LYK3_MEDTR
ID LYK3_MEDTR Reviewed; 620 AA.
AC Q6UD73; A0A072UFY4; A6H2J7; A6H2J8; A6H2K7;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=LysM domain receptor-like kinase 3 {ECO:0000303|PubMed:12947035};
DE Short=LysM-containing receptor-like kinase 3 {ECO:0000305};
DE Short=MtLYK3 {ECO:0000303|PubMed:17586690};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:20971894};
DE AltName: Full=LysM receptor kinase K1B {ECO:0000305};
DE AltName: Full=Protein HAIR CURLING {ECO:0000303|PubMed:11290290};
DE Flags: Precursor;
GN Name=LYK3 {ECO:0000303|PubMed:12947035};
GN Synonyms=HCL {ECO:0000303|PubMed:11290290}, RLK3 {ECO:0000305};
GN OrderedLocusNames=MTR_5g086130 {ECO:0000312|EMBL:AES99916.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000312|EMBL:AAQ73159.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Jemalong A17;
RX PubMed=12947035; DOI=10.1126/science.1090074;
RA Limpens E., Franken C., Smit P., Willemse J., Bisseling T., Geurts R.;
RT "LysM domain receptor kinases regulating rhizobial Nod factor-induced
RT infection.";
RL Science 302:630-633(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 121-276
RP (ISOFORM 1/2), FUNCTION, MUTAGENESIS OF PRO-87 AND GLY-334, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Root;
RX PubMed=17586690; DOI=10.1104/pp.107.100495;
RA Smit P., Limpens E., Geurts R., Fedorova E., Dolgikh E., Gough C.,
RA Bisseling T.;
RT "Medicago LYK3, an entry receptor in rhizobial nodulation factor
RT signaling.";
RL Plant Physiol. 145:183-191(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [5]
RP FUNCTION, MUTAGENESIS OF PRO-87 AND GLY-334, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Jemalong A17;
RX PubMed=11290290; DOI=10.1242/dev.128.9.1507;
RA Catoira R., Timmers A.C., Maillet F., Galera C., Penmetsa R.V., Cook D.,
RA Denarie J., Gough C.;
RT "The HCL gene of Medicago truncatula controls Rhizobium-induced root hair
RT curling.";
RL Development 128:1507-1518(2001).
RN [6]
RP AUTOPHOSPHORYLATION, AND GENE FAMILY.
RC STRAIN=cv. Jemalong A17;
RX PubMed=16844829; DOI=10.1104/pp.106.084657;
RA Arrighi J.-F., Barre A., Ben Amor B., Bersoult A., Soriano L.C.,
RA Mirabella R., de Carvalho-Niebel F., Journet E.-P., Gherardi M., Huguet T.,
RA Geurts R., Denarie J., Rouge P., Gough C.;
RT "The Medicago truncatula lysin [corrected] motif-receptor-like kinase gene
RT family includes NFP and new nodule-expressed genes.";
RL Plant Physiol. 142:265-279(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PUB1, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Jemalong A17;
RX PubMed=20971894; DOI=10.1105/tpc.110.075861;
RA Mbengue M., Camut S., de Carvalho-Niebel F., Deslandes L., Froidure S.,
RA Klaus-Heisen D., Moreau S., Rivas S., Timmers T., Herve C., Cullimore J.,
RA Lefebvre B.;
RT "The Medicago truncatula E3 ubiquitin ligase PUB1 interacts with the LYK3
RT symbiotic receptor and negatively regulates infection and nodulation.";
RL Plant Cell 22:3474-3488(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=23432463; DOI=10.1111/nph.12198;
RA Rey T., Nars A., Bonhomme M., Bottin A., Huguet S., Balzergue S.,
RA Jardinaud M.-F., Bono J.-J., Cullimore J., Dumas B., Gough C., Jacquet C.;
RT "NFP, a LysM protein controlling Nod factor perception, also intervenes in
RT Medicago truncatula resistance to pathogens.";
RL New Phytol. 198:875-886(2013).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jemalong A17;
RX PubMed=25351493; DOI=10.1105/tpc.114.129502;
RA Moling S., Pietraszewska-Bogiel A., Postma M., Fedorova E., Hink M.A.,
RA Limpens E., Gadella T.W.J., Bisseling T.;
RT "Nod factor receptors form heteromeric complexes and are essential for
RT intracellular infection in medicago nodules.";
RL Plant Cell 26:4188-4199(2014).
