GRM8_HUMAN
ID GRM8_HUMAN Reviewed; 908 AA.
AC O00222; A4D0Y3; B0FZ74; B0M0L0; O15493; O95945; O95946; Q3MIV9; Q52M02;
AC Q6J165;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Metabotropic glutamate receptor 8;
DE Short=mGluR8;
DE Flags: Precursor;
GN Name=GRM8; Synonyms=GPRC1H, MGLUR8;
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 A).
RX PubMed=9299241; DOI=10.1006/geno.1997.4842;
RA Scherer S.W., Soder S., Duvoisin R.M., Huizenga J.J., Tsui L.-C.;
RT "The human metabotropic glutamate receptor 8 (GRM8) gene: a
RT disproportionately large gene located at 7q31.3-q32.1.";
RL Genomics 44:232-236(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND VARIANT ASN-768.
RX PubMed=9473604; DOI=10.1016/s0169-328x(97)00277-5;
RA Wu S., Wright R.A., Rockey P.K., Burgett S.G., Arnold J.S.,
RA Rosteck P.R. Jr., Johnson B.G., Schoepp D.D., Belagaje R.M.;
RT "Group III human metabotropic glutamate receptors 4, 7 and 8: molecular
RT cloning, functional expression, and comparison of pharmacological
RT properties in RGT cells.";
RL Brain Res. Mol. Brain Res. 53:88-97(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
RC TISSUE=Fetal brain;
RX PubMed=10216218; DOI=10.1016/s0169-328x(99)00050-9;
RA Malherbe P., Kratzeisen C., Lundstrom K., Richards J.G., Faull R.L.M.,
RA Mutel V.;
RT "Cloning and functional expression of alternative spliced variants of the
RT human metabotropic glutamate receptor 8.";
RL Brain Res. Mol. Brain Res. 67:201-210(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Stormann T.M., Simin R.T., Hammerland L.G., Fuller F.H.;
RT "Homo sapiens metabotropic glutamate receptor.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Brain;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-10; THR-265; TYR-362;
RP ASP-368 AND PHE-430.
RG NIEHS SNPs program;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM A), AND VARIANT
RP GLN-343.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Colon;
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).
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. {ECO:0000269|PubMed:9473604}.
CC -!- SUBUNIT: Interacts with PICK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=mGluR8a;
CC IsoId=O00222-1; Sequence=Displayed;
CC Name=B; Synonyms=mGluR8b;
CC IsoId=O00222-2; Sequence=VSP_002032;
CC Name=C; Synonyms=mGluR8c;
CC IsoId=O00222-3; Sequence=VSP_002033, VSP_002034;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/grm8/";
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DR EMBL; U95025; AAB72040.1; -; mRNA.
DR EMBL; U92459; AAB51764.1; -; mRNA.
DR EMBL; AJ236921; CAB36968.1; -; mRNA.
DR EMBL; AJ236922; CAB36969.1; -; mRNA.
DR EMBL; AY608335; AAT37959.1; -; mRNA.
DR EMBL; EU432125; ABY87924.1; -; mRNA.
DR EMBL; EU368948; ABY59657.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24322.1; -; Genomic_DNA.
DR EMBL; BC093725; AAH93725.1; -; mRNA.
DR EMBL; BC101675; AAI01676.1; -; mRNA.
DR CCDS; CCDS47696.1; -. [O00222-2]
DR CCDS; CCDS5794.1; -. [O00222-1]
DR RefSeq; NP_000836.2; NM_000845.2. [O00222-1]
DR RefSeq; NP_001120795.1; NM_001127323.1. [O00222-2]
DR RefSeq; XP_006716001.1; XM_006715938.3.
DR RefSeq; XP_011514393.1; XM_011516091.1.
DR RefSeq; XP_011514394.1; XM_011516092.2.
DR RefSeq; XP_016867563.1; XM_017012074.1.
DR PDB; 6BSZ; X-ray; 2.65 A; A/B=37-514.
DR PDB; 6BT5; X-ray; 2.92 A; A/B=37-514.
DR PDB; 6E5V; X-ray; 2.95 A; A/B=2-508.
DR PDBsum; 6BSZ; -.
DR PDBsum; 6BT5; -.
DR PDBsum; 6E5V; -.
DR AlphaFoldDB; O00222; -.
DR SMR; O00222; -.
DR BioGRID; 109175; 1.
DR CORUM; O00222; -.
