ID A0A1S3FY43_DIPOR Unreviewed; 882 AA.
AC A0A1S3FY43;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Metabotropic glutamate receptor 3 {ECO:0000256|ARBA:ARBA00020281};
GN Name=Grm3 {ECO:0000313|RefSeq:XP_012881481.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881481.1};
RN [1] {ECO:0000313|RefSeq:XP_012881481.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881481.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00025645}.
CC -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000256|ARBA:ARBA00011150}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000256|ARBA:ARBA00007242}.
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DR RefSeq; XP_012881481.1; XM_013026027.1.
DR AlphaFoldDB; A0A1S3FY43; -.
DR STRING; 10020.ENSDORP00000003646; -.
DR GeneID; 105992929; -.
DR KEGG; dord:105992929; -.
DR CTD; 2913; -.
DR InParanoid; A0A1S3FY43; -.
DR OMA; ILKCNIQ; -.
DR OrthoDB; 5388627at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_012881481.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..882
FT /note="Metabotropic glutamate receptor 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010233638"
FT TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 579..845
FT /note="G-protein coupled receptors family 3 profile"
FT /evidence="ECO:0000259|PROSITE:PS50259"
SQ SEQUENCE 882 AA; 99088 MW; 0B2202F91626CD18 CRC64;
MGSIKMLTRL QVLTLALFSK GFLLSLGDHN FLRKEIKIEG DLVLGGLFPI NEKGTGTEEC
GRINEDRGIQ RLEAMLFAID EINKDNYLLP GVKLGVHILD TCSRDTYALE QSLEFVRASL
TKVDEAEYMC PDGSYAIQEN IPLLIAGVIG GSYSSVSIQV ANLLRLFQIP QISYASTSAK
LSDKSRYDYF ARTVPPDFYQ AKAMAEILRF FNWTYVSTVA SEGDYGETGI EAFEQEARLR
NICIATAEKV GRSNIRKSYD SVIRELLQKP NARVVVLFMR SDDSRELIAA ASRANASFTW
VASDGWGAQE SIVKGSEHVA YGAITLELAS QPVRQFDRYF QSLNPYNNHR NPWFRDFWEQ
KFQCSLQNKR NHRRLCDKHL AIDSSNYEQE SKIMFVVNAV YAMAHALHKM QRTLCPNTTK
LCDAMKILDG KKLYKDYLLK INFTAPFNPN NDADSIVKFD TYGDGMGRYN VFNFQYLGGK
YSYLKVGHWA ETLSLNVDSI HWSRNSVPTS QCSDPCAPNE MKNMQPGDVC CWICIPCESY
EYLADEFTCM DCGPGQWPTA DLSGCFDLPE DYIKWEDAWA IGPVTIACLG FMCTCIVITV
FIKHNNTPLV KASGRELCYI LLFGVGLSYS MTFFFIAKPS PVICALRRLG LGTSFAICYS
ALLTKTNCIA RIFDGVKNGA QRPKFISPSS QVFICLGLIL VQIVVVSVWL ILEAPGTRRY
TLPEKRETVI LKCNVKDSSM LISLTYDVIL VILCTVYAFK TRKCPENFNE AKFIGFTMYT
TCIIWLAFLP IFYVTSSDYR VQTTTMCISV SLSGFVVLGC LFAPKVHIVL FQPQKNVVTH
RLHLNRFSVS GTGTTYSQSS ASTYVPTVCN GREVLDSTTS SL
//
