ERL1_ARATH
ID ERL1_ARATH Reviewed; 966 AA.
AC C0LGW6; Q6XAT3; Q8GXT4; Q9LVB3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase ERL1 {ECO:0000303|PubMed:14985254};
DE EC=2.7.11.1;
DE AltName: Full=Protein ERECTA-like kinase 1;
DE Flags: Precursor;
GN Name=ERL1 {ECO:0000303|PubMed:14985254};
GN OrderedLocusNames=At5g62230 {ECO:0000312|Araport:AT5G62230};
GN ORFNames=MMI9.14 {ECO:0000303|PubMed:10718197};
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], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=14985254; DOI=10.1242/dev.01028;
RA Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.;
RT "Synergistic interaction of three ERECTA-family receptor-like kinases
RT controls Arabidopsis organ growth and flower development by promoting cell
RT proliferation.";
RL Development 131:1491-1501(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 638-966.
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 [6]
RP FUNCTION.
RX PubMed=16002616; DOI=10.1126/science.1109710;
RA Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.;
RT "Stomatal patterning and differentiation by synergistic interactions of
RT receptor kinases.";
RL Science 309:290-293(2005).
RN [7]
RP FUNCTION.
RX PubMed=17652352; DOI=10.1242/dev.004788;
RA Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.;
RT "Haploinsufficiency after successive loss of signaling reveals a role for
RT ERECTA-family genes in Arabidopsis ovule development.";
RL Development 134:3099-3109(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ERECTA; TMM; EPF1
RP AND EPF2, AND SUBUNIT.
RX PubMed=22241782; DOI=10.1101/gad.179895.111;
RA Lee J.S., Kuroha T., Hnilova M., Khatayevich D., Kanaoka M.M., McAbee J.M.,
RA Sarikaya M., Tamerler C., Torii K.U.;
RT "Direct interaction of ligand-receptor pairs specifying stomatal
RT patterning.";
RL Genes Dev. 26:126-136(2012).
RN [9]
RP FUNCTION.
RX PubMed=23881395; DOI=10.1093/jxb/ert196;
RA Uchida N., Tasaka M.;
RT "Regulation of plant vascular stem cells by endodermis-derived EPFL-family
RT peptide hormones and phloem-expressed ERECTA-family receptor kinases.";
RL J. Exp. Bot. 64:5335-5343(2013).
RN [10]
RP INTERACTION WITH SERK1; SERK2; SERK3/BAK1 AND SERK4.
RX PubMed=26320950; DOI=10.1016/j.cub.2015.07.068;
RA Meng X., Chen X., Mang H., Liu C., Yu X., Gao X., Torii K.U., He P.,
RA Shan L.;
RT "Differential function of Arabidopsis SERK family receptor-like kinases in
RT stomatal patterning.";
RL Curr. Biol. 25:2361-2372(2015).
RN [11]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH TMM.
RX PubMed=28536146; DOI=10.1101/gad.297580.117;
RA Lin G., Zhang L., Han Z., Yang X., Liu W., Li E., Chang J., Qi Y.,
RA Shpak E.D., Chai J.;
RT "A receptor-like protein acts as a specificity switch for the regulation of
RT stomatal development.";
RL Genes Dev. 31:927-938(2017).
CC -!- FUNCTION: Receptor kinase that regulates inflorescence architecture and
CC organ shape as well as stomatal patterning, including density and
CC clustering, together with ER and ERL2. Redundantly involved with ER in
CC procambial development regulation. Forms a functional ligand-receptor
CC pair with EPF1 (AC Q8S8I4) (PubMed:22241782). Forms a constitutive
CC complex with TMM involved in the recognition of the stomatal regulatory
CC peptides EPF1, EPF2 and EPFL9/STOMAGEN (PubMed:28536146).
