GLR34_ARATH
ID GLR34_ARATH Reviewed; 959 AA.
AC Q8GXJ4; O23048; Q8LGM9; Q9SWD9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Glutamate receptor 3.4 {ECO:0000303|PubMed:11379626};
DE Short=AtGLR3.4 {ECO:0000303|PubMed:11379626};
DE AltName: Full=Glutamate receptor-like protein 3.4 {ECO:0000303|PubMed:12082126};
DE AltName: Full=Ligand-gated ion channel 3.4 {ECO:0000305};
DE Flags: Precursor;
GN Name=GLR3.4 {ECO:0000303|PubMed:11379626};
GN Synonyms=GLR4 {ECO:0000305}, GLUR3 {ECO:0000303|PubMed:15864638};
GN OrderedLocusNames=At1g05200 {ECO:0000312|Araport:AT1G05200};
GN ORFNames=YUP8H12.19 {ECO:0000312|EMBL:AAB71458.1};
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [2]
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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-959 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, INDUCTION BY ABIOTIC STRESSES, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15864638; DOI=10.1007/s00425-005-1551-3;
RA Meyerhoff O., Mueller K., Roelfsema M.R.G., Latz A., Lacombe B.,
RA Hedrich R., Dietrich P., Becker D.;
RT "AtGLR3.4, a glutamate receptor channel-like gene is sensitive to touch and
RT cold.";
RL Planta 222:418-427(2005).
RN [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21110940; DOI=10.1016/j.bbabio.2010.11.008;
RA Teardo E., Formentin E., Segalla A., Giacometti G.M., Marin O., Zanetti M.,
RA Lo Schiavo F., Zoratti M., Szabo I.;
RT "Dual localization of plant glutamate receptor AtGLR3.4 to plastids and
RT plasmamembrane.";
RL Biochim. Biophys. Acta 1807:359-367(2011).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22447719; DOI=10.1104/pp.112.197509;
RA Vincill E.D., Bieck A.M., Spalding E.P.;
RT "Ca(2+) conduction by an amino acid-gated ion channel related to glutamate
RT receptors.";
RL Plant Physiol. 159:40-46(2012).
RN [10]
RP FUNCTION, INTERACTION WITH GLR3.2, 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 [11]
RP FUNCTION.
RX PubMed=29432559; DOI=10.1093/pcp/pcy034;
RA Cheng Y., Zhang X., Sun T., Tian Q., Zhang W.H.;
RT "Glutamate receptor homolog3.4 is involved in regulation of seed
RT germination under salt stress in Arabidopsis.";
RL Plant Cell Physiol. 59:978-988(2018).
CC -!- FUNCTION: Glutamate-gated receptor that probably acts as non-selective
CC cation channel, at least in hypocotyls (Probable). Can be triggered by
CC Asn, Ser, Gly and, to a lower extent, Ala, Cys and Glu
CC (PubMed:18162597, PubMed:22447719). May be involved in light-signal
CC transduction and calcium homeostasis via the regulation of calcium
CC influx into cells (Probable). Plays an important role in the calcium-
CC based fast transmission of environmental stress (PubMed:15864638). Acts
CC as negative regulator of lateral root initiation and development
CC (PubMed:23590882). May restrict primordia numbers and position along
CC the root axis by a signaling process originating in the phloem
CC (PubMed:23590882). AtGLR3.4-mediated cytosolic calcium influx may be
CC involved in the regulation of seed germination under salt stress by
CC modulating sodium accumulation through the SOS pathway
CC (PubMed:29432559). {ECO:0000269|PubMed:15864638,
CC ECO:0000269|PubMed:18162597, ECO:0000269|PubMed:22447719,
CC ECO:0000269|PubMed:23590882, ECO:0000269|PubMed:29432559,
CC ECO:0000305|PubMed:15864638, ECO:0000305|PubMed:21110940}.
CC -!- SUBUNIT: Forms a heteromeric channel with GLR3.2.
CC {ECO:0000269|PubMed:23590882}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15864638,
CC ECO:0000269|PubMed:21110940, ECO:0000269|PubMed:22447719,
CC ECO:0000269|PubMed:23590882}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:21110940}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the plasma membrane.
