GLR33_ARATH
ID GLR33_ARATH Reviewed; 933 AA.
AC Q9C8E7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glutamate receptor 3.3 {ECO:0000303|PubMed:11379626};
DE Short=AtGLR3.3 {ECO:0000303|PubMed:11379626};
DE AltName: Full=Glutamate receptor-like protein 3.3 {ECO:0000303|PubMed:12082126};
DE AltName: Full=Ligand-gated ion channel 3.3 {ECO:0000303|PubMed:11379626};
DE Flags: Precursor;
GN Name=GLR3.3 {ECO:0000303|PubMed:11379626};
GN OrderedLocusNames=At1g42540 {ECO:0000312|Araport:AT1G42540};
GN ORFNames=T8D8.1 {ECO:0000312|EMBL:AAG51316.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11379626; DOI=10.1126/science.292.5521.1486b;
RA Lacombe B., Becker D., Hedrich R., DeSalle R., Hollmann M., Kwak J.M.,
RA Schroeder J.I., Le Novere N., Nam H.G., Spalding E.P., Tester M.,
RA Turano F.J., Chiu J., Coruzzi G.;
RT "The identity of plant glutamate receptors.";
RL Science 292:1486-1487(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12082126; DOI=10.1093/oxfordjournals.molbev.a004165;
RA Chiu J.C., Brenner E.D., DeSalle R., Nitabach M.N., Holmes T.C.,
RA Coruzzi G.M.;
RT "Phylogenetic and expression analysis of the glutamate-receptor-like gene
RT family in Arabidopsis thaliana.";
RL Mol. Biol. Evol. 19:1066-1082(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17012403; DOI=10.1104/pp.106.088989;
RA Qi Z., Stephens N.R., Spalding E.P.;
RT "Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a
RT broad agonist profile.";
RL Plant Physiol. 142:963-971(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18162597; DOI=10.1104/pp.107.108134;
RA Stephens N.R., Qi Z., Spalding E.P.;
RT "Glutamate receptor subtypes evidenced by differences in desensitization
RT and dependence on the GLR3.3 and GLR3.4 genes.";
RL Plant Physiol. 146:529-538(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23969459; DOI=10.1038/nature12478;
RA Mousavi S.A., Chauvin A., Pascaud F., Kellenberger S., Farmer E.E.;
RT "GLUTAMATE RECEPTOR-LIKE genes mediate leaf-to-leaf wound signalling.";
RL Nature 500:422-426(2013).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23590882; DOI=10.1105/tpc.113.110668;
RA Vincill E.D., Clarin A.E., Molenda J.N., Spalding E.P.;
RT "Interacting glutamate receptor-like proteins in phloem regulate lateral
RT root initiation in Arabidopsis.";
RL Plant Cell 25:1304-1313(2013).
RN [9]
RP FUNCTION.
RX PubMed=23952652; DOI=10.1111/tpj.12311;
RA Manzoor H., Kelloniemi J., Chiltz A., Wendehenne D., Pugin A., Poinssot B.,
RA Garcia-Brugger A.;
RT "Involvement of the glutamate receptor AtGLR3.3 in plant defense signaling
RT and resistance to Hyaloperonospora arabidopsidis.";
RL Plant J. 76:466-480(2013).
RN [10]
RP FUNCTION.
RX PubMed=23656893; DOI=10.1104/pp.113.217208;
RA Li F., Wang J., Ma C., Zhao Y., Wang Y., Hasi A., Qi Z.;
RT "Glutamate receptor-like channel3.3 is involved in mediating glutathione-
RT triggered cytosolic calcium transients, transcriptional changes, and innate
RT immunity responses in Arabidopsis.";
RL Plant Physiol. 162:1497-1509(2013).
RN [11]
RP FUNCTION.
RX PubMed=24716546; DOI=10.1111/nph.12807;
RA Salvador-Recatala V., Tjallingii W.F., Farmer E.E.;
RT "Real-time, in vivo intracellular recordings of caterpillar-induced
RT depolarization waves in sieve elements using aphid electrodes.";
RL New Phytol. 203:674-684(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 463-570 AND 681-813 IN COMPLEX
RP WITH L-GLUTATMATE; GLYCINE; L-CYSTEINE AND L-METHIONINE, AND DISULFIDE
RP BOND.
