ID GRM3_HUMAN Reviewed; 879 AA. AC Q14832; Q2PNZ6; Q75MV4; Q75N17; Q86YG6; Q8TBH9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 27-MAR-2024, entry version 196. DE RecName: Full=Metabotropic glutamate receptor 3; DE Short=mGluR3; DE Flags: Precursor; GN Name=GRM3; Synonyms=GPRC1C, MGLUR3; 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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=8840013; DOI=10.1016/0169-328x(96)00037-x; RA Makoff A., Volpe F., Lelchuk R., Harrington K., Emson P.; RT "Molecular characterization and localization of human metabotropic RT glutamate receptor type 3."; RL Brain Res. Mol. Brain Res. 40:55-63(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Lymphoblast; RX PubMed=16417579; DOI=10.1111/j.1471-4159.2005.03609.x; RA Sartorius L.J., Nagappan G., Lipska B.K., Lu B., Sei Y., Ren-Patterson R., RA Li Z., Weinberger D.R., Harrison P.J.; RT "Alternative splicing of human metabotropic glutamate receptor 3."; RL J. Neurochem. 96:1139-1148(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 26-504 OF MUTANT SER-240, AND RP DISULFIDE BONDS. RG Structural genomics consortium (SGC); RT "Crystal structure of metabotropic glutamate receptor 3 precursor in RT presence of LY341495 antagonist."; RL Submitted (JUL-2011) to the PDB data bank. 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 inhibits adenylate cyclase activity. CC {ECO:0000269|PubMed:8840013}. CC -!- SUBUNIT: Interacts with TAMALIN. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8840013}; CC Multi-pass membrane protein {ECO:0000269|PubMed:8840013}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14832-1; Sequence=Displayed; CC Name=2; Synonyms=GRM3Delta4; CC IsoId=Q14832-2; Sequence=VSP_047679, VSP_047680; CC -!- TISSUE SPECIFICITY: Detected in brain cortex, thalamus, subthalamic CC nucleus, substantia nigra, hypothalamus, hippocampus, corpus callosum, CC caudate nucleus and amygdala. {ECO:0000269|PubMed:8840013}. CC -!- MISCELLANEOUS: [Isoform 2]: Appears to be membrane-associated, despite CC the absence of the seven-transmembrane domain. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD15616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=ABC47402.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA54796.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; X77748; CAA54796.1; ALT_INIT; mRNA. DR EMBL; DQ315361; ABC47402.1; ALT_INIT; mRNA. DR EMBL; AC004829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005009; AAD15616.1; ALT_INIT; Genomic_DNA. DR EMBL; AC002081; AAC60379.2; -; Genomic_DNA. DR EMBL; BC022496; AAH22496.2; -; mRNA. DR EMBL; BC041407; AAH41407.1; -; mRNA. DR CCDS; CCDS5600.1; -. [Q14832-1] DR CCDS; CCDS87515.1; -. [Q14832-2] DR RefSeq; NP_000831.2; NM_000840.2. [Q14832-1] DR RefSeq; XP_011514390.1; XM_011516088.1. DR PDB; 3SM9; X-ray; 2.26 A; A=26-504. DR PDB; 4XAR; X-ray; 2.26 A; A=2-508. DR PDB; 5CNK; X-ray; 3.15 A; A/B/C=2-507. DR PDB; 5CNM; X-ray; 2.84 A; A=2-507. DR PDB; 6B7H; X-ray; 2.82 A; A=2-507. DR PDB; 7WI6; EM; 3.71 A; A/B=23-879. DR PDB; 7WI8; EM; 4.17 A; A/B=23-879. DR PDB; 7WIH; EM; 3.68 A; A/B=23-879. DR PDB; 8JCU; EM; 2.80 A; 3=23-879. DR PDB; 8JCV; EM; 3.40 A; 3=23-879. DR PDB; 8JCW; EM; 3.00 A; 3=23-879. DR PDB; 8JCX; EM; 3.00 A; 3=23-879. DR PDB; 8JCY; EM; 2.90 A; 3=23-879. DR PDB; 8JCZ; EM; 3.00 A; 3=23-879. DR PDB; 8JD0; EM; 3.30 A; 3=23-879. DR PDB; 8JD1; EM; 3.70 A; 3=23-879. DR PDB; 8JD2; EM; 2.80 A; 3=23-879. DR PDB; 8JD3; EM; 3.30 A; 3=23-879. DR PDBsum; 3SM9; -. DR PDBsum; 4XAR; -. DR PDBsum; 5CNK; -. DR PDBsum; 5CNM; -. DR PDBsum; 6B7H; -. DR PDBsum; 7WI6; -. DR PDBsum; 7WI8; -. DR PDBsum; 7WIH; -. 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 AlphaFoldDB; Q14832; -. DR EMDB; EMD-32526; -. DR EMDB; EMD-32527; -. DR EMDB; EMD-32530; -. DR EMDB; EMD-36174; -. DR SMR; Q14832; -. DR BioGRID; 109170; 8. DR CORUM; Q14832; -. DR IntAct; Q14832; 1. DR STRING; 9606.ENSP00000355316; -. DR BindingDB; Q14832; -. DR ChEMBL; CHEMBL2888; -. DR DrugBank; DB05096; LY2140023. DR DrugCentral; Q14832; -. DR GuidetoPHARMACOLOGY; 291; -. DR GlyCosmos; Q14832; 4 sites, No reported glycans. DR GlyGen; Q14832; 4 sites. DR iPTMnet; Q14832; -. DR PhosphoSitePlus; Q14832; -. DR BioMuta; GRM3; -. DR DMDM; 76803803; -. DR MassIVE; Q14832; -. DR PaxDb; 9606-ENSP00000355316; -. DR PeptideAtlas; Q14832; -. DR ProteomicsDB; 60202; -. [Q14832-1] DR ProteomicsDB; 61428; -. DR Antibodypedia; 15243; 443 antibodies from 35 providers. DR DNASU; 2913; -. DR