CC -!- FUNCTION: Putative receptor for S.meliloti Nod factor signals essential
CC for the establishment of the nitrogen-fixing, root nodule symbiosis
CC with S.meliloti (PubMed:20971894, PubMed:12947035, PubMed:17586690,
CC PubMed:25351493). Involved in the control of root hair curling after
CC S.meliloti infection, probably by modulating the reorganization of the
CC microtubular cytoskeleton in epidermal and cortical cells
CC (PubMed:17586690, PubMed:11290290). Regulates a subset of Nod factor-
CC induced genes (PubMed:17586690). {ECO:0000269|PubMed:11290290,
CC ECO:0000269|PubMed:12947035, ECO:0000269|PubMed:17586690,
CC ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:25351493}.
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 Evidence={ECO:0000269|PubMed:20971894};
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; Evidence={ECO:0000269|PubMed:20971894};
CC -!- SUBUNIT: Forms homodimers and homooligomers (By similarity). Forms
CC heteromeric complexes with NFP at the cell periphery in nodules
CC (PubMed:25351493). Interacts with PUB1 (PubMed:20971894).
CC {ECO:0000250|UniProtKB:A8R7E6, ECO:0000269|PubMed:20971894,
CC ECO:0000269|PubMed:25351493}.
CC -!- INTERACTION:
CC Q6UD73; G7KAT5: 11409451; NbExp=6; IntAct=EBI-12551665, EBI-12551650;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20971894,
CC ECO:0000269|PubMed:25351493}; Single-pass membrane protein
CC {ECO:0000255}. Vacuole lumen {ECO:0000269|PubMed:25351493}.
CC Note=Removed from the plasma membrane upon the release of rhizobia into
CC the host cytoplasm. Vacuolar localization is observed in cells
CC undergoing breakdown of the receptors. {ECO:0000269|PubMed:25351493}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6UD73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UD73-2; Sequence=VSP_058382;
CC -!- TISSUE SPECIFICITY: Expressed in the epidermal and root hair cells of
CC the developing root hair zone during nonsymbiotic growth. Accumulates
CC in roots and nodules during symbiotic growth with rhizobia
CC (PubMed:12947035, PubMed:20971894). Localized at the cell periphery in
CC a narrow zone of about two cell layers (e.g. L1/L2 zone) at the nodule
CC apex upon infection by rhizobia, from the meristem to the infection
CC zone (at protein level) (PubMed:25351493).
CC {ECO:0000269|PubMed:12947035, ECO:0000269|PubMed:20971894,
CC ECO:0000269|PubMed:25351493}.
CC -!- DEVELOPMENTAL STAGE: Following inoculation with S.meliloti, accumulates
CC strongly in the nodule primordia. In young nodules, expressed in a
CC broad apical region and in the vasculature. In mature nodules,
CC predominantly observed in the apical part of the nodule encompassing
CC the pre-infection and infection zones (PubMed:20971894). Localized on
CC infection threads before rhizobia are released (PubMed:25351493).
CC {ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:25351493}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16844829,
CC ECO:0000269|PubMed:20971894}.
CC -!- DISRUPTION PHENOTYPE: In the lyk3-4 mutant, increased nodulation in
CC plants infected by S.meliloti, mostly resulting in tubular infection
CC threads, and, to a lower extent, in sac-like structures
CC (PubMed:20971894, PubMed:12947035). The weak hcl-4 mutant is unable to
CC form curled root hairs, a step preceding infection thread formation
CC upon infection by S.meliloti and leading to nodulation. In the hcl-2
CC mutant, S.meliloti induces extensive root hair deformation and
CC continuous curling, but is unable to induce the formation of tight root
CC hair curls and the subsequent infection threads (PubMed:17586690). In
CC the hcl-2 mutant, there is reduced S. meliloti Nod factor-mediated
CC induction of cortical cell division foci. Impaired asymmetric
CC microtubule network formation in curled root hairs, and failure of
CC activated cortical cells to become polarised and to exhibit the
CC microtubular cytoplasmic bridges characteristic of the pre-infection
CC threads induced by rhizobia (PubMed:11290290). Increased infection
CC threads in nodules due to a slower release of bacteria into the
CC cytoplasm (PubMed:25351493). Normal susceptibility to the root oomycete
CC A.euteiches and to the fungus C.trifolii (PubMed:23432463).
CC {ECO:0000269|PubMed:11290290, ECO:0000269|PubMed:12947035,
CC ECO:0000269|PubMed:17586690, ECO:0000269|PubMed:20971894,
CC ECO:0000269|PubMed:23432463, ECO:0000269|PubMed:25351493}.
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; AY372402; AAQ73155.1; -; Genomic_DNA.
DR EMBL; AY372406; AAQ73159.1; -; mRNA.
DR EMBL; AM420448; CAM06620.1; -; Genomic_DNA.
DR EMBL; AM420450; CAM06621.1; -; Genomic_DNA.
DR EMBL; AM420451; CAM06622.1; -; Genomic_DNA.
DR EMBL; AM420459; CAM06630.1; -; mRNA.
DR EMBL; CM001221; AES99916.1; -; Genomic_DNA.
