GLR32_ARATH
ID GLR32_ARATH Reviewed; 912 AA.
AC Q93YT1; O65498; Q9C561;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glutamate receptor 3.2 {ECO:0000303|PubMed:11379626};
DE Short=AtGLR3.2 {ECO:0000303|PubMed:11379626};
DE AltName: Full=AtGluR2 {ECO:0000303|PubMed:11158446};
DE AltName: Full=Glutamate receptor-like protein 3.2 {ECO:0000303|PubMed:12082126};
DE AltName: Full=Ligand-gated ion channel 3.2 {ECO:0000305};
DE Flags: Precursor;
GN Name=GLR3.2 {ECO:0000303|PubMed:11379626};
GN Synonyms=GLUR2 {ECO:0000303|PubMed:11158446};
GN OrderedLocusNames=At4g35290 {ECO:0000312|Araport:AT4G35290};
GN ORFNames=F23E12.150 {ECO:0000312|EMBL:CAA18740.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11158446; DOI=10.1093/pcp/pce008;
RA Kim S.A., Kwak J.M., Jae S.-K., Wang M.-H., Nam H.G.;
RT "Overexpression of the AtGluR2 gene encoding an Arabidopsis homolog of
RT mammalian glutamate receptors impairs calcium utilization and sensitivity
RT to ionic stress in transgenic plants.";
RL Plant Cell Physiol. 42:74-84(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX DOI=10.1016/S0168-9452(02)00057-2;
RA Turano F.J., Muhitch M.J., Felker F.C., McMahon M.B.;
RT "The putative glutamate receptor 3.2 from Arabidopsis thaliana (AtGLR3.2)
RT is an integral membrane peptide that accumulates in rapidly growing tissues
RT and persists in vascular-associated tissues.";
RL Plant Sci. 163:43-51(2002).
RN [8]
RP FUNCTION, INTERACTION WITH GLR3.4, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 419-572 AND 682-811 IN COMPLEX
RP WITH L-METHIONINE AND GLYCINE, AND MUTAGENESIS OF ARG-551.
RX PubMed=33027636; DOI=10.1016/j.str.2020.09.006;
RA Gangwar S.P., Green M.N., Michard E., Simon A.A., Feijo J.A.,
RA Sobolevsky A.I.;
RT "Structure of the Arabidopsis glutamate receptor-like channel GLR3.2
RT ligand-binding domain.";
RL Structure 0:0-0(2020).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel (Probable). May be involved in light-signal transduction
CC and calcium homeostasis via the regulation of calcium influx into cells
CC (Probable). Could play a role in calcium unloading from the xylem
CC vessels (PubMed:11158446). Acts as negative regulator of lateral root
CC initiation and development (PubMed:23590882). May restrict primordia
CC numbers and position along the root axis by a signaling process
CC originating in the phloem (PubMed:23590882).
CC {ECO:0000269|PubMed:11158446, ECO:0000269|PubMed:23590882,
CC ECO:0000305}.
CC -!- SUBUNIT: Forms a heteromeric channel with GLR3.4.
CC {ECO:0000269|PubMed:23590882}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23590882,
CC ECO:0000269|Ref.7}; Multi-pass membrane protein {ECO:0000269|Ref.7}.
CC Note=Localizes to the plasma membrane. {ECO:0000269|PubMed:23590882,
CC ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and siliques, and at lower
CC level in flowers and roots (PubMed:12082126). Detected in the vascular
CC tissues of both shoots and roots (PubMed:11158446, Ref.7). Expressed in
CC root phloem (PubMed:23590882). {ECO:0000269|PubMed:11158446,
CC ECO:0000269|PubMed:12082126, ECO:0000269|PubMed:23590882,
CC ECO:0000269|Ref.7}.
CC -!- DISRUPTION PHENOTYPE: Overproduction and aberrant placement of lateral
CC root primordia. {ECO:0000269|PubMed:23590882}.
CC -!- MISCELLANEOUS: Overexpression of the gene leads to calcium deficiency
CC and hypersensitivity to potassium and sodium.
CC {ECO:0000269|PubMed:11158446}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF159498; AAK13248.1; -; mRNA.
DR EMBL; AF159499; AAK13249.1; -; Genomic_DNA.
DR EMBL; AL022604; CAA18740.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86490.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86491.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67778.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67779.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67781.1; -; Genomic_DNA.
DR EMBL; AY059778; AAL24126.1; -; mRNA.
DR PIR; T06128; T06128.
DR RefSeq; NP_001320141.1; NM_001342335.1.
DR RefSeq; NP_001329586.1; NM_001342336.1.
DR RefSeq; NP_001329588.1; NM_001342337.1.
DR RefSeq; NP_567981.1; NM_119695.4.
DR RefSeq; NP_974686.1; NM_202957.3.
DR PDB; 6VE8; X-ray; 1.75 A; A=419-572, A=682-811.
DR PDB; 6VEA; X-ray; 1.58 A; A=419-572, A=682-811.
DR PDBsum; 6VE8; -.
DR PDBsum; 6VEA; -.
DR AlphaFoldDB; Q93YT1; -.
DR SMR; Q93YT1; -.
DR BioGRID; 14964; 15.
DR IntAct; Q93YT1; 4.