Ensembl; ENST00000361669.7; ENSP00000355316.2; ENSG00000198822.11. [Q14832-1] DR Ensembl; ENST00000439827.1; ENSP00000398767.1; ENSG00000198822.11. [Q14832-2] DR GeneID; 2913; -. DR KEGG; hsa:2913; -. DR MANE-Select; ENST00000361669.7; ENSP00000355316.2; NM_000840.3; NP_000831.2. DR UCSC; uc003uid.4; human. [Q14832-1] DR AGR; HGNC:4595; -. DR CTD; 2913; -. DR DisGeNET; 2913; -. DR GeneCards; GRM3; -. DR HGNC; HGNC:4595; GRM3. DR HPA; ENSG00000198822; Tissue enriched (brain). DR MIM; 601115; gene. DR neXtProt; NX_Q14832; -. DR OpenTargets; ENSG00000198822; -. DR PharmGKB; PA28992; -. DR VEuPathDB; HostDB:ENSG00000198822; -. DR eggNOG; KOG1056; Eukaryota. DR GeneTree; ENSGT01030000234595; -. DR HOGENOM; CLU_005389_0_0_1; -. DR InParanoid; Q14832; -. DR OMA; ILKCNIQ; -. DR OrthoDB; 5388627at2759; -. DR PhylomeDB; Q14832; -. DR TreeFam; TF313240; -. DR PathwayCommons; Q14832; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR SignaLink; Q14832; -. DR SIGNOR; Q14832; -. DR BioGRID-ORCS; 2913; 11 hits in 1147 CRISPR screens. DR ChiTaRS; GRM3; human. DR GeneWiki; Metabotropic_glutamate_receptor_3; -. DR GenomeRNAi; 2913; -. DR Pharos; Q14832; Tchem. DR PRO; PR:Q14832; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q14832; Protein. DR Bgee; ENSG00000198822; Expressed in endothelial cell and 102 other cell types or tissues. DR ExpressionAtlas; Q14832; 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:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. 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: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:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR CDD; cd15448; 7tmC_mGluR3; 1. 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; IPR001234; GPCR_3_mGluR3. DR InterPro; IPR000162; GPCR_3_mtglu_rcpt. DR InterPro; IPR028082; Peripla_BP_I. DR PANTHER; PTHR24060; METABOTROPIC GLUTAMATE RECEPTOR; 1. DR PANTHER; PTHR24060:SF160; METABOTROPIC GLUTAMATE RECEPTOR 3; 1. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF07562; NCD3G; 1. DR PRINTS; PR00248; GPCRMGR. DR PRINTS; PR01053; MTABOTROPC3R. 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; Q14832; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..879 FT /note="Metabotropic glutamate receptor 3" FT /id="PRO_0000012927" FT TOPO_DOM 23..576 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 577..599 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 600..613 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 614..634 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 635..645 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 646..664 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 665..688 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 689..709 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 710..734 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 735..756 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 757..769 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 770..792 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 793..802 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 803..828 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 829..879 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT BINDING 151 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 172..174 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 301 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT BINDING 389 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250" FT CARBOHYD 209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 292 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 439 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 57..99 FT /evidence="ECO:0000269|Ref.5" FT DISULFID 240..527 FT /evidence="ECO:0000250" FT DISULFID 361..373 FT /evidence="ECO:0000269|Ref.5" FT DISULFID 412..419 FT /evidence="ECO:0000269|Ref.5" FT DISULFID 509..528 FT /evidence="ECO:0000250" FT DISULFID 513..531 FT /evidence="ECO:0000250" FT DISULFID 534..546 FT /evidence="ECO:0000250" FT DISULFID 549..562 FT /evidence="ECO:0000250" FT VAR_SEQ 442..537 FT /note="APFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLD FT VNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPY -> GADDNHVHLCQ FT PEWLCGLGLFVCTQGSHHPVSTPEECCHTQTAPQQVQCQWNWDHILSVLCKHVCANGVQ FT WAGSPRLHHLISVIVNCSSVLVFLDC (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16417579" FT /id="VSP_047679" FT VAR_SEQ 538..879 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16417579" FT /id="VSP_047680" FT VARIANT 