DR IntAct; O00222; 1.
DR STRING; 9606.ENSP00000344173; -.
DR BindingDB; O00222; -.
DR ChEMBL; CHEMBL3228; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugCentral; O00222; -.
DR GuidetoPHARMACOLOGY; 296; -.
DR GlyGen; O00222; 5 sites.
DR iPTMnet; O00222; -.
DR PhosphoSitePlus; O00222; -.
DR BioMuta; GRM8; -.
DR MassIVE; O00222; -.
DR PaxDb; O00222; -.
DR PeptideAtlas; O00222; -.
DR PRIDE; O00222; -.
DR Antibodypedia; 17706; 380 antibodies from 34 providers.
DR DNASU; 2918; -.
DR Ensembl; ENST00000339582.7; ENSP00000344173.2; ENSG00000179603.18. [O00222-1]
DR Ensembl; ENST00000341617.7; ENSP00000345747.3; ENSG00000179603.18. [O00222-3]
DR Ensembl; ENST00000358373.7; ENSP00000351142.3; ENSG00000179603.18. [O00222-2]
DR Ensembl; ENST00000472701.5; ENSP00000419832.1; ENSG00000179603.18. [O00222-2]
DR GeneID; 2918; -.
DR KEGG; hsa:2918; -.
DR MANE-Select; ENST00000339582.7; ENSP00000344173.2; NM_000845.3; NP_000836.2.
DR UCSC; uc003vlr.3; human. [O00222-1]
DR CTD; 2918; -.
DR DisGeNET; 2918; -.
DR GeneCards; GRM8; -.
DR HGNC; HGNC:4600; GRM8.
DR HPA; ENSG00000179603; Group enriched (brain, choroid plexus).
DR MIM; 601116; gene.
DR neXtProt; NX_O00222; -.
DR OpenTargets; ENSG00000179603; -.
DR PharmGKB; PA28997; -.
DR VEuPathDB; HostDB:ENSG00000179603; -.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT01030000234648; -.
DR HOGENOM; CLU_005389_0_0_1; -.
DR InParanoid; O00222; -.
DR OMA; MNQDISE; -.
DR OrthoDB; 483746at2759; -.
DR PhylomeDB; O00222; -.
DR TreeFam; TF313240; -.
DR PathwayCommons; O00222; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR SignaLink; O00222; -.
DR SIGNOR; O00222; -.
DR BioGRID-ORCS; 2918; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; GRM8; human.
DR GeneWiki; Metabotropic_glutamate_receptor_8; -.
DR GenomeRNAi; 2918; -.
DR Pharos; O00222; Tchem.
DR PRO; PR:O00222; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O00222; protein.
DR Bgee; ENSG00000179603; Expressed in left testis and 135 other tissues.
DR ExpressionAtlas; O00222; baseline and differential.
DR Genevisible; O00222; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB.
DR GO; GO:0001642; F:group III metabotropic glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0007196; P:adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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; IPR000144; GPCR_3_mGluR8.
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; PR01058; MTABOTROPC8R.
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; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Isopeptide bond; Membrane;
KW Receptor; Reference proteome; Sensory transduction; Signal; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..908
FT /note="Metabotropic glutamate receptor 8"
FT /id="PRO_0000012941"
FT TOPO_DOM 34..583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..608
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..768
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..803
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..843
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 177..179
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..106
FT /evidence="ECO:0000250"
FT DISULFID 246..534
FT /evidence="ECO:0000250"
FT DISULFID 369..384
FT /evidence="ECO:0000250"
FT DISULFID 424..431
FT /evidence="ECO:0000250"
FT DISULFID 516..535
FT /evidence="ECO:0000250"
FT DISULFID 520..538
FT /evidence="ECO:0000250"
FT DISULFID 541..553
FT /evidence="ECO:0000250"
FT DISULFID 556..569
FT /evidence="ECO:0000250"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P47743"
FT VAR_SEQ 454..501
FT /note="SAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVED ->
