ID GRM2_HUMAN Reviewed; 872 AA. AC Q14416; B0M0K7; Q14CU5; Q52MC6; Q9H3N6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 27-MAR-2024, entry version 181. DE RecName: Full=Metabotropic glutamate receptor 2; DE Short=mGluR2; DE Flags: Precursor; GN Name=GRM2 {ECO:0000312|HGNC:HGNC:4594}; Synonyms=GPRC1B, MGLUR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=7620613; DOI=10.1111/j.1460-9568.1995.tb00666.x; RA Flor P.J., Lindauer K., Puttner I., Ruegg D., Lukic S., Knopfel T., RA Kuhn R.; RT "Molecular cloning, functional expression and pharmacological RT characterization of the human metabotropic glutamate receptor type 2."; RL Eur. J. Neurosci. 7:622-629(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Yasuyuki F., Akiko J.; RT "Structure and polymorphisms of the human metabotropic glutamate receptor RT type 2 (hmGluR2) gene: analysis of association with schizophrenia."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Bonner T.I., Kauffman D., Nagle J.W.; RT "Complete coding sequence of human metabotropic glutamate receptor 2."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH HTR2A, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=18297054; DOI=10.1038/nature06612; RA Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V., RA Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G., RA Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.; RT "Identification of a serotonin/glutamate receptor complex implicated in RT psychosis."; RL Nature 452:93-97(2008). RN [8] RP INTERACTION WITH HTR2A, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ALA-677; ALA-681 AND ALA-685. RX PubMed=23129762; DOI=10.1074/jbc.m112.413161; RA Moreno J.L., Muguruza C., Umali A., Mortillo S., Holloway T., RA Pilar-Cuellar F., Mocci G., Seto J., Callado L.F., Neve R.L., Milligan G., RA Sealfon S.C., Lopez-Gimenez J.F., Meana J.J., Benson D.L., RA Gonzalez-Maeso J.; RT "Identification of three residues essential for 5-hydroxytryptamine 2A- RT metabotropic glutamate 2 (5-HT2A.mGlu2) receptor heteromerization and its RT psychoactive behavioral function."; RL J. Biol. Chem. 287:44301-44319(2012). RN [9] RP INTERACTION WITH HTR2A, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22300836; DOI=10.1016/j.neuropharm.2012.01.010; RA Delille H.K., Becker J.M., Burkhardt S., Bleher B., Terstappen G.C., RA Schmidt M., Meyer A.H., Unger L., Marek G.J., Mezler M.; RT "Heterocomplex formation of 5-HT2A-mGlu2 and its relevance for cellular RT signaling cascades."; RL Neuropharmacology 62:2184-2191(2012). 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, such as adenylate cyclase. Signaling inhibits CC adenylate cyclase activity. May mediate suppression of CC neurotransmission or may be involved in synaptogenesis or synaptic CC stabilization. {ECO:0000269|PubMed:18297054, CC ECO:0000269|PubMed:22300836, ECO:0000269|PubMed:23129762, CC ECO:0000269|PubMed:7620613}. CC -!- SUBUNIT: Interacts with TAMALIN (By similarity). Interacts with HTR2A. CC {ECO:0000250, ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:22300836, CC ECO:0000269|PubMed:23129762}. CC -!- INTERACTION: CC Q14416; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-10232876, EBI-10961679; CC Q14416; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-10232876, EBI-7730807; CC Q14416; Q13520: AQP6; NbExp=3; IntAct=EBI-10232876, EBI-13059134; CC Q14416; Q13323: BIK; NbExp=3; IntAct=EBI-10232876, EBI-700794; CC Q14416; Q8WV48: CCDC107; NbExp=3; IntAct=EBI-10232876, EBI-947033; CC Q14416; P57739: CLDN2; NbExp=3; IntAct=EBI-10232876, EBI-751440; CC Q14416; O95484: CLDN9; NbExp=3; IntAct=EBI-10232876, EBI-18341636; CC Q14416; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10232876, EBI-18013275; CC Q14416; P00387: CYB5R3; NbExp=3; IntAct=EBI-10232876, EBI-1046040; CC Q14416; P27487: DPP4; NbExp=2; IntAct=EBI-10232876, EBI-2871277; CC Q14416; P28223-1: HTR2A; NbExp=4; IntAct=EBI-10232876, EBI-15573967; CC Q14416; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-10232876, EBI-373355; CC Q14416; O14880: MGST3; NbExp=3; IntAct=EBI-10232876, EBI-724754; CC Q14416; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-10232876, EBI-6163737; CC Q14416; Q58DX5: NAALADL2; NbExp=3; IntAct=EBI-10232876, EBI-10178964; CC Q14416; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-10232876, EBI-716063; CC Q14416; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10232876, EBI-3920694; CC Q14416; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-10232876, EBI-10262251; CC Q14416; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-10232876, EBI-9978441; CC Q14416; P27105: STOM; NbExp=3; IntAct=EBI-10232876, EBI-1211440; CC Q14416; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-10232876, EBI-19763514; CC Q14416; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-10232876, EBI-10982110; CC Q14416; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-10232876, EBI-10314986; CC Q14416; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-10232876, EBI-17670824; CC Q14416; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-10232876, EBI-10173939; CC Q14416; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-10232876, EBI-25474821; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Synapse {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level). Widely CC expressed in different regions of the adult brain as well as in fetal CC brain. {ECO:0000269|PubMed:18297054}. 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; L35318; AAA76855.1; -; mRNA. DR EMBL; AB045011; BAB19817.1; -; Genomic_DNA. DR EMBL; AY999299; AAY14640.1; -; mRNA. DR EMBL; EU432122; ABY87921.1; -; mRNA. DR EMBL; CH471055; EAW65150.1; -; Genomic_DNA. DR EMBL; BC113615; AAI13616.1; -; mRNA. DR EMBL; BC113619; AAI13620.1; -; mRNA. DR CCDS; CCDS2834.1; -. DR RefSeq; NP_000830.2; NM_000839.3. DR RefSeq; XP_016861760.1; XM_017006271.1. DR PDB; 4XAQ; X-ray; 2.21 A; A/B=2-493. DR PDB; 4XAS; X-ray; 2.35 A; A/B=2-493. DR PDB; 5CNI; X-ray; 2.69 A; A/B=2-493. DR PDB; 5CNJ; X-ray; 2.65 A; A/B=2-493. DR PDB; 5KZN; X-ray; 2.80 A; A=1-562. DR PDB; 5KZQ; X-ray; 2.80 A; A=1-562. DR PDB; 7E9G; EM; 3.50 A; R/S=19-825. DR PDB; 7EPA; EM; 3.60 A; A/B=19-825. DR PDB; 7EPB; EM; 3.10 A; A/B=19-825. DR PDB; 7EPD; EM; 3.90 A; A=19-825. DR PDB; 7MTQ; EM; 3.65 A; A/B=18-872. DR PDB; 7MTR; EM; 3.30 A; A/B=18-872. DR PDB; 7MTS; EM; 3.20 A; A/B=18-872. DR PDB; 8JCU; EM; 2.80 A; 2=19-872. DR PDB; 8JCV; EM; 3.40 A; 2=19-872. DR PDB; 8JCW; EM; 3.00 A; 2=19-872. DR PDB; 8JCX; EM; 3.00 A; 2=19-872. DR PDB; 8JCY; EM; 2.90 A; 2=19-872. DR PDB; 8JCZ; EM; 3.00 A; 2=19-872. DR PDB; 8JD0; EM; 3.30 A; 2=19-872. DR PDB; 8JD1; EM; 3.70 A; 2=19-872. DR PDB; 8JD2; EM; 2.80 A; 2=19-872. DR PDB; 8JD3; EM; 3.30 A; 2=19-872. DR PDB; 8JD4; EM; 2.90 A; 2=19-872. DR PDB; 8JD5; EM; 3.60 A; 2=19-872. DR PDBsum; 4XAQ; -. DR PDBsum; 4XAS; -. DR PDBsum; 5CNI; -. DR PDBsum; 5CNJ; -. DR PDBsum; 5KZN; -. DR PDBsum; 5KZQ; -. DR PDBsum; 7E9G; -. DR PDBsum; 7EPA; -. DR PDBsum; 7EPB; -. DR PDBsum; 7EPD; -. DR PDBsum; 7MTQ; -. DR PDBsum; 7MTR; -. DR PDBsum; 7MTS; -. DR PDBsum; 8JCU; -. DR PDBsum; 8JCV; -. DR PDBsum; 8JCW; -. DR PDBsum; 8JCX; -. DR PDBsum; 8JCY; -. DR PDBsum; 8JCZ; -. DR PDBsum; 8JD0; -. DR PDBsum; 8JD1; -. DR PDBsum; 8JD2; -. DR PDBsum; 8JD3; -. DR PDBsum; 8JD4; -. DR PDBsum; 8JD5; -. DR AlphaFoldDB; Q14416; -. DR EMDB; EMD-23994; -. DR EMDB; EMD-23995; -. DR EMDB; EMD-23996; -. DR EMDB; EMD-31031; -. DR EMDB; EMD-31235; -. DR EMDB; EMD-31236; -. DR EMDB; EMD-31238; -. DR