ID GRM7_RAT Reviewed; 915 AA.
AC P35400;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-APR-2013, entry version 98.
DE RecName: Full=Metabotropic glutamate receptor 7;
DE Short=mGluR7;
DE Flags: Precursor;
GN Name=Grm7; Synonyms=Gprc1g, Mglur7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8288585;
RA Okamoto N., Hori S., Akazawa C., Hayashi Y., Shigemoto R., Mizuno N.,
RA Nakanishi S.;
RT "Molecular characterization of a new metabotropic glutamate receptor
RT mGluR7 coupled to inhibitory cyclic AMP signal transduction.";
RL J. Biol. Chem. 269:1231-1236(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX PubMed=8145723;
RA Saugstad J.A., Kinzie J.M., Mulvihill E.R., Segerson T.P.,
RA Westbrook G.L.;
RT "Cloning and expression of a new member of the L-2-amino-4-
RT phosphonobutyric acid-sensitive class of metabotropic glutamate
RT receptors.";
RL Mol. Pharmacol. 45:367-372(1994).
RN [3]
RP INTERACTION WITH PICK1.
RX PubMed=11122333; DOI=10.1046/j.1460-9568.2000.01309.x;
RA El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A.,
RA Betz H.;
RT "Interaction of the C-terminal tail region of the metabotropic
RT glutamate receptor 7 with the protein kinase C substrate PICK1.";
RL Eur. J. Neurosci. 12:4215-4221(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-521, AND DISULFIDE BONDS.
RX PubMed=17360426; DOI=10.1073/pnas.0611577104;
RA Muto T., Tsuchiya D., Morikawa K., Jingami H.;
RT "Structures of the extracellular regions of the group II/III
RT metabotropic glutamate receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007).
CC -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC mediated by a G-protein that inhibits adenylate cyclase activity.
CC -!- SUBUNIT: Interacts with PICK1.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely distributed throughout the brain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR EMBL; D16817; BAA04092.1; -; mRNA.
DR EMBL; U06832; AAA20655.1; -; mRNA.
DR IPI; IPI00198587; -.
DR PIR; A49874; A49874.
DR RefSeq; NP_112302.1; NM_031040.1.
DR UniGene; Rn.10409; -.
DR PDB; 2E4Z; X-ray; 3.30 A; A=33-521.
DR PDBsum; 2E4Z; -.
DR ProteinModelPortal; P35400; -.
DR SMR; P35400; 40-511.
DR DIP; DIP-41145N; -.
DR MINT; MINT-146474; -.
DR STRING; 10116.ENSRNOP00000053411; -.
DR PhosphoSite; P35400; -.
DR PRIDE; P35400; -.
DR GeneID; 81672; -.
DR KEGG; rno:81672; -.
DR CTD; 2917; -.
DR RGD; 619857; Grm7.
DR eggNOG; NOG295200; -.
DR HOVERGEN; HBG107965; -.
DR KO; K04608; -.
DR BindingDB; P35400; -.
DR ChEMBL; CHEMBL3879; -.
DR EvolutionaryTrace; P35400; -.
DR NextBio; 615264; -.
DR Genevestigator; P35400; -.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0043234; C:protein complex; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
DR GO; GO:0007611; P:learning or memory; TAS:UniProtKB.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IDA:RGD.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR InterPro; IPR001883; GPCR_3_mtglu_rcpt_7.
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 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Olfaction;
KW Receptor; Reference proteome; Sensory transduction; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1 34 Potential.
FT CHAIN 35 915 Metabotropic glutamate receptor 7.
FT /FTId=PRO_0000012940.
FT TOPO_DOM 35 590 Extracellular (Potential).
FT TRANSMEM 591 615 Helical; Name=1; (Potential).
FT TOPO_DOM 616 627 Cytoplasmic (Potential).
FT TRANSMEM 628 648 Helical; Name=2; (Potential).
FT TOPO_DOM 649 654 Extracellular (Potential).
FT TRANSMEM 655 675 Helical; Name=3; (Potential).
FT TOPO_DOM 676 702 Cytoplasmic (Potential).
FT TRANSMEM 703 723 Helical; Name=4; (Potential).
FT TOPO_DOM 724 753 Extracellular (Potential).
FT TRANSMEM 754 775 Helical; Name=5; (Potential).
FT TOPO_DOM 776 788 Cytoplasmic (Potential).
FT TRANSMEM 789 810 Helical; Name=6; (Potential).
FT TOPO_DOM 811 825 Extracellular (Potential).
FT TRANSMEM 826 850 Helical; Name=7; (Potential).
FT TOPO_DOM 851 915 Cytoplasmic (Potential).
FT CARBOHYD 98 98 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 458 458 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 486 486 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 572 572 N-linked (GlcNAc...) (Potential).
FT DISULFID 67 109
FT DISULFID 249 541 By similarity.
FT DISULFID 374 390
FT DISULFID 430 437
FT DISULFID 523 542 By similarity.
FT DISULFID 527 545 By similarity.
FT DISULFID 548 560 By similarity.
FT DISULFID 563 576 By similarity.
FT STRAND 42 45
FT STRAND 48 55
FT STRAND 58 60
FT STRAND 62 64
FT STRAND 66 70
FT HELIX 72 91
FT STRAND 93 98
FT STRAND 101 107
FT HELIX 112 118
FT HELIX 119 126
FT STRAND 150 154
FT HELIX 159 165
FT HELIX 168 171
FT STRAND 176 180
FT HELIX 184 187
FT TURN 189 192
FT STRAND 193 199
FT HELIX 202 215
FT STRAND 221 228
FT HELIX 229 244
FT STRAND 250 256
FT HELIX 265 274
FT STRAND 282 286
FT HELIX 289 301
FT TURN 305 307
FT STRAND 308 312
FT TURN 314 318
FT HELIX 321 323
FT HELIX 327 330
FT STRAND 334 339
FT HELIX 344 350
FT TURN 355 357
FT HELIX 364 371
FT HELIX 394 397
FT HELIX 408 429
FT TURN 438 443
FT HELIX 445 452
FT STRAND 477 483
FT STRAND 491 504
FT STRAND 506 508
SQ SEQUENCE 915 AA; 102232 MW; F28AFC4C6454A6C2 CRC64;
MVQLGKLLRV LTLMKFPCCV LEVLLCVLAA AARGQEMYAP HSIRIEGDVT LGGLFPVHAK
GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT LGARILDTCS RDTYALEQSL
TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA
STAPELSDDR RYDFFSRVVP PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTQ
ISKEAGGLCI AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK
RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF TSRTLENNRR
NVWFAEYWEE NFNCKLTISG SKKEDTDRKC TGQERIGKDS NYEQEGKVQF VIDAVYAMAH
ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK YIRHVNFNGS AGTPVMFNKN GDAPGRYDIF
QYQTTNTTNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPS SVCTLPCKPG QRKKTQKGTP
CCWTCEPCDG YQYQFDEMTC QHCPYDQRPN ENRTGCQNIP 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 ELCENVDPNS
PAAKKKYVSY NNLVI
//