RX PubMed=31871183; DOI=10.1073/pnas.1905142117;
RA Alfieri A., Doccula F.G., Pederzoli R., Grenzi M., Bonza M.C., Luoni L.,
RA Candeo A., Romano Armada N., Barbiroli A., Valentini G., Schneider T.R.,
RA Bassi A., Bolognesi M., Nardini M., Costa A.;
RT "The structural bases for agonist diversity in an Arabidopsis thaliana
RT glutamate receptor-like channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:752-760(2020).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel, at least in roots and hypocotyls (Probable). Can be
CC triggered by Ala, Asn, Cys, Glu, Gly, Ser and glutathione (a tripeptide
CC consisting of Glu-Gly-Cys) (PubMed:18162597). Mediates leaf-to-leaf
CC wound signaling (PubMed:23969459). May be involved in light-signal
CC transduction and calcium homeostasis via the regulation of calcium
CC influx into cells (PubMed:17012403). Contributes to pathogen-associated
CC molecular patterns (PAMP) elicitor-mediated resistance
CC (PubMed:23952652). Partially involved in free cytosolic calcium
CC variations, nitric oxide (NO) production, reactive oxygen species (ROS)
CC production and expression of defense-related genes in response to
CC oligogalacturonide elicitors (PubMed:23952652). Inovlved in resistance
CC against Hyaloperonospora arabidopsidis (PubMed:23952652). Required for
CC glutathione-induced defense responses, and innate immunity responses
CC against the bacterial pathogen Pseudomonas syringae pv tomato strain
CC DC3000 (PubMed:23656893). Required for the transmission of wound-
CC induced, phloem-propagated action potential to neighbor leaves
CC (PubMed:24716546). {ECO:0000269|PubMed:17012403,
CC ECO:0000269|PubMed:18162597, ECO:0000269|PubMed:23656893,
CC ECO:0000269|PubMed:23952652, ECO:0000269|PubMed:23969459,
CC ECO:0000269|PubMed:24716546, ECO:0000305|PubMed:17012403}.
CC -!- SUBUNIT: May form heteromers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23590882};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma
CC membrane. {ECO:0000269|PubMed:23590882}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots and siliques.
CC {ECO:0000269|PubMed:12082126}.
CC -!- DISRUPTION PHENOTYPE: Impaired glutamate-triggered (and Ala, Asn, Cys,
CC Gly, Ser and glutathione-triggered) membrane depolarization and calcium
CC rise (PubMed:17012403, PubMed:18162597). Reduced wound-activated
CC surface potential changes (WASP) duration in the wounded leaf,
CC resulting in a decreased induction of the regulators of jasmonate-
CC signaling in the systemic leaves (PubMed:23969459). Glr3.3 and glr3.6
CC double mutant has no detectable changes in surface potential in
CC systemic leaves and the induction of the regulators of jasmonate-
CC signaling is more strongly decreased (PubMed:23969459).
CC {ECO:0000269|PubMed:17012403, ECO:0000269|PubMed:18162597,
CC ECO:0000269|PubMed:23969459}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
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DR EMBL; AC025815; AAG51316.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31925.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59840.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59841.1; -; Genomic_DNA.
DR PIR; C96495; C96495.
DR RefSeq; NP_001322169.1; NM_001333200.1.
DR RefSeq; NP_001322170.1; NM_001333202.1.
DR RefSeq; NP_174978.1; NM_103438.3.
DR PDB; 6R85; X-ray; 2.00 A; A/B=463-570, A/B=681-813.
DR PDB; 6R88; X-ray; 1.60 A; A/B/C/D=463-570, A/B/C/D=681-813.
DR PDB; 6R89; X-ray; 2.50 A; A/B/C/D=463-570, A/B/C/D=681-813.
DR PDB; 6R8A; X-ray; 3.10 A; A/B/C/D=463-570, A/B/C/D=681-813.
DR PDBsum; 6R85; -.
DR PDBsum; 6R88; -.
DR PDBsum; 6R89; -.
DR PDBsum; 6R8A; -.
DR AlphaFoldDB; Q9C8E7; -.
DR SMR; Q9C8E7; -.
DR BioGRID; 26087; 2.
DR STRING; 3702.AT1G42540.1; -.
DR TCDB; 1.A.10.1.10; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR iPTMnet; Q9C8E7; -.
DR PaxDb; Q9C8E7; -.
DR PRIDE; Q9C8E7; -.
DR ProteomicsDB; 247364; -.
DR EnsemblPlants; AT1G42540.1; AT1G42540.1; AT1G42540.
DR EnsemblPlants; AT1G42540.2; AT1G42540.2; AT1G42540.
DR EnsemblPlants; AT1G42540.4; AT1G42540.4; AT1G42540.
DR GeneID; 840859; -.
DR Gramene; AT1G42540.1; AT1G42540.1; AT1G42540.