EMDB; EMD-36174; -. DR EMDB; EMD-36176; -. DR SMR; Q14416; -. DR BioGRID; 109169; 36. DR CORUM; Q14416; -. DR DIP; DIP-59826N; -. DR IntAct; Q14416; 31. DR MINT; Q14416; -. DR STRING; 9606.ENSP00000378492; -. DR BindingDB; Q14416; -. DR ChEMBL; CHEMBL5137; -. DR DrugBank; DB05096; LY2140023. DR DrugCentral; Q14416; -. DR GuidetoPHARMACOLOGY; 290; -. DR TCDB; 9.A.14.7.9; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q14416; 5 sites, No reported glycans. DR GlyGen; Q14416; 5 sites. DR iPTMnet; Q14416; -. DR PhosphoSitePlus; Q14416; -. DR BioMuta; GRM2; -. DR DMDM; 76803802; -. DR MassIVE; Q14416; -. DR PaxDb; 9606-ENSP00000378492; -. DR PeptideAtlas; Q14416; -. DR ProteomicsDB; 59986; -. DR Antibodypedia; 14188; 623 antibodies from 44 providers. DR DNASU; 2912; -. DR Ensembl; ENST00000395052.8; ENSP00000378492.3; ENSG00000164082.15. DR GeneID; 2912; -. DR KEGG; hsa:2912; -. DR MANE-Select; ENST00000395052.8; ENSP00000378492.3; NM_000839.5; NP_000830.2. DR UCSC; uc010hlv.4; human. DR AGR; HGNC:4594; -. DR CTD; 2912; -. DR DisGeNET; 2912; -. DR GeneCards; GRM2; -. DR HGNC; HGNC:4594; GRM2. DR HPA; ENSG00000164082; Tissue enriched (brain). DR MIM; 604099; gene. DR neXtProt; NX_Q14416; -. DR OpenTargets; ENSG00000164082; -. DR PharmGKB; PA28991; -. DR VEuPathDB; HostDB:ENSG00000164082; -. DR eggNOG; KOG1056; Eukaryota. DR GeneTree; ENSGT01030000234595; -. DR InParanoid; Q14416; -. DR OMA; IPWATPS; -. DR OrthoDB; 5388627at2759; -. DR PhylomeDB; Q14416; -. DR TreeFam; TF313240; -. DR PathwayCommons; Q14416; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR SignaLink; Q14416; -. DR SIGNOR; Q14416; -. DR BioGRID-ORCS; 2912; 9 hits in 1154 CRISPR screens. DR GeneWiki; Metabotropic_glutamate_receptor_2; -. DR GenomeRNAi; 2912; -. DR Pharos; Q14416; Tchem. DR PRO; PR:Q14416; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q14416; Protein. DR Bgee; ENSG00000164082; Expressed in cortical plate and 156 other cell types or tissues. DR ExpressionAtlas; Q14416; baseline and differential. DR GO; GO:0097449; C:astrocyte projection; ISS:ARUK-UCL. DR GO; GO:0030424; C:axon; ISS:ARUK-UCL. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl. DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:UniProtKB. DR GO; GO:0008066; F:glutamate receptor activity; TAS:UniProtKB. DR GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IBA:GO_Central. DR GO; GO:0097110; F:scaffold protein binding; ISS:ARUK-UCL. DR GO; GO:0035095; P:behavioral response to nicotine; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0014047; P:glutamate secretion; IEA:Ensembl. DR GO; GO:0090461; P:intracellular glutamate homeostasis; IEA:Ensembl. DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl. DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:ARUK-UCL. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0014048; P:regulation of glutamate secretion; IEA:Ensembl. DR GO; GO:2001023; P:regulation of response to drug; IEA:Ensembl. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR CDD; cd06375; PBP1_mGluR_groupII; 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; IPR001458; GPCR_3_mGluR2. DR InterPro; IPR000162; GPCR_3_mtglu_rcpt. DR InterPro; IPR028082; Peripla_BP_I. DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1. DR PANTHER; PTHR24060:SF147; METABOTROPIC GLUTAMATE RECEPTOR 2; 1. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF07562; NCD3G; 1. DR PRINTS; PR00248; GPCRMGR. DR PRINTS; PR01052; MTABOTROPC2R. DR PRINTS; PR00593; MTABOTROPICR. 