BRL1_ARATH
ID BRL1_ARATH Reviewed; 1166 AA.
AC Q9ZWC8; C0LGH1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase BRI1-like 1;
DE EC=2.7.11.1;
DE AltName: Full=BRASSINOSTEROID INSENSITIVE 1-like protein 1;
DE Flags: Precursor;
GN Name=BRL1; OrderedLocusNames=At1g55610; ORFNames=F20N2.4;
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].
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, STEROID-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=15486337; DOI=10.1242/dev.01403;
RA Cano-Delgado A., Yin Y., Yu C., Vafeados D., Mora-Garcia S., Cheng J.-C.,
RA Nam K.H., Li J., Chory J.;
RT "BRL1 and BRL3 are novel brassinosteroid receptors that function in
RT vascular differentiation in Arabidopsis.";
RL Development 131:5341-5351(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15469497; DOI=10.1111/j.1365-313x.2004.02214.x;
RA Zhou A., Wang H., Walker J.C., Li J.;
RT "BRL1, a leucine-rich repeat receptor-like protein kinase, is functionally
RT redundant with BRI1 in regulating Arabidopsis brassinosteroid signaling.";
RL Plant J. 40:399-409(2004).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity.
CC Regulates, in response to brassinosteroid binding, a signaling cascade
CC involved in plant development. Binds brassinolide. May be involved in
CC cell growth and vascular differentiation. {ECO:0000269|PubMed:15469497,
CC ECO:0000269|PubMed:15486337}.
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 -!- INTERACTION:
CC Q9ZWC8; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-590903, EBI-16902452;
CC Q9ZWC8; Q9LVM0: At5g58300; NbExp=2; IntAct=EBI-590903, EBI-4475781;
CC Q9ZWC8; Q94F62: BAK1; NbExp=7; IntAct=EBI-590903, EBI-617138;
CC Q9ZWC8; Q9FMZ0: BKI1; NbExp=4; IntAct=EBI-590903, EBI-1111615;
CC Q9ZWC8; Q9FGL5: CEPR1; NbExp=2; IntAct=EBI-590903, EBI-20656524;
CC Q9ZWC8; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-590903, EBI-16895926;
CC Q9ZWC8; Q9C8I6: IOS1; NbExp=2; IntAct=EBI-590903, EBI-16924837;
CC Q9ZWC8; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-590903, EBI-20651739;
CC Q9ZWC8; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-590903, EBI-16146189;
CC Q9ZWC8; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-590903, EBI-16887868;
CC Q9ZWC8; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-590903, EBI-16954301;
CC Q9ZWC8; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-590903, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15486337};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15486337}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in vascular tissues. From 7
CC day old seedlings, it is expressed in the columella cells of the root
CC tip, in the vascular initials in the meristematic region of the root
CC and in vascular tissues. After germination, it is expressed in the
CC stele cell and in the early differentiation zone of the root, where the
CC expression continues from the root to the hypocotyls and cotyledons
CC following the midvein. In mature plants, it is expressed in the
CC vasculature of the leaf, predominantly in the midvein, and in the
CC vascular bundles of inflorescence stems. Localizes to procambial cells
CC of the vascular bundles located between the differentiating xylem and
CC the phloem. {ECO:0000269|PubMed:15469497, ECO:0000269|PubMed:15486337}.
CC -!- DOMAIN: Contains two pairs of conservatively spaced Cys (Cys pair 1 and
CC 2) possibly involved in forming some heterodimers. {ECO:0000250}.
CC -!- DOMAIN: A 70 amino acid island between the 19th and the 20th LRR is
CC essential for the binding of brassinosteroids. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FJ708660; ACN59256.1; -; mRNA.
DR EMBL; AC002328; AAF79510.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33271.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33272.1; -; Genomic_DNA.
DR PIR; F96598; F96598.
DR RefSeq; NP_001117501.1; NM_001124029.2.
DR RefSeq; NP_175957.1; NM_104437.3.
DR PDB; 4J0M; X-ray; 2.50 A; A/B=25-758.
DR PDBsum; 4J0M; -.
DR AlphaFoldDB; Q9ZWC8; -.
DR SMR; Q9ZWC8; -.
DR BioGRID; 27235; 17.
DR IntAct; Q9ZWC8; 28.
DR STRING; 3702.AT1G55610.2; -.
DR iPTMnet; Q9ZWC8; -.
DR PaxDb; Q9ZWC8; -.
DR PRIDE; Q9ZWC8; -.
DR ProteomicsDB; 240631; -.
DR EnsemblPlants; AT1G55610.1; AT1G55610.1; AT1G55610.
DR EnsemblPlants; AT1G55610.2; AT1G55610.2; AT1G55610.
DR GeneID; 842010; -.
DR Gramene; AT1G55610.1; AT1G55610.1; AT1G55610.
DR Gramene; AT1G55610.2; AT1G55610.2; AT1G55610.
DR KEGG; ath:AT1G55610; -.
DR Araport; AT1G55610; -.
DR TAIR; locus:2020457; AT1G55610.
DR eggNOG; ENOG502QQ5H; Eukaryota.
DR HOGENOM; CLU_000288_22_4_1; -.
DR InParanoid; Q9ZWC8; -.
DR OMA; MWANNLS; -.
DR OrthoDB; 104425at2759; -.
DR PhylomeDB; Q9ZWC8; -.
DR PRO; PR:Q9ZWC8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWC8; baseline and differential.