CC {ECO:0000269|PubMed:15864638, ECO:0000269|PubMed:21110940,
CC ECO:0000269|PubMed:22447719, ECO:0000269|PubMed:23590882}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=GLR3.4a;
CC IsoId=Q8GXJ4-1; Sequence=Displayed;
CC Name=2; Synonyms=GLR3.4b;
CC IsoId=Q8GXJ4-2; Sequence=VSP_009219, VSP_009220;
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC leaves and siliques (PubMed:12082126). Expressed in seedlings,
CC cotyledons, roots (e.g. root hairs, epidermis and cortex cells), stems,
CC leaves (e.g. vascular bundles and hydathodes), and siliques
CC (PubMed:15864638). Expressed in root phloem (PubMed:23590882).
CC {ECO:0000269|PubMed:12082126, ECO:0000269|PubMed:15864638,
CC ECO:0000269|PubMed:23590882}.
CC -!- INDUCTION: The induction by glutamate, gamma-amino butiric acid (GABA),
CC malate, aspartate, acetate, wounding, touch, and cold stress stimuli is
CC abscisic acid (ABA)-independent, but calcium-dependent. Cold-mediated
CC induction is rapid but transient. {ECO:0000269|PubMed:15864638}.
CC -!- DISRUPTION PHENOTYPE: Impaired glutamate-triggered (and Ala, Asn, Cys,
CC Gly, Ser-triggered) membrane depolarization and calcium rise
CC (PubMed:18162597). Slight reduction of photosynthetic yield of
CC Photosystem II (PubMed:21110940). Overproduction and aberrant placement
CC of lateral root primordia (PubMed:23590882).
CC {ECO:0000269|PubMed:18162597, ECO:0000269|PubMed:21110940,
CC ECO:0000269|PubMed:23590882}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71458.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD47833.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY072070; AAL61999.1; -; mRNA.
DR EMBL; AC000098; AAB71458.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27803.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27804.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58387.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58390.1; -; Genomic_DNA.
DR EMBL; AK118206; BAC42828.1; -; mRNA.
DR EMBL; AF167355; AAD47833.1; ALT_SEQ; mRNA.
DR PIR; D86186; D86186.
DR PIR; T51135; T51135.
DR RefSeq; NP_001030971.1; NM_001035894.1. [Q8GXJ4-1]
DR RefSeq; NP_001320828.1; NM_001331525.1. [Q8GXJ4-2]
DR RefSeq; NP_001320831.1; NM_001331526.1. [Q8GXJ4-1]
DR RefSeq; NP_172012.2; NM_100398.3. [Q8GXJ4-1]
DR PDB; 7LZ0; X-ray; 2.29 A; A/B/C=492-601, A/B/C=709-842.
DR PDB; 7LZ1; X-ray; 1.51 A; A/B/C=492-601, A/B/C=709-842.
DR PDB; 7LZ2; X-ray; 1.50 A; A/B/C=492-601, A/B/C=709-842.
DR PDB; 7LZH; EM; 3.57 A; A/B/C/D=1-959.
DR PDB; 7LZI; EM; 4.39 A; A/B/C/D=1-959.
DR PDBsum; 7LZ0; -.
DR PDBsum; 7LZ1; -.
DR PDBsum; 7LZ2; -.
DR PDBsum; 7LZH; -.
DR PDBsum; 7LZI; -.
DR AlphaFoldDB; Q8GXJ4; -.
DR SMR; Q8GXJ4; -.
DR BioGRID; 24503; 22.
DR IntAct; Q8GXJ4; 12.
DR STRING; 3702.AT1G05200.2; -.
DR TCDB; 1.A.10.1.10; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR iPTMnet; Q8GXJ4; -.
DR PaxDb; Q8GXJ4; -.
DR PRIDE; Q8GXJ4; -.
DR ProteomicsDB; 248596; -. [Q8GXJ4-1]
DR EnsemblPlants; AT1G05200.1; AT1G05200.1; AT1G05200. [Q8GXJ4-1]
DR EnsemblPlants; AT1G05200.2; AT1G05200.2; AT1G05200. [Q8GXJ4-1]
DR EnsemblPlants; AT1G05200.5; AT1G05200.5; AT1G05200. [Q8GXJ4-2]
DR EnsemblPlants; AT1G05200.6; AT1G05200.6; AT1G05200. [Q8GXJ4-1]
DR GeneID; 839268; -.
DR Gramene; AT1G05200.1; AT1G05200.1; AT1G05200. [Q8GXJ4-1]
DR Gramene; AT1G05200.2; AT1G05200.2; AT1G05200. [Q8GXJ4-1]
DR Gramene; AT1G05200.5; AT1G05200.5; AT1G05200. [Q8GXJ4-2]
DR Gramene; AT1G05200.6; AT1G05200.6; AT1G05200. [Q8GXJ4-1]
DR KEGG; ath:AT1G05200; -.