CC {ECO:0000269|PubMed:14985254, ECO:0000269|PubMed:16002616,
CC ECO:0000269|PubMed:17652352, ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:23881395, ECO:0000269|PubMed:28536146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Homodimer and heterodimer with ERECTA and TMM. Interacts with
CC EPF1 and EPF2. Interacts with SERK1, SERK2, SERK3/BAK1 and SERK4 in a
CC EPF1-induced manner (PubMed:26320950). {ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:26320950, ECO:0000269|PubMed:28536146}.
CC -!- INTERACTION:
CC C0LGW6; Q8VYT3: At4g30520; NbExp=3; IntAct=EBI-16914248, EBI-16902452;
CC C0LGW6; Q94F62: BAK1; NbExp=4; IntAct=EBI-16914248, EBI-617138;
CC C0LGW6; O49545: BAM1; NbExp=2; IntAct=EBI-16914248, EBI-17069471;
CC C0LGW6; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-16914248, EBI-16895926;
CC C0LGW6; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-16914248, EBI-16924837;
CC C0LGW6; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16914248, EBI-20651739;
CC C0LGW6; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-16914248, EBI-1238953;
CC C0LGW6; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-16914248, EBI-6290483;
CC C0LGW6; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-16914248, EBI-16954301;
CC C0LGW6; Q8RWZ1: SUB; NbExp=4; IntAct=EBI-16914248, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22241782,
CC ECO:0000303|PubMed:14985254}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=C0LGW6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in developing organs, including
CC bud clusters, flowers, siliques and young rosettes. Also detected in
CC mature aboveground organs, such as leaves, stems and pedicels, but
CC barely in roots. {ECO:0000269|PubMed:14985254}.
CC -!- DEVELOPMENTAL STAGE: At the vegetative stage, strongly expressed in the
CC shoot meristem, leaf primordia and juvenile leaves. At the reproductive
CC stage, localized in the young developing flowers. Expressed in
CC inflorescence meristem and is up-regulated during flower initiation and
CC formation of flower organs. Also found in cells that differentiate into
CC pedicels. {ECO:0000269|PubMed:14985254}.
CC -!- DOMAIN: The kinase domain is not required for ligand binding.
CC {ECO:0000269|PubMed:22241782}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY244745; AAP69763.1; -; mRNA.
DR EMBL; AB019235; BAA97187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97583.1; -; Genomic_DNA.
DR EMBL; FJ708810; ACN59401.1; -; mRNA.
DR EMBL; AK118052; BAC42683.1; ALT_INIT; mRNA.
DR RefSeq; NP_201029.1; NM_125617.3. [C0LGW6-1]
DR PDB; 5XJO; X-ray; 2.63 A; A/B=28-566.
DR PDB; 5XJX; X-ray; 3.06 A; A/B/E/G/I/K=24-573.
DR PDB; 5XKJ; X-ray; 3.48 A; A/B=24-572.
DR PDBsum; 5XJO; -.
DR PDBsum; 5XJX; -.
DR PDBsum; 5XKJ; -.
DR AlphaFoldDB; C0LGW6; -.
DR SMR; C0LGW6; -.
DR BioGRID; 21588; 37.
DR IntAct; C0LGW6; 43.
DR STRING; 3702.AT5G62230.1; -.
DR PaxDb; C0LGW6; -.
DR ProteomicsDB; 220693; -. [C0LGW6-1]
DR EnsemblPlants; AT5G62230.1; AT5G62230.1; AT5G62230. [C0LGW6-1]
DR GeneID; 836344; -.
DR Gramene; AT5G62230.1; AT5G62230.1; AT5G62230. [C0LGW6-1]
DR KEGG; ath:AT5G62230; -.
DR Araport; AT5G62230; -.
DR TAIR; locus:2167948; AT5G62230.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR InParanoid; C0LGW6; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; C0LGW6; -.
DR PRO; PR:C0LGW6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGW6; baseline and differential.
