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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   29-OCT-2014, entry version 107.
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
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
//
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