ID GRM3_PONAB Reviewed; 879 AA.
AC Q5RAL3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 76.
DE RecName: Full=Metabotropic glutamate receptor 3;
DE Short=mGluR3;
DE Flags: Precursor;
GN Name=GRM3;
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 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 TAMALIN. {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; CR859002; CAH91197.1; -; mRNA.
DR RefSeq; NP_001125703.1; NM_001132231.1.
DR AlphaFoldDB; Q5RAL3; -.
DR SMR; Q5RAL3; -.
DR STRING; 9601.ENSPPYP00000020006; -.
DR GlyCosmos; Q5RAL3; 4 sites, No reported glycans.
DR GeneID; 100172627; -.
DR KEGG; pon:100172627; -.
DR CTD; 2913; -.
DR eggNOG; KOG1056; Eukaryota.
DR InParanoid; Q5RAL3; -.
DR OrthoDB; 5388627at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0008066; F:glutamate receptor activity; IEA:UniProt.
DR CDD; cd15448; 7tmC_mGluR3; 1.
DR CDD; cd06375; PBP1_mGluR_groupII; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 2.10.50.30; GPCR, family 3, nine cysteines domain; 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; IPR001234; GPCR_3_mGluR3.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1.
DR PANTHER; PTHR24060:SF160; METABOTROPIC GLUTAMATE RECEPTOR 3; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00248; GPCRMGR.
DR PRINTS; PR01053; MTABOTROPC3R.
DR PRINTS; PR00593; MTABOTROPICR.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..879
FT /note="Metabotropic glutamate receptor 3"
FT /id="PRO_0000042105"
FT TOPO_DOM 23..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..599
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..664
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..734
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..756
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 757..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..792
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..828
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 151
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..99
FT /evidence="ECO:0000250"
FT DISULFID 240..527
FT /evidence="ECO:0000250"
FT DISULFID 361..373
FT /evidence="ECO:0000250"
FT DISULFID 412..419
FT /evidence="ECO:0000250"
FT DISULFID 509..528
FT /evidence="ECO:0000250"
FT DISULFID 513..531
FT /evidence="ECO:0000250"
FT DISULFID 534..546
FT /evidence="ECO:0000250"
FT DISULFID 549..562
FT /evidence="ECO:0000250"
SQ SEQUENCE 879 AA; 98975 MW; 086005EDEAF5BA18 CRC64;
MKMLTRLQVL TLALFSKGFL LSLGDHNFLR REIKIEGDLV LGGLFPINEK GTGTEECGRI
NEDRGIQRLE AMLFAIDEIN KDDYLLPGVE LGVHILDTCS RDTYALEQSL EFVRASLTKV
DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD
KSRYDYFART VPPDFYQAKA MAEILRFFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC
IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAASR ANASFTWVAS
DGWGAQESII KGSEHVAYGA ITLELASQPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ
CSLQNKRNHR RVCDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD
AMRILDGKKL YRDYLLKINF TAPFNPNKDA DSIVKFDTFG DGMGRYNVFN FQNVGGKYSY
LKVGHWAETL SLDVDSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL
ADEFTCMDCG PGQWPTADLT GCYDLPEDYI RWEDAWVIGP VTIACLGFMC TCMVVTVFIK
HNNTPLVKAS GRELCYILLF GVGLSYCMTF FFIAKPSPVI CALRRLGLGS SFAICYSALL
TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE APGTRRYTLA
EKRETVILKC NVKDSSMLIS LTYDVILVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI
IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIILFQP QKNVVTHRLH
LNRFSVSGTG TTYSQSSAST YVPTVCNGRE VLDSTTSSL
//
