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Database: UniProt
Entry: GRM7_RAT
LinkDB: GRM7_RAT
Original site: GRM7_RAT 
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   26-NOV-2014, entry version 108.
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], FUNCTION, AND TISSUE SPECIFICITY.
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], FUNCTION, AND TISSUE SPECIFICITY.
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: 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
CC       activity of down-stream effectors, such as adenylate cyclase.
CC       Signaling inhibits adenylate cyclase activity.
CC       {ECO:0000269|PubMed:8145723, ECO:0000269|PubMed:8288585}.
CC   -!- SUBUNIT: Interacts with PICK1. {ECO:0000269|PubMed:11122333}.
CC   -!- INTERACTION:
CC       P97879:Grip1; NbExp=3; IntAct=EBI-6936416, EBI-936113;
CC       Q9EP80:Pick1; NbExp=2; IntAct=EBI-6936416, EBI-77728;
CC       P63088:Ppp1cc; NbExp=4; IntAct=EBI-6936416, EBI-80049;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely distributed throughout the brain.
CC       {ECO:0000269|PubMed:8145723, ECO:0000269|PubMed:8288585}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
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DR   EMBL; D16817; BAA04092.1; -; mRNA.
DR   EMBL; U06832; AAA20655.1; -; mRNA.
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   BioGrid; 249569; 10.
DR   DIP; DIP-41145N; -.
DR   IntAct; P35400; 6.
DR   MINT; MINT-146474; -.
DR   STRING; 10116.ENSRNOP00000053411; -.
DR   BindingDB; P35400; -.
DR   ChEMBL; CHEMBL2111335; -.
DR   GuidetoPHARMACOLOGY; 295; -.
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   InParanoid; P35400; -.
DR   KO; K04608; -.
DR   PhylomeDB; P35400; -.
DR   EvolutionaryTrace; P35400; -.
DR   NextBio; 615264; -.
DR   Genevestigator; P35400; -.
DR   GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:RefGenome.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
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:0045202; C:synapse; IDA:RGD.
DR   GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR   GO; GO:0001640; F:adenylate cyclase inhibiting G-protein coupled glutamate receptor activity; IDA:RGD.
DR   GO; GO:0005246; F:calcium channel regulator activity; IBA:RefGenome.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
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:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
DR   GO; GO:0007196; P:adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway; 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:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:RefGenome.
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   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   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       {ECO:0000255}.
FT   CHAIN        35    915       Metabotropic glutamate receptor 7.
FT                                /FTId=PRO_0000012940.
FT   TOPO_DOM     35    590       Extracellular. {ECO:0000255}.
FT   TRANSMEM    591    615       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    616    627       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    628    648       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    649    654       Extracellular. {ECO:0000255}.
FT   TRANSMEM    655    675       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    676    702       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    703    723       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    724    753       Extracellular. {ECO:0000255}.
FT   TRANSMEM    754    775       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    776    788       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    789    810       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    811    825       Extracellular. {ECO:0000255}.
FT   TRANSMEM    826    850       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    851    915       Cytoplasmic. {ECO:0000255}.
FT   REGION      180    182       Glutamate binding. {ECO:0000250}.
FT   BINDING     159    159       Glutamate. {ECO:0000250}.
FT   BINDING     230    230       Glutamate. {ECO:0000250}.
FT   BINDING     314    314       Glutamate. {ECO:0000250}.
FT   BINDING     407    407       Glutamate. {ECO:0000250}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    458    458       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    572    572       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     67    109       {ECO:0000269|PubMed:17360426}.
FT   DISULFID    249    541       {ECO:0000250}.
FT   DISULFID    374    390       {ECO:0000269|PubMed:17360426}.
FT   DISULFID    430    437       {ECO:0000269|PubMed:17360426}.
FT   DISULFID    523    542       {ECO:0000250}.
FT   DISULFID    527    545       {ECO:0000250}.
FT   DISULFID    548    560       {ECO:0000250}.
FT   DISULFID    563    576       {ECO:0000250}.
FT   STRAND       42     45       {ECO:0000244|PDB:2E4Z}.
FT   STRAND       48     55       {ECO:0000244|PDB:2E4Z}.
FT   STRAND       58     60       {ECO:0000244|PDB:2E4Z}.
FT   STRAND       62     64       {ECO:0000244|PDB:2E4Z}.
FT   STRAND       66     70       {ECO:0000244|PDB:2E4Z}.
FT   HELIX        72     91       {ECO:0000244|PDB:2E4Z}.
FT   STRAND       93     98       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      101    107       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       112    118       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       119    126       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      150    154       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       159    165       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       168    171       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      176    180       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       184    187       {ECO:0000244|PDB:2E4Z}.
FT   TURN        189    192       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      193    199       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       202    215       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      221    228       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       229    244       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      250    256       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       265    274       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      282    286       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       289    301       {ECO:0000244|PDB:2E4Z}.
FT   TURN        305    307       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      308    312       {ECO:0000244|PDB:2E4Z}.
FT   TURN        314    318       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       321    323       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       327    330       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      334    339       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       344    350       {ECO:0000244|PDB:2E4Z}.
FT   TURN        355    357       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       364    371       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       394    397       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       408    429       {ECO:0000244|PDB:2E4Z}.
FT   TURN        438    443       {ECO:0000244|PDB:2E4Z}.
FT   HELIX       445    452       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      477    483       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      491    504       {ECO:0000244|PDB:2E4Z}.
FT   STRAND      506    508       {ECO:0000244|PDB:2E4Z}.
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
//
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