586
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..624
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..671
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical; Name=SP 6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 180..182
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 249..538
FT /evidence="ECO:0000250"
FT DISULFID 372..388
FT /evidence="ECO:0000250"
FT DISULFID 428..435
FT /evidence="ECO:0000250"
FT DISULFID 520..539
FT /evidence="ECO:0000250"
FT DISULFID 524..542
FT /evidence="ECO:0000250"
FT DISULFID 545..557
FT /evidence="ECO:0000250"
FT DISULFID 560..573
FT /evidence="ECO:0000250"
SQ SEQUENCE 912 AA; 101831 MW; 071D76AB48872D6A CRC64;
MPGKSGLGWW WARLPLCLLL SLYGPWMPSS LGKPKGHPHM NSIRIDGDIT LGGLFPVHGR
GSEGKACGEL KKEKGIHRLE AMLFALDRIN NDPDLLPNIT LGARILDTCS RDTHALEQSL
TFVQALIEKD GTEVRCGSGG PPIITKPERV VGVIGASGSS VSIMVANILR LFKIPQISYA
STAPDLSDNS RYDFFSRVVP SDTYQAQAMV DIVRALKWNY VSTVASEGSY GESGVEAFIQ
KSREDGGVCI AQSVKIPREP KAGEFDKIIR RLLETSNARA VIIFANEDDI RRVLEAARRA
NQTGHFFWMG SDSWGSKIAP VLHLEEVAEG AVTILPKRMS VRGFDRYFSS RTLDNNRRNI
WFAEFWEDNF HCKLSRHALK KGSHVKKCTN RERIGQDSAY EQEGKVQFVI DAVYAMGHAL
HAMHRDLCPG RVGLCPRMDP VDGTQLLKYI RNVNFSGIAG NPVTFNENGD APGRYDIYQY
QLRNDSAEYK VIGSWTDHLH LRIERMHWPG SGQQLPRSIC SLPCQPGERK KTVKGMPCCW
HCEPCTGYQY QVDRYTCKTC PYDMRPTENR TGCRPIPIIK LEWDSPWAVL PLFLAVVGIA
ATLFVVITFV RYNDTPIVKA SGRELSYVLL AGIFLCYATT FLMIAEPDLG TCSLRRIFLG
LGMSISYAAL LTKTNRIYRI FEQGKRSVSA PRFISPASQL AITFSLISLQ LLGICVWFVV
DPSHSVVDFQ DQRTLDPRFA RGVLKCDISD LSLICLLGYS MLLMVTCTVY AIKTRGVPET
FNEAKPIGFT MYTTCIVWLA FIPIFFGTSQ SADKLYIQTT TLTVSVSLSA SVSLGMLYMP
KVYIILFHPE QNVPKRKRSL KAVVTAATMS NKFTQKGNFR PNGEAKSELC ENLEAPALAT
KQTYVTYTNH AI