DR STRING; 3702.AT4G35290.2; -.
DR PaxDb; Q93YT1; -.
DR PRIDE; Q93YT1; -.
DR EnsemblPlants; AT4G35290.1; AT4G35290.1; AT4G35290.
DR EnsemblPlants; AT4G35290.2; AT4G35290.2; AT4G35290.
DR EnsemblPlants; AT4G35290.3; AT4G35290.3; AT4G35290.
DR EnsemblPlants; AT4G35290.4; AT4G35290.4; AT4G35290.
DR EnsemblPlants; AT4G35290.5; AT4G35290.5; AT4G35290.
DR GeneID; 829682; -.
DR Gramene; AT4G35290.1; AT4G35290.1; AT4G35290.
DR Gramene; AT4G35290.2; AT4G35290.2; AT4G35290.
DR Gramene; AT4G35290.3; AT4G35290.3; AT4G35290.
DR Gramene; AT4G35290.4; AT4G35290.4; AT4G35290.
DR Gramene; AT4G35290.5; AT4G35290.5; AT4G35290.
DR KEGG; ath:AT4G35290; -.
DR Araport; AT4G35290; -.
DR TAIR; locus:2122128; AT4G35290.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q93YT1; -.
DR OMA; KPEGFMI; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q93YT1; -.
DR PRO; PR:Q93YT1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93YT1; baseline and differential.
DR Genevisible; Q93YT1; 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; ISS:UniProtKB.
DR GO; GO:0008066; F:glutamate receptor activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS: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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..912
FT /note="Glutamate receptor 3.2"
FT /id="PRO_0000011606"
FT TOPO_DOM 23..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 850..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 888..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544..546
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VEA"
FT BINDING 544..546
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VE8"
FT BINDING 551
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VEA"
FT BINDING 551
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VE8"
FT BINDING 703
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VEA"
FT BINDING 703
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VE8"
FT BINDING 743..746
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VEA"
FT BINDING 743..746
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VE8"
FT CARBOHYD 306
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 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 755..809
FT /evidence="ECO:0000269|PubMed:33027636,
FT ECO:0007744|PDB:6VE8, ECO:0007744|PDB:6VEA"
FT MUTAGEN 551
FT /note="R->A: Behaves as a constitutively open channel."
FT /evidence="ECO:0000269|PubMed:33027636"
FT CONFLICT 523
FT /note="N -> S (in Ref. 4; AAL24126)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="P -> S (in Ref. 1; AAK13248/AAK13249)"
FT /evidence="ECO:0000305"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 494..504
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 566..571
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 686..690
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 704..709
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 716..718
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 725..733
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 738..743
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 744..753
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 756..762
FT /evidence="ECO:0007829|PDB:6VEA"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 778..792
FT /evidence="ECO:0007829|PDB:6VEA"
FT HELIX 795..804
FT /evidence="ECO:0007829|PDB:6VEA"
SQ SEQUENCE 912 AA; 101663 MW; 0736D75C864E97C7 CRC64;
MFWVLVLLSF IVLIGDGMIS EGAGLRPRYV DVGAIFSLGT LQGEVTNIAM KAAEEDVNSD
PSFLGGSKLR ITTYDAKRNG FLTIMGALQF METDAVAIIG PQTSIMAHVL SHLANELSVP
MLSFTALDPS LSALQFPFFV QTAPSDLFLM RAIAEMISYY GWSEVIALYN DDDNSRNGIT
ALGDELEGRR CKISYKAVLP LDVVITSPRE IINELVKIQG MESRVIIVNT FPKTGKKIFE
EAQKLGMMEK GYVWIATTWL TSLLDSVNPL PAKTAESLRG VLTLRIHTPN SKKKKDFVAR
WNKLSNGTVG LNVYGLYAYD TVWIIARAVK RLLDSRANIS FSSDPKLTSM KGGGSLNLGA
LSIFDQGSQF LDYIVNTNMT GVTGQIQFLP DRSMIQPSYD IINVVDDGFR QIGYWSNHSG
LSIIPPESLY KKLSNRSSSN QHLNNVTWPG GTSETPRGWV FPNNGRRLRI GVPDRASFKE
FVSRLDGSNK VQGYAIDVFE AAVKLISYPV PHEFVLFGDG LKNPNFNEFV NNVTIGVFDA
VVGDIAIVTK RTRIVDFTQP YIESGLVVVA PVTKLNDTPW AFLRPFTPPM WAVTAAFFLI
VGSVIWILEH RINDEFRGPP RKQIVTILWF SFSTMFFSHR ENTVSTLGRA VLLIWLFVVL
IITSSYTASL TSILTVQQLN SPIRGVDTLI SSSGRVGFQV GSYAENYMID ELNIARSRLV
PLGSPKEYAA ALQNGTVAAI VDERPYVDLF LSEFCGFAIR GQEFTRSGWG FAFPRDSPLA
IDMSTAILGL SETGQLQKIH DKWLSRSNCS NLNGSVSDED SEQLKLRSFW GLFLVCGISC
FIALFIYFFK IVRDFFRHGK YDEEATVPSP ESSRSKSLQT FLAYFDEKED ESKRRMKRKR
NDDLSLKPSR PI
