GRM2_HUMAN
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 03-AUG-2022, entry version 172.
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}.
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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 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 AlphaFoldDB; Q14416; -.
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 GlyGen; Q14416; 5 sites.
DR iPTMnet; Q14416; -.
DR PhosphoSitePlus; Q14416; -.
DR BioMuta; GRM2; -.
DR DMDM; 76803802; -.
DR MassIVE; Q14416; -.
DR PaxDb; Q14416; -.
DR PeptideAtlas; Q14416; -.
DR PRIDE; Q14416; -.
DR ProteomicsDB; 59986; -.
DR Antibodypedia; 14188; 549 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 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; SLIPWAE; -.
DR OrthoDB; 1154468at2759; -.
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 1076 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 154 other tissues.
DR ExpressionAtlas; Q14416; baseline and differential.
DR Genevisible; Q14416; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
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:0090461; P:glutamate homeostasis; IEA:Ensembl.
DR GO; GO:0014047; P:glutamate secretion; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
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:0051896; P:regulation of protein kinase B signaling; ISS:ARUK-UCL.
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 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; IPR001458; GPCR_3_mGluR2.
DR InterPro; IPR000162; GPCR_3_mtglu_rcpt.
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; PR01052; MTABOTROPC2R.
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; 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 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 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 435..437
FT /evidence="ECO:0007829|PDB:7EPB"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:4XAS"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:4XAQ"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:7EPB"
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 508..511
FT /evidence="ECO:0007829|PDB:5KZN"
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 544..546
FT /evidence="ECO:0007829|PDB:7MTS"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:5KZQ"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:7MTR"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:7EPB"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 569..591
FT /evidence="ECO:0007829|PDB:7EPB"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 603..624
FT /evidence="ECO:0007829|PDB:7EPB"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 632..658
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:7MTS"
FT HELIX 678..700
FT /evidence="ECO:0007829|PDB:7EPB"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:7MTS"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:7E9G"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:7MTS"
FT HELIX 725..746
FT /evidence="ECO:0007829|PDB:7EPB"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:7MTS"
FT HELIX 754..756
FT /evidence="ECO:0007829|PDB:7MTS"
FT HELIX 758..782
FT /evidence="ECO:0007829|PDB:7EPB"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:7EPB"
FT HELIX 787..815
FT /evidence="ECO:0007829|PDB:7EPB"
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