DR Gramene; AT1G42540.2; AT1G42540.2; AT1G42540.
DR Gramene; AT1G42540.4; AT1G42540.4; AT1G42540.
DR KEGG; ath:AT1G42540; -.
DR Araport; AT1G42540; -.
DR TAIR; locus:2206095; AT1G42540.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q9C8E7; -.
DR OMA; FNYTFKL; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q9C8E7; -.
DR PRO; PR:Q9C8E7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8E7; baseline and differential.
DR Genevisible; Q9C8E7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; IMP:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IMP:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IMP:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB.
DR CDD; cd19990; PBP1_GABAb_receptor_plant; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR044440; GABAb_receptor_plant_PBP1.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR017103; Iontropic_Glu_rcpt_pln.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PIRSF; PIRSF037090; Iontro_Glu-like_rcpt_pln; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..933
FT /note="Glutamate receptor 3.3"
FT /id="PRO_0000011607"
FT TOPO_DOM 24..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 890..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85"
FT BINDING 543..545
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R88"
FT BINDING 543..545
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R89"
FT BINDING 543..545
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85"
FT BINDING 543..545
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R8A"
FT BINDING 550
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R88"
FT BINDING 550
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R89"
FT BINDING 550
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85"
FT BINDING 550
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R8A"
FT BINDING 702
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R88"
FT BINDING 702
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R89"
FT BINDING 702
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85"
FT BINDING 702
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R8A"
FT BINDING 746..749
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R88"
FT BINDING 746..749
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R89"
FT BINDING 746..749
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85"
FT BINDING 746..749
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R8A"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 758..812
FT /evidence="ECO:0000269|PubMed:31871183,
FT ECO:0007744|PDB:6R85, ECO:0007744|PDB:6R88,
FT ECO:0007744|PDB:6R89, ECO:0007744|PDB:6R8A"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:6R88"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:6R8A"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 538..545
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 685..690
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 703..709
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 724..733
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 735..737
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 741..746
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 747..755
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:6R88"
FT STRAND 772..776
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 781..795
FT /evidence="ECO:0007829|PDB:6R88"
FT HELIX 798..807
FT /evidence="ECO:0007829|PDB:6R88"
SQ SEQUENCE 933 AA; 104689 MW; BB6DD65FDB97F975 CRC64;
MKQLWTFFFL SFLCSGLFRR THSEKPKVVK IGSIFSFDSV IGKVAKIAID EAVKDVNSNP
DILSGTKFSV SMQNSNCSGF MGMVEALRFM EKDIVGIIGP QCSVVAHMIS HMANELRVPL
LSFAVTDPVM SPLQFPYFIR TTQSDLYQMD AIASIVDFYG WKEVIAVFVD DDFGRNGVAA
LNDKLASRRL RITYKAGLHP DTAVNKNEIM NMLIKIMLLQ PRIVVIHVYS ELGFAVFKEA
KYLGMMGNGY VWIATDWLST NLDSSSPLPA ERLETIQGVL VLRPHTPDSD FKREFFKRWR
KMSGASLALN TYGLYAYDSV MLLARGLDKF FKDGGNISFS NHSMLNTLGK SGNLNLEAMT
VFDGGEALLK DILGTRMVGL TGQLQFTPDR SRTRPAYDII NVAGTGVRQI GYWSNHSGLS
TVLPELLYTK EKPNMSTSPK LKHVIWPGET FTKPRGWVFS NNGKELKIGV PLRVSYKEFV
SQIRGTENMF KGFCIDVFTA AVNLLPYAVP VKFIPYGNGK ENPSYTHMVE MITTGNFDGV
VGDVAIVTNR TKIVDFTQPY AASGLVVVAP FKKLNSGAWA FLRPFNRLMW AVTGCCFLFV
GIVVWILEHR TNDEFRGPPK RQCVTILWFS FSTMFFAHRE NTVSTLGRLV LIIWLFVVLI
INSSYTASLT SILTVQQLSS PIKGIESLRE RDDPIGYQVG SFAESYLRNE LNISESRLVP
LGTPEAYAKA LKDGPSKGGV AAIVDERPYV ELFLSSNCAY RIVGQEFTKS GWGFAFPRDS
PLAIDLSTAI LELAENGDLQ RIHDKWLMKN ACTLENAELE SDRLHLKSFW GLFLICGVAC
LLALFLYFVQ IIRQLYKKPT DDAIARDQQQ NHDSSSMRST RLQRFLSLMD EKEESKHESK
KRKIDGSMND TSGSTRSRGF DRERSFNSVN PLD