475 FT /note="G -> D (in dbSNP:rs17161026)" FT /id="VAR_049274" FT CONFLICT 96 FT /note="L -> F (in Ref. 4; AAH41407)" FT /evidence="ECO:0000305" FT CONFLICT 446 FT /note="P -> T (in Ref. 4; AAH22496)" FT /evidence="ECO:0000305" FT CONFLICT 512 FT /note="P -> A (in Ref. 4; AAH22496)" FT /evidence="ECO:0000305" FT CONFLICT 856 FT /note="S -> Y (in Ref. 4; AAH22496)" FT /evidence="ECO:0000305" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:8JCZ" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 66..81 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 142..146 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 151..161 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 168..172 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 181..186 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 212..220 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 221..235 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 240..247 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:8JD3" FT HELIX 253..264 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 271..275 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 278..290 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 301..305 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 307..310 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 314..319 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 331..338 FT /evidence="ECO:0007829|PDB:3SM9" FT TURN 342..344 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 351..359 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 381..383 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 390..411 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:8JD3" FT HELIX 420..423 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 427..433 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:4XAR" FT TURN 443..446 FT /evidence="ECO:0007829|PDB:8JCW" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:4XAR" FT STRAND 466..476 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 478..492 FT /evidence="ECO:0007829|PDB:3SM9" FT HELIX 494..496 FT /evidence="ECO:0007829|PDB:3SM9" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 507..510 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 515..517 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 518..521 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 530..533 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:8JCX" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 550..555 FT /evidence="ECO:0007829|PDB:8JD2" FT STRAND 556..560 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:8JCV" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:8JD2" FT HELIX 575..600 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 602..606 FT /evidence="ECO:0007829|PDB:8JD2" FT HELIX 611..632 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 640..664 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 683..699 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 700..702 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 703..706 FT /evidence="ECO:0007829|PDB:8JCU" FT STRAND 711..714 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 718..720 FT /evidence="ECO:0007829|PDB:8JCW" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:8JCU" FT TURN 730..732 FT /evidence="ECO:0007829|PDB:8JCX" FT HELIX 734..757 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 762..764 FT /evidence="ECO:0007829|PDB:8JD0" FT HELIX 765..791 FT /evidence="ECO:0007829|PDB:8JCU" FT HELIX 797..825 FT /evidence="ECO:0007829|PDB:8JCU" SQ SEQUENCE 879 AA; 98879 MW; 7EB84521676E8304 CRC64; MKMLTRLQVL TLALFSKGFL LSLGDHNFLR REIKIEGDLV LGGLFPINEK GTGTEECGRI NEDRGIQRLE AMLFAIDEIN KDDYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD KSRYDYFART VPPDFYQAKA MAEILRFFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAASR ANASFTWVAS DGWGAQESII KGSEHVAYGA ITLELASQPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ CSLQNKRNHR RVCDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD AMKILDGKKL YKDYLLKINF TAPFNPNKDA DSIVKFDTFG DGMGRYNVFN FQNVGGKYSY LKVGHWAETL SLDVNSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL ADEFTCMDCG SGQWPTADLT GCYDLPEDYI RWEDAWAIGP VTIACLGFMC TCMVVTVFIK HNNTPLVKAS GRELCYILLF GVGLSYCMTF FFIAKPSPVI CALRRLGLGS SFAICYSALL TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE APGTRRYTLA EKRETVILKC NVKDSSMLIS LTYDVILVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIILFQP QKNVVTHRLH LNRFSVSGTG TTYSQSSAST YVPTVCNGRE VLDSTTSSL //