DR Araport; AT1G05200; -.
DR TAIR; locus:2207165; AT1G05200.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007358_0_1_1; -.
DR InParanoid; Q8GXJ4; -.
DR OMA; EREQVFV; -.
DR PhylomeDB; Q8GXJ4; -.
DR PRO; PR:Q8GXJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GXJ4; baseline and differential.
DR Genevisible; Q8GXJ4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:TAIR.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0071311; P:cellular response to acetate; IEP:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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; Alternative splicing; Cell membrane; Chloroplast;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Plastid; Receptor; Reference proteome; Signal; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..959
FT /note="Glutamate receptor 3.4"
FT /id="PRO_0000011608"
FT TOPO_DOM 36..613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..959
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 893..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
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 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 656..669
FT /note="FSFSTMFFSHRENT -> LVSQFLTLEPEFTF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_009219"
FT VAR_SEQ 670..959
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_009220"
FT CONFLICT 57
FT /note="R -> G (in Ref. 5; AAD47833)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> P (in Ref. 5; AAD47833)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="H -> Q (in Ref. 5; AAD47833)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> A (in Ref. 4; BAC42828)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="Y -> N (in Ref. 5; AAD47833)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="A -> P (in Ref. 5; AAD47833)"
FT /evidence="ECO:0000305"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:7LZ2"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 575..578
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 592..597
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 712..717
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 722..725
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 730..738
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 742..744
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 751..760
FT /evidence="ECO:0007829|PDB:7LZ2"
FT TURN 762..765
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 768..773
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 774..782
FT /evidence="ECO:0007829|PDB:7LZ2"
FT TURN 783..786
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:7LZ2"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 809..823
FT /evidence="ECO:0007829|PDB:7LZ2"
FT HELIX 826..834
FT /evidence="ECO:0007829|PDB:7LZ2"
SQ SEQUENCE 959 AA; 107207 MW; 0709B834A76FAFC0 CRC64;
MGFLVMIREV SMAKAIRVVL LCVSVLWVVP KECACRSNFS RNSSSSSSSS LRPLRQRPSS
VNVGALFTYD SFIGRAAKPA VKAAMDDVNA DQSVLKGIKL NIIFQDSNCS GFIGTMGALQ
LMENKVVAAI GPQSSGIAHM ISYVANELHV PLLSFGATDP TLSSLQFPYF LRTTQNDYFQ
MHAIADFLSY SGWRQVIAIF VDDECGRNGI SVLGDVLAKK RSRISYKAAI TPGADSSSIR
DLLVSVNLME SRVFVVHVNP DSGLNVFSVA KSLGMMASGY VWIATDWLPT AMDSMEHVDS
DTMDLLQGVV AFRHYTIESS VKRQFMARWK NLRPNDGFNS YAMYAYDSVW LVARALDVFF
RENNNITFSN DPNLHKTNGS TIQLSALSVF NEGEKFMKII LGMNHTGVTG PIQFDSDRNR
VNPAYEVLNL EGTAPRTVGY WSNHSGLSVV HPETLYSRPP NTSTANQRLK GIIYPGEVTK
PPRGWVFPNN GKPLRIGVPN RVSYTDYVSK DKNPPGVRGY CIDVFEAAIE LLPYPVPRTY
ILYGDGKRNP SYDNLVNEVV ADNFDVAVGD ITIVTNRTRY VDFTQPFIES GLVVVAPVKE
AKSSPWSFLK PFTIEMWAVT GGFFLFVGAM VWILEHRFNQ EFRGPPRRQL ITIFWFSFST
MFFSHRENTV SSLGRFVLII WLFVVLIINS SYTASLTSIL TIRQLTSRIE GIDSLVTSNE
PIGVQDGTFA RNYLINELNI LPSRIVPLKD EEQYLSALQR GPNAGGVAAI VDELPYIEVL
LTNSNCKFRT VGQEFTRTGW GFAFQRDSPL AVDMSTAILQ LSEEGELEKI HRKWLNYKHE
CSMQISNSED SQLSLKSFWG LFLICGITCF MALTVFFWRV FWQYQRLLPE SADEERAGEV
SEPSRSGRGS RAPSFKELIK VVDKREAEIK EILKQKSSKK LKSTQSAAGT SQSQHGEIT