DR EMBL; CM001221; KEH28326.1; -; Genomic_DNA.
DR RefSeq; XP_003616958.1; XM_003616910.2.
DR RefSeq; XP_013454295.1; XM_013598841.1.
DR PDB; 6XWE; X-ray; 1.49 A; A=24-229.
DR PDBsum; 6XWE; -.
DR AlphaFoldDB; Q6UD73; -.
DR SMR; Q6UD73; -.
DR IntAct; Q6UD73; 1.
DR MINT; Q6UD73; -.
DR STRING; 3880.AES99916; -.
DR EnsemblPlants; AES99916; AES99916; MTR_5g086130. [Q6UD73-1]
DR EnsemblPlants; KEH28326; KEH28326; MTR_5g086130. [Q6UD73-2]
DR Gramene; AES99916; AES99916; MTR_5g086130. [Q6UD73-1]
DR Gramene; KEH28326; KEH28326; MTR_5g086130. [Q6UD73-2]
DR KEGG; mtr:MTR_5g086130; -.
DR eggNOG; ENOG502QPX8; Eukaryota.
DR OMA; HLRWRDR; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR ExpressionAtlas; Q6UD73; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
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:0019199; F:transmembrane receptor protein kinase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR GO; GO:0009877; P:nodulation; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0009609; P:response to symbiotic bacterium; IMP:UniProtKB.
DR InterPro; IPR044812; CERK1/LYK3-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46204; PTHR46204; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 Disulfide bond; Glycoprotein; Kinase; Membrane; Nodulation;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..620
FT /note="LysM domain receptor-like kinase 3"
FT /evidence="ECO:0000255"
FT /id="PRO_5006746948"
FT TOPO_DOM 24..231
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 46..72
FT /note="LysM 1; degenerate"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DOMAIN 102..148
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 167..210
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 322..595
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 265..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 441
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108..114
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 136..142
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT BINDING 328..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 25..92
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 29..154
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT DISULFID 90..152
FT /evidence="ECO:0000250|UniProtKB:A8R7E6"
FT VAR_SEQ 277..278
FT /note="Missing (in isoform 2)"
FT /id="VSP_058382"
FT MUTAGEN 87
FT /note="P->S: In hcl-3; S.meliloti induces extensive root
FT hair deformation and continuous curling, but is unable to
FT induce the formation of tight root hair curls and the
FT subsequent infection threads."
FT /evidence="ECO:0000269|PubMed:11290290,
FT ECO:0000269|PubMed:17586690"
FT MUTAGEN 334
FT /note="G->E: In hcl-1; S.meliloti induces extensive root
FT hair deformation and continuous curling, but is unable to
FT induce the formation of tight root hair curls and the
FT subsequent infection threads."
FT /evidence="ECO:0000269|PubMed:11290290,
FT ECO:0000269|PubMed:17586690"
FT CONFLICT 87
FT /note="P -> S (in Ref. 2; CAM06621)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="G -> E (in Ref. 2; CAM06620)"
FT /evidence="ECO:0000305"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:6XWE"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:6XWE"
FT TURN 118..122
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6XWE"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6XWE"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6XWE"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:6XWE"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6XWE"
SQ SEQUENCE 620 AA; 68580 MW; 884D5593B8FEB66E CRC64;
MNLKNGLLLF ILFLDCVFFK VESKCVKGCD VALASYYIIP SIQLRNISNF MQSKIVLTNS
FDVIMSYNRD VVFDKSGLIS YTRINVPFPC ECIGGEFLGH VFEYTTKEGD DYDLIANTYY
ASLTTVELLK KFNSYDPNHI PVKAKINVTV ICSCGNSQIS KDYGLFVTYP LRSDDTLAKI
ATKAGLDEGL IQNFNQDANF SIGSGIVFIP GRDQNGHFFP LYSRTGIAKG SAVGIAMAGI
FGLLLFVIYI YAKYFQKKEE EKTKLPQTSR AFSTQDASGS AEYETSGSSG HATGSAAGLT
GIMVAKSTEF TYQELAKATN NFSLDNKIGQ GGFGAVYYAE LRGEKTAIKK MDVQASSEFL
CELKVLTHVH HLNLVRLIGY CVEGSLFLVY EHIDNGNLGQ YLHGIGTEPL PWSSRVQIAL
DSARGLEYIH EHTVPVYIHR DVKSANILID KNLRGKVADF GLTKLIEVGN STLHTRLVGT
FGYMPPEYAQ YGDVSPKIDV YAFGVVLYEL ITAKNAVLKT GESVAESKGL VQLFEEALHR
MDPLEGLRKL VDPRLKENYP IDSVLKMAQL GRACTRDNPL LRPSMRSIVV ALMTLSSPTE
DCDDDSSYEN QSLINLLSTR