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. DR Genevisible; Q14416; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cell projection; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Signal; Synapse; Transducer; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..872 FT /note="Metabotropic glutamate receptor 2" FT /id="PRO_0000012925" FT TOPO_DOM 19..567 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 568..590 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 591..604 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 605..625 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 626..636 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 637..655 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 656..679 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 680..700 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 701..725 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 726..747 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 748..760 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 761..783 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 784..793 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 794..819 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 820..872 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 677..685 FT /note="Important for interaction with HTR2A" FT BINDING 145 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 166..168 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 216 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 295 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 377 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT CARBOHYD 203 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 286 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 338 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 402 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 547 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 50..92 FT /evidence="ECO:0000250" FT DISULFID 234..518 FT /evidence="ECO:0000250" FT DISULFID 355..362 FT /evidence="ECO:0000250" FT DISULFID 400..407 FT /evidence="ECO:0000250" FT DISULFID 500..519 FT /evidence="ECO:0000250" FT DISULFID 504..522 FT /evidence="ECO:0000250" FT DISULFID 525..537 FT /evidence="ECO:0000250" FT DISULFID 540..553 FT /evidence="ECO:0000250" FT MUTAGEN 677 FT /note="A->S: Impairs interaction with HTR2A." FT /evidence="ECO:0000269|PubMed:23129762" FT MUTAGEN 681 FT /note="A->F: Impairs interaction with HTR2A." FT /evidence="ECO:0000269|PubMed:23129762" FT MUTAGEN 685 FT /note="A->G: Impairs interaction with HTR2A." FT /evidence="ECO:0000269|PubMed:23129762" FT CONFLICT 12 FT /note="L -> P (in Ref. 1; AAA76855)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="V -> E (in Ref. 1; AAA76855)" FT /evidence="ECO:0000305" FT CONFLICT 496 FT /note="P -> A (in Ref. 1; AAA76855)" FT /evidence="ECO:0000305" FT CONFLICT 748 FT /note="K -> N (in Ref. 1; AAA76855)" FT /evidence="ECO:0000305" FT CONFLICT 776 FT /note="F -> L (in Ref. 1; AAA76855)" FT /evidence="ECO:0000305" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:8JCW" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 55..58 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 59..74 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:4XAS" FT STRAND 84..90 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 95..106 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:7EPB" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 145..155 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 175..177 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 188..202 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 206..214 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 217..230 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 234..241 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 247..258 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:5CNJ" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 