FT CRRGIQMSLPWPTLFTPSFSSSWAVLALLSLLMKTEMLLDVMISSSIK (in
FT isoform C)"
FT /evidence="ECO:0000303|PubMed:10216218"
FT /id="VSP_002033"
FT VAR_SEQ 502..908
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10216218"
FT /id="VSP_002034"
FT VAR_SEQ 893..908
FT /note="TSSTKTTYISYSNHSI -> SKSSVEFPMVKSGSTS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10216218, ECO:0000303|Ref.4"
FT /id="VSP_002032"
FT VARIANT 10
FT /note="S -> C (in dbSNP:rs769194)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014446"
FT VARIANT 21
FT /note="F -> C (in dbSNP:rs769202)"
FT /id="VAR_014447"
FT VARIANT 265
FT /note="I -> T (in dbSNP:rs17150343)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_049278"
FT VARIANT 343
FT /note="R -> Q (in dbSNP:rs13309334)"
FT /evidence="ECO:0000269|PubMed:12853948"
FT /id="VAR_054752"
FT VARIANT 362
FT /note="F -> Y (in dbSNP:rs78124913)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_054477"
FT VARIANT 368
FT /note="G -> D (in dbSNP:rs78947184)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_054478"
FT VARIANT 392
FT /note="R -> Q (in dbSNP:rs2234947)"
FT /id="VAR_014448"
FT VARIANT 430
FT /note="L -> F (in dbSNP:rs75863532)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_054479"
FT VARIANT 548
FT /note="V -> G (in dbSNP:rs2234948)"
FT /id="VAR_014449"
FT VARIANT 768
FT /note="I -> N (in dbSNP:rs1051433)"
FT /evidence="ECO:0000269|PubMed:9473604"
FT /id="VAR_054753"
FT VARIANT 902
FT /note="S -> I (in dbSNP:rs10225567)"
FT /id="VAR_054754"
FT CONFLICT 194
FT /note="R -> A (in Ref. 1; AAB72040)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="T -> I (in Ref. 1; AAB72040)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="A -> V (in Ref. 5; ABY87924)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="A -> G (in Ref. 1; AAB72040)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="S -> T (in Ref. 1; AAB72040)"
FT /evidence="ECO:0000305"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 316..320
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 322..327
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:6BSZ"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 402..423
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:6BT5"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:6E5V"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:6BT5"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:6BT5"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:6BSZ"
FT STRAND 483..497
FT /evidence="ECO:0007829|PDB:6BSZ"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:6BSZ"
SQ SEQUENCE 908 AA; 101741 MW; 95C2D5883DAF6FDE CRC64;
MVCEGKRSAS CPCFFLLTAK FYWILTMMQR THSQEYAHSI RVDGDIILGG LFPVHAKGER
GVPCGELKKE KGIHRLEAML YAIDQINKDP DLLSNITLGV RILDTCSRDT YALEQSLTFV
QALIEKDASD VKCANGDPPI FTKPDKISGV IGAAASSVSI MVANILRLFK IPQISYASTA
PELSDNTRYD FFSRVVPPDS YQAQAMVDIV TALGWNYVST LASEGNYGES GVEAFTQISR
EIGGVCIAQS QKIPREPRPG EFEKIIKRLL ETPNARAVIM FANEDDIRRI LEAAKKLNQS
GHFLWIGSDS WGSKIAPVYQ QEEIAEGAVT ILPKRASIDG FDRYFRSRTL ANNRRNVWFA
EFWEENFGCK LGSHGKRNSH IKKCTGLERI ARDSSYEQEG KVQFVIDAVY SMAYALHNMH
KDLCPGYIGL CPRMSTIDGK ELLGYIRAVN FNGSAGTPVT FNENGDAPGR YDIFQYQITN
KSTEYKVIGH WTNQLHLKVE DMQWAHREHT HPASVCSLPC KPGERKKTVK GVPCCWHCER
CEGYNYQVDE LSCELCPLDQ RPNMNRTGCQ LIPIIKLEWH SPWAVVPVFV AILGIIATTF
VIVTFVRYND TPIVRASGRE LSYVLLTGIF LCYSITFLMI AAPDTIICSF RRVFLGLGMC
FSYAALLTKT NRIHRIFEQG KKSVTAPKFI SPASQLVITF SLISVQLLGV FVWFVVDPPH
IIIDYGEQRT LDPEKARGVL KCDISDLSLI CSLGYSILLM VTCTVYAIKT RGVPETFNEA
KPIGFTMYTT CIIWLAFIPI FFGTAQSAEK MYIQTTTLTV SMSLSASVSL GMLYMPKVYI
IIFHPEQNVQ KRKRSFKAVV TAATMQSKLI QKGNDRPNGE VKSELCESLE TNTSSTKTTY
ISYSNHSI
