GRM1_RAT
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 03-AUG-2022, entry version 198.
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}.
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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. [P23385-1]
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 GlyGen; P23385; 4 sites.
DR iPTMnet; P23385; -.
DR PhosphoSitePlus; P23385; -.
DR PaxDb; P23385; -.
DR PRIDE; P23385; -.
DR Ensembl; ENSRNOT00000044325; ENSRNOP00000047790; ENSRNOG00000014290. [P23385-2]
DR GeneID; 24414; -.
DR KEGG; rno:24414; -.
DR UCSC; RGD:2742; rat. [P23385-1]
DR CTD; 2911; -.
DR RGD; 2742; Grm1.
DR VEuPathDB; HostDB:ENSRNOG00000014290; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234595; -.
DR InParanoid; P23385; -.
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 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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; 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; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density 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:0007216; P:G protein-coupled glutamate receptor signaling pathway; IMP:SynGO.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISS: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: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; IEP:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; TAS:UniProtKB.
DR Gene3D; 2.10.50.30; -; 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 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; 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; 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