272..284 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 295..299 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 327..332 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 345..352 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 361..364 FT /evidence="ECO:0007829|PDB:5KZQ" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 378..399 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:8JCW" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 415..421 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:4XAQ" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:4XAS" FT STRAND 434..436 FT /evidence="ECO:0007829|PDB:8JD4" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:4XAS" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:8JD0" FT STRAND 453..460 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 461..464 FT /evidence="ECO:0007829|PDB:8JD4" FT STRAND 466..480 FT /evidence="ECO:0007829|PDB:4XAQ" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:4XAQ" FT TURN 486..490 FT /evidence="ECO:0007829|PDB:5KZN" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:8JCW" FT STRAND 508..511 FT /evidence="ECO:0007829|PDB:5KZN" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:8JD2" FT HELIX 517..519 FT /evidence="ECO:0007829|PDB:8JD0" FT STRAND 521..524 FT /evidence="ECO:0007829|PDB:5KZN" FT STRAND 529..533 FT /evidence="ECO:0007829|PDB:5KZN" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:5KZN" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:5KZQ" FT STRAND 553..555 FT /evidence="ECO:0007829|PDB:7MTR" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 564..567 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 569..588 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 592..594 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 596..600 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 603..624 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 628..630 FT /evidence="ECO:0007829|PDB:7EPB" FT HELIX 631..658 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 663..665 FT /evidence="ECO:0007829|PDB:7MTS" FT HELIX 676..698 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 705..708 FT /evidence="ECO:0007829|PDB:7MTS" FT TURN 711..713 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 718..721 FT /evidence="ECO:0007829|PDB:8JCZ" FT HELIX 726..748 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 749..751 FT /evidence="ECO:0007829|PDB:7MTS" FT STRAND 753..755 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 756..783 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 787..806 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 810..818 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:7MTS" SQ SEQUENCE 872 AA; 95568 MW; 801976D034AA8100 CRC64; MGSLLALLAL LLLWGAVAEG PAKKVLTLEG DLVLGGLFPV HQKGGPAEDC GPVNEHRGIQ RLEAMLFALD RINRDPHLLP GVRLGAHILD SCSKDTHALE QALDFVRASL SRGADGSRHI CPDGSYATHG DAPTAITGVI GGSYSDVSIQ VANLLRLFQI PQISYASTSA KLSDKSRYDY FARTVPPDFF QAKAMAEILR FFNWTYVSTV ASEGDYGETG IEAFELEARA RNICVATSEK VGRAMSRAAF EGVVRALLQK PSARVAVLFT RSEDARELLA ASQRLNASFT WVASDGWGAL ESVVAGSEGA AEGAITIELA SYPISDFASY FQSLDPWNNS RNPWFREFWE QRFRCSFRQR DCAAHSLRAV PFEQESKIMF VVNAVYAMAH ALHNMHRALC PNTTRLCDAM RPVNGRRLYK DFVLNVKFDA PFRPADTHNE VRFDRFGDGI GRYNIFTYLR AGSGRYRYQK VGYWAEGLTL DTSLIPWASP SAGPLPASRC SEPCLQNEVK SVQPGEVCCW LCIPCQPYEY RLDEFTCADC GLGYWPNASL TGCFELPQEY IRWGDAWAVG PVTIACLGAL ATLFVLGVFV RHNATPVVKA SGRELCYILL GGVFLCYCMT FIFIAKPSTA VCTLRRLGLG TAFSVCYSAL LTKTNRIARI FGGAREGAQR PRFISPASQV AICLALISGQ LLIVVAWLVV EAPGTGKETA PERREVVTLR CNHRDASMLG SLAYNVLLIA LCTLYAFKTR KCPENFNEAK FIGFTMYTTC IIWLAFLPIF YVTSSDYRVQ TTTMCVSVSL SGSVVLGCLF APKLHIILFQ PQKNVVSHRA PTSRFGSAAA RASSSLGQGS GSQFVPTVCN GREVVDSTTS SL //