DR Genevisible; C0LGW6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR GO; GO:0048481; P:plant ovule development; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..966
FT /note="LRR receptor-like serine/threonine-protein kinase
FT ERL1"
FT /id="PRO_0000387509"
FT TOPO_DOM 26..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 40..63
FT /note="LRR 1"
FT REPEAT 75..94
FT /note="LRR 2"
FT REPEAT 95..118
FT /note="LRR 3"
FT REPEAT 120..142
FT /note="LRR 4"
FT REPEAT 143..166
FT /note="LRR 5"
FT REPEAT 168..190
FT /note="LRR 6"
FT REPEAT 192..214
FT /note="LRR 7"
FT REPEAT 215..238
FT /note="LRR 8"
FT REPEAT 239..261
FT /note="LRR 9"
FT REPEAT 262..285
FT /note="LRR 10"
FT REPEAT 286..311
FT /note="LRR 11"
FT REPEAT 313..333
FT /note="LRR 12"
FT REPEAT 334..357
FT /note="LRR 13"
FT REPEAT 359..381
FT /note="LRR 14"
FT REPEAT 383..404
FT /note="LRR 15"
FT REPEAT 405..429
FT /note="LRR 16"
FT REPEAT 431..453
FT /note="LRR 17"
FT REPEAT 454..476
FT /note="LRR 18"
FT REPEAT 478..500
FT /note="LRR 19"
FT REPEAT 501..525
FT /note="LRR 20"
FT REPEAT 527..550
FT /note="LRR 21"
FT DOMAIN 648..921
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 773
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 654..662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 637
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 721
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 760
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 815
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
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 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 368
FT /note="N -> S (in Ref. 1; AAP69763)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="S -> F (in Ref. 5; BAC42683)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="D -> G (in Ref. 1; AAP69763)"
FT /evidence="ECO:0000305"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5XJX"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:5XKJ"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5XJX"
SQ SEQUENCE 966 AA; 106486 MW; A4C91ACB33A864B8 CRC64;
MKEKMQRMVL SLAMVGFMVF GVASAMNNEG KALMAIKGSF SNLVNMLLDW DDVHNSDLCS
WRGVFCDNVS YSVVSLNLSS LNLGGEISPA IGDLRNLQSI DLQGNKLAGQ IPDEIGNCAS
LVYLDLSENL LYGDIPFSIS KLKQLETLNL KNNQLTGPVP ATLTQIPNLK RLDLAGNHLT
GEISRLLYWN EVLQYLGLRG NMLTGTLSSD MCQLTGLWYF DVRGNNLTGT IPESIGNCTS
FQILDISYNQ ITGEIPYNIG FLQVATLSLQ GNRLTGRIPE VIGLMQALAV LDLSDNELVG
PIPPILGNLS FTGKLYLHGN MLTGPIPSEL GNMSRLSYLQ LNDNKLVGTI PPELGKLEQL
FELNLANNRL VGPIPSNISS CAALNQFNVH GNLLSGSIPL AFRNLGSLTY LNLSSNNFKG
KIPVELGHII NLDKLDLSGN NFSGSIPLTL GDLEHLLILN LSRNHLSGQL PAEFGNLRSI
QMIDVSFNLL SGVIPTELGQ LQNLNSLILN NNKLHGKIPD QLTNCFTLVN LNVSFNNLSG
IVPPMKNFSR FAPASFVGNP YLCGNWVGSI CGPLPKSRVF SRGALICIVL GVITLLCMIF
LAVYKSMQQK KILQGSSKQA EGLTKLVILH MDMAIHTFDD IMRVTENLNE KFIIGYGASS
TVYKCALKSS RPIAIKRLYN QYPHNLREFE TELETIGSIR HRNIVSLHGY ALSPTGNLLF
YDYMENGSLW DLLHGSLKKV KLDWETRLKI AVGAAQGLAY LHHDCTPRII HRDIKSSNIL
LDENFEAHLS DFGIAKSIPA SKTHASTYVL GTIGYIDPEY ARTSRINEKS DIYSFGIVLL
ELLTGKKAVD NEANLHQLIL SKADDNTVME AVDPEVTVTC MDLGHIRKTF QLALLCTKRN
PLERPTMLEV SRVLLSLVPS LQVAKKLPSL DHSTKKLQQE NEVRNPDAEA SQWFVQFREV
ISKSSI
