ID GRM1_RAT Reviewed; 1199 AA. AC P23385; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Metabotropic glutamate receptor 1; DE Short=mGluR1; DE Flags: Precursor; GN Name=Grm1; Synonyms=Gprc1a, Mglur1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=1847995; DOI=10.1038/349760a0; RA Masu M., Tanabe Y., Tsuchida K., Shigemoto R., Nakanishi S.; RT "Sequence and expression of a metabotropic glutamate receptor."; RL Nature 349:760-765(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=1656524; DOI=10.1126/science.1656524; RA Houamed K.M., Kuijper J.L., Gilbert T.L., Haldeman B.A., O'Hara P.J., RA Mulvihill E.R., Almers W., Hagen F.S.; RT "Cloning, expression, and gene structure of a G protein-coupled glutamate RT receptor from rat brain."; RL Science 252:1318-1321(1991). RN [3] RP ALTERNATIVE SPLICING (ISOFORM 1B). RC TISSUE=Brain; RX PubMed=1309649; DOI=10.1016/0896-6273(92)90118-w; RA Tanabe Y., Masu M., Ishii T., Shigemoto R., Nakanishi S.; RT "A family of metabotropic glutamate receptors."; RL Neuron 8:169-179(1992). RN [4] RP ALTERNATIVE SPLICING (ISOFORM 1C), AND FUNCTION. RC TISSUE=Brain; RX PubMed=1438218; DOI=10.1073/pnas.89.21.10331; RA Pin J.-P., Waeber C., Prezeau L., Bockaert J., Heinemann S.F.; RT "Alternative splicing generates metabotropic glutamate receptors inducing RT different patterns of calcium release in Xenopus oocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 89:10331-10335(1992). RN [5] RP INTERACTION WITH SIAH1. RX PubMed=10469171; DOI=10.1046/j.1365-2443.1999.00269.x; RA Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S., Nakanishi S.; RT "Competitive interaction of seven in absentia homolog-1A and RT Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic glutamate RT receptors."; RL Genes Cells 4:381-390(1999). RN [6] RP FUNCTION, INTERCHAIN DISULFIDE BOND, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF CYS-67; CYS-109 AND CYS-140. RX PubMed=10945991; DOI=10.1074/jbc.m005581200; RA Ray K., Hauschild B.C.; RT "Cys-140 is critical for metabotropic glutamate receptor-1 dimerization."; RL J. Biol. Chem. 275:34245-34251(2000). RN [7] RP INTERACTION WITH TAMALIN. RX PubMed=11850456; DOI=10.1523/jneurosci.22-04-01280.2002; RA Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y., RA Nakanishi S.; RT "Tamalin, a PDZ domain-containing protein, links a protein complex RT formation of group 1 metabotropic glutamate receptors and the guanine RT nucleotide exchange factor cytohesins."; RL J. Neurosci. 22:1280-1289(2002). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-894; SER-1147 AND THR-1151, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 33-522 ALONE AND IN COMPLEX WITH RP GLUTAMATE, SUBUNIT, GLYCOSYLATION AT ASN-98 AND ASN-223, GLUTAMATE-BINDING RP SITES, AND DISULFIDE BONDS. RX PubMed=11069170; DOI=10.1038/35039564; RA Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T., RA Nakanishi S., Jingami H., Morikawa K.; RT "Structural basis of glutamate recognition by a dimeric metabotropic RT glutamate receptor."; RL Nature 407:971-977(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-522 IN COMPLEX WITH GLUTAMATE RP AND ANTAGONIST, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=11867751; DOI=10.1073/pnas.052708599; RA Tsuchiya D., Kunishima N., Kamiya N., Jingami H., Morikawa K.; RT "Structural views of the ligand-binding cores of a metabotropic glutamate RT receptor complexed with an antagonist and both glutamate and Gd3+."; RL Proc. Natl. Acad. Sci. U.S.A. 99:2660-2665(2002). 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 activates a phosphatidylinositol- CC calcium second messenger system. May participate in the central action CC of glutamate in the CNS, such as long-term potentiation in the CC hippocampus and long-term depression in the cerebellum CC (PubMed:10945991, PubMed:1438218, PubMed:1656524, PubMed:1847995). May CC function in the light response in the retina (By similarity). CC {ECO:0000250|UniProtKB:P97772, ECO:0000269|PubMed:10945991, CC ECO:0000269|PubMed:1438218, ECO:0000269|PubMed:1656524, CC ECO:0000269|PubMed:1847995}. CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:11069170, CC PubMed:11867751). The PPXXF motif binds HOMER1, HOMER2 and HOMER3. CC Interacts with TAMALIN (PubMed:11850456). Interacts with RYR1, RYR2, CC ITPR1, SHANK1 and SHANK3. Interacts with SIAH1 (PubMed:10469171). CC {ECO:0000269|PubMed:10469171, ECO:0000269|PubMed:11069170, CC ECO:0000269|PubMed:11850456, ECO:0000269|PubMed:11867751}. CC -!