DR Genevisible; Q9ZWC8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR045381; BRI1_island_dom.
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; PF20141; Island; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 16.
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; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Steroid-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1166
FT /note="Serine/threonine-protein kinase BRI1-like 1"
FT /id="PRO_0000024308"
FT TOPO_DOM 22..776
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..1166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 78..99
FT /note="LRR 1"
FT REPEAT 103..124
FT /note="LRR 2"
FT REPEAT 126..147
FT /note="LRR 3"
FT REPEAT 152..173
FT /note="LRR 4"
FT REPEAT 176..197
FT /note="LRR 5"
FT REPEAT 202..224
FT /note="LRR 6"
FT REPEAT 227..248
FT /note="LRR 7"
FT REPEAT 252..274
FT /note="LRR 8"
FT REPEAT 278..300
FT /note="LRR 9"
FT REPEAT 303..325
FT /note="LRR 10"
FT REPEAT 327..349
FT /note="LRR 11"
FT REPEAT 352..375
FT /note="LRR 12"
FT REPEAT 376..397
FT /note="LRR 13"
FT REPEAT 403..424
FT /note="LRR 14"
FT REPEAT 427..449
FT /note="LRR 15"
FT REPEAT 451..473
FT /note="LRR 16"
FT REPEAT 476..498
FT /note="LRR 17"
FT REPEAT 500..522
FT /note="LRR 18"
FT REPEAT 524..547
FT /note="LRR 19"
FT REPEAT 548..570
FT /note="LRR 20"
FT REPEAT 664..686
FT /note="LRR 21"
FT REPEAT 688..710
FT /note="LRR 22"
FT REPEAT 712..734
FT /note="LRR 23"
FT DOMAIN 859..1147
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1142..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 66..73
FT /note="Cys pair 1"
FT MOTIF 748..755
FT /note="Cys pair 2"
FT COMPBIAS 1150..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 987
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 865..873
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 848
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 856
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 932
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1030
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:14506206"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
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 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
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 521
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 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 193..198
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 270..275
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 468..472
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 517..521
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 569..573
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 594..597
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 598..603
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 609..614
FT /evidence="ECO:0007829|PDB:4J0M"
FT TURN 616..620
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 623..630
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 642..645
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 657..661
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 681..685
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 705..709
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 733..735
FT /evidence="ECO:0007829|PDB:4J0M"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:4J0M"
FT STRAND 745..749
FT /evidence="ECO:0007829|PDB:4J0M"
SQ SEQUENCE 1166 AA; 127424 MW; 8C4DD9231A466AF7 CRC64;
MKQRWLLVLI LCFFTTSLVM GIHGKHLIND DFNETALLLA FKQNSVKSDP NNVLGNWKYE
SGRGSCSWRG VSCSDDGRIV GLDLRNSGLT GTLNLVNLTA LPNLQNLYLQ GNYFSSGGDS
SGSDCYLQVL DLSSNSISDY SMVDYVFSKC SNLVSVNISN NKLVGKLGFA PSSLQSLTTV
DLSYNILSDK IPESFISDFP ASLKYLDLTH NNLSGDFSDL SFGICGNLTF FSLSQNNLSG
DKFPITLPNC KFLETLNISR NNLAGKIPNG EYWGSFQNLK QLSLAHNRLS GEIPPELSLL
CKTLVILDLS GNTFSGELPS QFTACVWLQN LNLGNNYLSG DFLNTVVSKI TGITYLYVAY
NNISGSVPIS LTNCSNLRVL DLSSNGFTGN VPSGFCSLQS SPVLEKILIA NNYLSGTVPM
ELGKCKSLKT IDLSFNELTG PIPKEIWMLP NLSDLVMWAN NLTGTIPEGV CVKGGNLETL
ILNNNLLTGS IPESISRCTN MIWISLSSNR LTGKIPSGIG NLSKLAILQL GNNSLSGNVP
RQLGNCKSLI WLDLNSNNLT GDLPGELASQ AGLVMPGSVS GKQFAFVRNE GGTDCRGAGG
LVEFEGIRAE RLERLPMVHS CPATRIYSGM TMYTFSANGS MIYFDISYNA VSGFIPPGYG
NMGYLQVLNL GHNRITGTIP DSFGGLKAIG VLDLSHNNLQ GYLPGSLGSL SFLSDLDVSN
NNLTGPIPFG GQLTTFPVSR YANNSGLCGV PLRPCGSAPR RPITSRIHAK KQTVATAVIA
GIAFSFMCFV MLVMALYRVR KVQKKEQKRE KYIESLPTSG SCSWKLSSVP EPLSINVATF
EKPLRKLTFA HLLEATNGFS AETMVGSGGF GEVYKAQLRD GSVVAIKKLI RITGQGDREF
MAEMETIGKI KHRNLVPLLG YCKVGEERLL VYEYMKWGSL ETVLHEKSSK KGGIYLNWAA
RKKIAIGAAR GLAFLHHSCI PHIIHRDMKS SNVLLDEDFE ARVSDFGMAR LVSALDTHLS
VSTLAGTPGY VPPEYYQSFR CTAKGDVYSY GVILLELLSG KKPIDPGEFG EDNNLVGWAK
QLYREKRGAE ILDPELVTDK SGDVELFHYL KIASQCLDDR PFKRPTMIQL MAMFKEMKAD
TEEDESLDEF SLKETPLVEE SRDKEP
