GRM7_PONAB
ID GRM7_PONAB Reviewed; 922 AA.
AC Q5RDQ8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Metabotropic glutamate receptor 7;
DE Short=mGluR7;
DE Flags: Precursor;
GN Name=GRM7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: G-protein coupled receptor activated by glutamate that
CC regulates axon outgrowth through the MAPK-cAMP-PKA signaling pathway
CC during neuronal development (By similarity). Ligand binding causes a
CC conformation change that triggers signaling via guanine nucleotide-
CC binding proteins (G proteins) and modulates the activity of downstream
CC effectors, such as adenylate cyclase that it inhibits (By similarity).
CC {ECO:0000250|UniProtKB:Q14831}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PICK1.
CC {ECO:0000250|UniProtKB:P35400, ECO:0000250|UniProtKB:Q14831}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14831};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14831}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; CR857845; CAH90099.1; -; mRNA.
DR RefSeq; NP_001125005.1; NM_001131533.1.
DR AlphaFoldDB; Q5RDQ8; -.
DR SMR; Q5RDQ8; -.
DR STRING; 9601.ENSPPYP00000015309; -.
DR GeneID; 100171884; -.
DR KEGG; pon:100171884; -.
DR CTD; 2917; -.
DR eggNOG; KOG1056; Eukaryota.
DR InParanoid; Q5RDQ8; -.
DR OrthoDB; 483746at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0061564; P:axon development; 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; IPR001883; GPCR_3_mGluR7.
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; PR01057; MTABOTROPC7R.
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; Sensory transduction; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..922
FT /note="Metabotropic glutamate receptor 7"
FT /id="PRO_0000042106"
FT TOPO_DOM 35..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..615
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..753
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..775
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 789..810
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..825
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 851..922
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 314
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 407
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 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..109
FT /evidence="ECO:0000250"
FT DISULFID 249..541
FT /evidence="ECO:0000250"
FT DISULFID 374..390
FT /evidence="ECO:0000250"
FT DISULFID 430..437
FT /evidence="ECO:0000250"
FT DISULFID 523..542
FT /evidence="ECO:0000250"
FT DISULFID 527..545
FT /evidence="ECO:0000250"
FT DISULFID 548..560
FT /evidence="ECO:0000250"
FT DISULFID 563..576
FT /evidence="ECO:0000250"
SQ SEQUENCE 922 AA; 103022 MW; 4609BF3B669FB763 CRC64;
MVQLRKLLRV LTLMKFPCCV LEVLLCALAA AARGQEMYAP HSIRIEGDVT LGGLFPVHAK
GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT LGARILDTCS RDTYALEQSL
TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA
STAPGLSDDR RYDFFSRVVP PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTR
ISKEAGGLCI AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK
RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF TSRTLENNRR
NVWFAEYWEE NFNCKLTIGG SKKEDTDRKC TGQERIGKDS NYEQEGKVQF VIDAVYAMAH
ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK YIRNVNFNGS AGTPVMFNKN GDAPGRYDIF
QYQTTNTSNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPP SVCTLPCKPG QRKKTQKGTP
CCWTCEPCDG YQYQFDEMTC QHCPYDQRPN ENRTGCQDIP IIKLEWHSPW AVIPVFLAML
GIIATIFVMA TFIRYNDTPI VRASGRELSY VLLTGIFLCY IITFLMIAKP DVAVCSFRRV
FLGLGMCISY AALLTKTNRI YRIFEQGKKS VTAPRLISPT SQLAITSSLI SVQLLGVFIW
FGVDPPNIII DYDEHKTMNP EQARGVLKCD ITDLQIICSL GYSILLMVTC TVYAIKTRGV
PENFNEAKPI GFTMYTTCIV WLAFIPIFFG TAQSAEKLYI QTTTLTISMN LSASVALGML
YMPKVYIIIF HPELNVQKRK RSFKAVVTAA TMSSRLSHKP SDRPNGEAKT ELCENVDPNN
CIPPVRKSVQ KSVTWYTIPP TV