- INTERACTION: CC P23385; P63088: Ppp1cc; NbExp=15; IntAct=EBI-4410410, EBI-80049; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10945991}; CC Multi-pass membrane protein {ECO:0000269|PubMed:10945991}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1A; CC IsoId=P23385-1; Sequence=Displayed; CC Name=1B; CC IsoId=P23385-2; Sequence=VSP_002026, VSP_002027; CC Name=1C; CC IsoId=P23385-3; Sequence=VSP_002028, VSP_002029; CC -!- TISSUE SPECIFICITY: Predominantly expressed in cerebellar Purkinje CC cells, CA2-CA3 pyramidal cells of the hippocampus, and mitral and CC tufted cells of the olfactory bulb. {ECO:0000269|PubMed:1656524, CC ECO:0000269|PubMed:1847995}. CC -!- MISCELLANEOUS: Activated by quisqualate > glutamate > ibotenate > CC trans-1- aminocyclopentyl-1,3-dicarboxylate; inhibited by 2-amino-3- CC phosphonopropionate. CC -!- MISCELLANEOUS: [Isoform 1B]: C-terminally truncated forms of isoform CC 1A. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 1C]: C-terminally truncated forms of isoform CC 1A. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57569; CAA40799.1; -; mRNA. DR EMBL; M61099; AAA19497.1; -; mRNA. DR EMBL; S48085; AAB24138.1; -; mRNA. DR PIR; A41939; A41939. DR RefSeq; NP_001107802.1; NM_001114330.1. [P23385-2] DR RefSeq; NP_058707.1; NM_017011.1. DR PDB; 1EWK; X-ray; 2.20 A; A/B=33-522. DR PDB; 1EWT; X-ray; 3.70 A; A/B=33-522. DR PDB; 1EWV; X-ray; 4.00 A; A/B=33-522. DR PDB; 1ISR; X-ray; 4.00 A; A=33-522. DR PDB; 1ISS; X-ray; 3.30 A; A/B=33-522. DR PDBsum; 1EWK; -. DR PDBsum; 1EWT; -. DR PDBsum; 1EWV; -. DR PDBsum; 1ISR; -. DR PDBsum; 1ISS; -. DR AlphaFoldDB; P23385; -. DR SMR; P23385; -. DR BioGRID; 246579; 13. DR CORUM; P23385; -. DR DIP; DIP-44897N; -. DR ELM; P23385; -. DR IntAct; P23385; 5. DR MINT; P23385; -. DR STRING; 10116.ENSRNOP00000019319; -. DR BindingDB; P23385; -. DR ChEMBL; CHEMBL4477; -. DR DrugCentral; P23385; -. DR GuidetoPHARMACOLOGY; 289; -. DR GlyCosmos; P23385; 4 sites, No reported glycans. DR GlyGen; P23385; 4 sites. DR iPTMnet; P23385; -. DR PhosphoSitePlus; P23385; -. DR PaxDb; 10116-ENSRNOP00000019319; -. DR Ensembl; ENSRNOT00000044325.4; ENSRNOP00000047790.3; ENSRNOG00000014290.8. [P23385-2] DR Ensembl; ENSRNOT00055002855; ENSRNOP00055002139; ENSRNOG00055001767. [P23385-1] DR Ensembl; ENSRNOT00060010027; ENSRNOP00060007508; ENSRNOG00060006069. [P23385-1] DR Ensembl; ENSRNOT00065043138; ENSRNOP00065035335; ENSRNOG00065025066. [P23385-1] DR GeneID; 24414; -. DR KEGG; rno:24414; -. DR UCSC; RGD:2742; rat. [P23385-1] DR AGR; RGD:2742; -. DR CTD; 2911; -. DR RGD; 2742; Grm1. DR VEuPathDB; HostDB:ENSRNOG00000014290; -. DR eggNOG; KOG1056; Eukaryota. DR GeneTree; ENSGT01030000234595; -. DR InParanoid; P23385; -. DR OrthoDB; 5388627at2759; -. DR PhylomeDB; P23385; -. DR Reactome; R-RNO-416476; G alpha (q) signalling events. DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR Reactome; R-RNO-6794361; Neurexins and neuroligins. DR EvolutionaryTrace; P23385; -. DR PRO; PR:P23385; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000014290; Expressed in Ammon's horn and 3 other cell types or tissues. DR ExpressionAtlas; P23385; baseline and differential. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:RGD. DR GO; GO:0038037; C:G protein-coupled receptor dimeric complex; ISO:RGD. DR GO; GO:0038038; C:G protein-coupled receptor homodimeric complex; ISO:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; ISO:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD. DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central. DR GO; GO:0098872; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:RGD. DR GO; GO:0099530; F:G protein-coupled receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO. DR GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB. DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD. DR GO; GO:0001639; F:PLC activating G protein-coupled glutamate receptor activity; TAS:UniProtKB. DR GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD. DR GO; GO:0071257; P:cellular response to electrical stimulus; ISO:RGD. DR GO; GO:0007268; P:chemical synaptic transmission; IEP:RGD. DR GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; ISO:RGD. DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IMP:SynGO. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0098712; P:L-glutamate import across plasma membrane; ISO:RGD. DR GO; GO:0007626; P:locomotory behavior; ISO:RGD. DR GO; GO:0051899; P:membrane depolarization; TAS:UniProtKB. DR GO; GO:0007206; P:phospholipase C-activating G protein-coupled glutamate receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD. DR GO; GO:0014048; P:regulation of glutamate secretion; TAS:UniProtKB. DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD. DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IDA:UniProtKB. DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD. DR GO; GO:0051932; P:synaptic transmission, GABAergic; TAS:UniProtKB. DR CDD; cd15449; 7tmC_mGluR1; 1. DR CDD; cd06374; PBP1_mGluR_groupI; 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; IPR001256; GPCR_3_mGluR1. DR InterPro; IPR000162; GPCR_3_mtglu_rcpt. DR InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd. DR InterPro; IPR028082; Peripla_BP_I. DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1. DR PANTHER; PTHR24060:SF29; METABOTROPIC GLUTAMATE RECEPTOR 1; 1. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF10606; GluR_Homer-bdg; 1. DR Pfam; PF07562; NCD3G; 1. DR PRINTS; PR00248; GPCRMGR. DR PRINTS; PR01051; MTABOTROPC1R. DR PRINTS; PR00593; MTABOTROPICR. DR SMART; SM01229; GluR_Homer-bdg; 1. 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 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Signal; Transducer; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1199 FT /note="Metabotropic glutamate receptor 1" FT /id="PRO_0000012924" FT TOPO_DOM 19..592 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 593..615 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 616..629 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 630..650 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 651..658 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 659..680 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 681..703 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 704..727 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 728..750 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 751..772 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 773..785 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 786..807 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 808..815 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 816..840 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 841..1199 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 882..905 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 959..1036 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1056..1081 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1120..1177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1011..1033 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1157..1177 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 74 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:11069170, FT ECO:0000269|PubMed:11867751" FT BINDING 165 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:11069170, FT ECO:0000269|PubMed:11867751" FT BINDING 186..188 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 236 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:11069170, FT ECO:0000269|PubMed:11867751" FT BINDING 318 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:11069170, FT ECO:0000269|PubMed:11867751" FT BINDING 409 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:11069170, FT ECO:0000269|PubMed:11867751" FT MOD_RES 853 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97772" FT MOD_RES 871 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P97772" FT MOD_RES 894 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 969 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97772" FT MOD_RES 1098 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97772" FT MOD_RES 1147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1151 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 1154 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97772" FT CARBOHYD 98 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11069170" FT CARBOHYD 223 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11069170" FT CARBOHYD 397 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 515 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 67..109 FT DISULFID 140 FT /note="Interchain" FT DISULFID 289..291 FT DISULFID 378..394 FT DISULFID 432..439 FT DISULFID 657..746 FT /evidence="ECO:0000250" FT VAR_SEQ 887..906 FT /note="NSNGKSVSWSEPGGRQAPKG -> KKRQPEFSPSSQCPSAHAQL (in FT isoform 1B)" FT /evidence="ECO:0000305" FT /id="VSP_002026" FT VAR_SEQ 888..897 FT /note="SNGKSVSWSE -> FALDRQNTVY (in isoform 1C)" FT /evidence="ECO:0000305" FT /id="VSP_002028" FT VAR_SEQ 898..1199 FT /note="Missing (in isoform 1C)" FT /evidence="ECO:0000305" FT /id="VSP_002029" FT VAR_SEQ 907..1199 FT /note="Missing (in isoform 1B)" FT /evidence="ECO:0000305" FT /id="VSP_002027" FT MUTAGEN 67 FT /note="C->S: Impairs protein folding and abolishes location FT at the cell surface." FT /evidence="ECO:0000269|PubMed:10945991" FT MUTAGEN 109 FT /note="C->S: Impairs protein folding and abolishes location FT at the cell surface." FT /evidence="ECO:0000269|PubMed:10945991" FT MUTAGEN 140 FT /note="C->S: Impairs homodimerization." FT /evidence="ECO:0000269|PubMed:10945991" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 44..51 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 59..65 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 72..75 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 76..91 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 165..175 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 190..193 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 208..221 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 226..234 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 235..251 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 254..261 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:1ISS" FT HELIX 267..278 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 279..283 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 293..306 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 313..316 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 318..322 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 324..327 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 348..354 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 368..375 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 400..403 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 410..431 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:1EWK" FT HELIX 447..455 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 458..460 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 466..468 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 479..486 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 492..501 FT /evidence="ECO:0007829|PDB:1EWK" FT STRAND 504..507 FT /evidence="ECO:0007829|PDB:1EWK" FT TURN 509..511 FT /evidence="ECO:0007829|PDB:1EWK" SQ SEQUENCE 1199 AA; 133236 MW; EEE5A04C50694B9F CRC64; MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI EFIRDSLISI RDEKDGLNRC LPDGQTLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL EENYVQDSKM GFVINAIYAM AHGLQNMHHA LCPGHVGLCD AMKPIDGRKL LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE VSCCWICTAC KENEFVQDEF TCRACDLGWW PNAELTGCEP IPVRYLEWSD IESIIAIAFS CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS TKTLYNVEEE DNTPSAHFSP PSSPSMVVHR RGPPVATTPP LPPHLTAEET PLFLADSVIP KGLPPPLPQQ QPQQPPPQQP PQQPKSLMDQ LQGVVTNFGS GIPDFHAVLA GPGTPGNSLR SLYPPPPPPQ HLQMLPLHLS TFQEESISPP GEDIDDDSER FKLLQEFVYE REGNTEEDEL EEEEDLPTAS KLTPEDSPAL TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL //