D14_ORYSJ
ID D14_ORYSJ Reviewed; 318 AA.
AC Q10QA5; A0A0N7KGS6;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Strigolactone esterase D14 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
DE AltName: Full=Protein DWARF 14 {ECO:0000303|PubMed:19542179};
DE AltName: Full=Protein DWARF 88 {ECO:0000303|PubMed:19603144};
DE AltName: Full=Protein HIGH-TILLERING DWARF 2 {ECO:0000303|PubMed:19579033};
GN Name=D14 {ECO:0000303|PubMed:19542179};
GN Synonyms=D88 {ECO:0000303|PubMed:19603144},
GN HTD2 {ECO:0000303|PubMed:19579033};
GN OrderedLocusNames=Os03g0203200 {ECO:0000312|EMBL:BAS82841.1},
GN LOC_Os03g10620 {ECO:0000312|EMBL:ABF94526.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-79.
RC STRAIN=cv. Lansheng;
RX PubMed=19603144; DOI=10.1007/s11103-009-9522-x;
RA Gao Z., Qian Q., Liu X., Yan M., Feng Q., Dong G., Liu J., Han B.;
RT "Dwarf 88, a novel putative esterase gene affecting architecture of rice
RT plant.";
RL Plant Mol. Biol. 71:265-276(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=15659436; DOI=10.1093/pcp/pci022;
RA Ishikawa S., Maekawa M., Arite T., Onishi K., Takamure I., Kyozuka J.;
RT "Suppression of tiller bud activity in tillering dwarf mutants of rice.";
RL Plant Cell Physiol. 46:79-86(2005).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=17655651; DOI=10.1111/j.1365-313x.2007.03210.x;
RA Arite T., Iwata H., Ohshima K., Maekawa M., Nakajima M., Kojima M.,
RA Sakakibara H., Kyozuka J.;
RT "DWARF10, an RMS1/MAX4/DAD1 ortholog, controls lateral bud outgrowth in
RT rice.";
RL Plant J. 51:1019-1029(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19579033; DOI=10.1007/s00425-009-0975-6;
RA Liu W., Wu C., Fu Y., Hu G., Si H., Zhu L., Luan W., He Z., Sun Z.;
RT "Identification and characterization of HTD2: a novel gene negatively
RT regulating tiller bud outgrowth in rice.";
RL Planta 230:649-658(2009).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19542179; DOI=10.1093/pcp/pcp091;
RA Arite T., Umehara M., Ishikawa S., Hanada A., Maekawa M., Yamaguchi S.,
RA Kyozuka J.;
RT "d14, a strigolactone-insensitive mutant of rice, shows an accelerated
RT outgrowth of tillers.";
RL Plant Cell Physiol. 50:1416-1424(2009).
RN [11]
RP 3D-STRUCTURE MODELING.
RX PubMed=22713366; DOI=10.1186/1756-0500-5-307;
RA Gaiji N., Cardinale F., Prandi C., Bonfante P., Ranghino G.;
RT "The computational-based structure of Dwarf14 provides evidence for its
RT role as potential strigolactone receptor in plants.";
RL BMC Res. Notes 5:307-307(2012).
RN [12]
RP INTERACTION WITH D53 AND D3, ACTIVE SITES, AND MUTAGENESIS OF SER-147;
RP GLY-153; ASP-268 AND HIS-297.
RX PubMed=24336200; DOI=10.1038/nature12870;
RA Jiang L., Liu X., Xiong G., Liu H., Chen F., Wang L., Meng X., Liu G.,
RA Yu H., Yuan Y., Yi W., Zhao L., Ma H., He Y., Wu Z., Melcher K., Qian Q.,
RA Xu H.E., Wang Y., Li J.;
RT "DWARF 53 acts as a repressor of strigolactone signalling in rice.";
RL Nature 504:401-405(2013).
RN [13]
RP INTERACTION WITH D53 AND D3.
RX PubMed=24336215; DOI=10.1038/nature12878;
RA Zhou F., Lin Q., Zhu L., Ren Y., Zhou K., Shabek N., Wu F., Mao H.,
RA Dong W., Gan L., Ma W., Gao H., Chen J., Yang C., Wang D., Tan J.,
RA Zhang X., Guo X., Wang J., Jiang L., Liu X., Chen W., Chu J., Yan C.,
RA Ueno K., Ito S., Asami T., Cheng Z., Wang J., Lei C., Zhai H., Wu C.,
RA Wang H., Zheng N., Wan J.;
RT "D14-SCF(D3)-dependent degradation of D53 regulates strigolactone
RT signalling.";
RL Nature 504:406-410(2013).
RN [14]
RP REVIEW.
RX PubMed=25179782; DOI=10.1016/j.pbi.2014.08.001;
RA Bennett T., Leyser O.;
RT "Strigolactone signalling: standing on the shoulders of DWARFs.";
RL Curr. Opin. Plant Biol. 22:7-13(2014).
RN [15]
RP FUNCTION, INTERACTION WITH D3, AND SUBCELLULAR LOCATION.
RX PubMed=24616269; DOI=10.1093/pcp/pcu045;
RA Zhao J., Wang T., Wang M., Liu Y., Yuan S., Gao Y., Yin L., Sun W.,
RA Peng L., Zhang W., Wan J., Li X.;
RT "DWARF3 participates in an SCF complex and associates with DWARF14 to
RT suppress rice shoot branching.";
RL Plant Cell Physiol. 55:1096-1109(2014).
RN [16]
RP INTERACTION WITH D53.
RX PubMed=25713176; DOI=10.1093/pcp/pcv028;
RA Umehara M., Cao M., Akiyama K., Akatsu T., Seto Y., Hanada A., Li W.,
RA Takeda-Kamiya N., Morimoto Y., Yamaguchi S.;
RT "Structural requirements of strigolactones for shoot branching inhibition
RT in rice and Arabidopsis.";
RL Plant Cell Physiol. 56:1059-1072(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 55-318 IN COMPLEX WITH INHIBITOR,
RP AND FUNCTION.
RX PubMed=23301669; DOI=10.1111/gtc.12025;
RA Kagiyama M., Hirano Y., Mori T., Kim S.Y., Kyozuka J., Seto Y.,
RA Yamaguchi S., Hakoshima T.;
RT "Structures of D14 and D14L in the strigolactone and karrikin signaling
RT pathways.";
RL Genes Cells 18:147-160(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 51-318, AND FUNCTION.
RX PubMed=23381136; DOI=10.1038/cr.2013.19;
RA Zhao L.H., Zhou X.E., Wu Z.S., Yi W., Xu Y., Li S., Xu T.H., Liu Y.,
RA Chen R.Z., Kovach A., Kang Y., Hou L., He Y., Xie C., Song W., Zhong D.,
RA Xu Y., Wang Y., Li J., Zhang C., Melcher K., Xu H.E.;
RT "Crystal structures of two phytohormone signal-transducing alpha/beta
RT hydrolases: karrikin-signaling KAI2 and strigolactone-signaling DWARF14.";
RL Cell Res. 23:436-439(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 54-318 OF APOPROTEIN AND IN
RP COMPLEX WITH SUBSTRATE ANALOG, INTERACTION WITH SLR1, SUBCELLULAR LOCATION,
RP FUNCTION, AND MUTAGENESIS OF PHE-186; TRP-205; PHE-245 AND HIS-297.
RX PubMed=24131983; DOI=10.1038/ncomms3613;
RA Nakamura H., Xue Y.L., Miyakawa T., Hou F., Qin H.M., Fukui K., Shi X.,
RA Ito E., Ito S., Park S.H., Miyauchi Y., Asano A., Totsuka N., Ueda T.,
RA Tanokura M., Asami T.;
RT "Molecular mechanism of strigolactone perception by DWARF14.";
RL Nat. Commun. 4:2613-2613(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 52-318 IN COMPLEX WITH
RP STRIGOLACTONE.
RX PubMed=26470846; DOI=10.1038/cr.2015.122;
RA Zhao L.H., Zhou X.E., Yi W., Wu Z., Liu Y., Kang Y., Hou L., de Waal P.W.,
RA Li S., Jiang Y., Scaffidi A., Flematti G.R., Smith S.M., Lam V.Q.,
RA Griffin P.R., Wang Y., Li J., Melcher K., Xu H.E.;
RT "Destabilization of strigolactone receptor DWARF14 by binding of ligand and
RT E3-ligase signaling effector DWARF3.";
RL Cell Res. 25:1219-1236(2015).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 54-318.
RX PubMed=30464344; DOI=10.1038/s41586-018-0743-5;
RA Shabek N., Ticchiarelli F., Mao H., Hinds T.R., Leyser O., Zheng N.;
RT "Structural plasticity of D3-D14 ubiquitin ligase in strigolactone
RT signalling.";
RL Nature 563:652-656(2018).
CC -!- FUNCTION: Involved in strigolactone (SL) signaling pathway. May
CC function downstream of SL synthesis, as a component of hormone
CC signaling or as an enzyme that participates in the conversion of SL to
CC the bioactive form. Strigolactones are hormones that inhibit tillering
CC and shoot branching through the MAX-dependent pathway, contribute to
CC the regulation of shoot architectural response to phosphate-limiting
CC conditions and function as rhizosphere signal that stimulates hyphal
CC branching of arbuscular mycorrhizal fungi and trigger seed germination
CC of root parasitic weeds (PubMed:19579033, PubMed:19542179,
CC PubMed:23301669). Strigolactone-dependent association of D14 with D3
CC and D53 (a repressor of SL signaling) triggers D53 ubiquitination and
CC degradation (PubMed:24336200, PubMed:24616269). Hydrolyzes the
CC butenolide ring of SLs (PubMed:23381136, PubMed:24131983). A reaction
CC product D-OH is trapped in the cavity of D14, inducing the interaction
CC with SLR1, and probably with other proteins such as D3 and D53
CC (PubMed:24131983). Contributes to the negative regulation of
CC gibberellin signaling (PubMed:24131983). {ECO:0000269|PubMed:19542179,
CC ECO:0000269|PubMed:19579033, ECO:0000269|PubMed:23301669,
CC ECO:0000269|PubMed:23381136, ECO:0000269|PubMed:24131983,
CC ECO:0000269|PubMed:24336200, ECO:0000269|PubMed:24616269}.
CC -!- SUBUNIT: Interacts with D53 (PubMed:24336200, PubMed:24336215,
CC PubMed:25713176). The interaction between D53 and D14 is enhanced in
CC the presence of strigolactones (PubMed:24336200, PubMed:24336215). The
CC interaction with D53 occurs in the presence of (2'R) stereoisomers of
CC strigolactones, but not (2'S) stereoisomers (PubMed:25713176).
CC Interacts with SLR1 in a strigolactone-dependent manner
CC (PubMed:24131983). Interacts with D3 in a strigolactone-dependent
CC manner (PubMed:24336200, PubMed:24336215, PubMed:24616269).
CC {ECO:0000269|PubMed:24131983, ECO:0000269|PubMed:24336200,
CC ECO:0000269|PubMed:24336215, ECO:0000269|PubMed:24616269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24131983}. Nucleus
CC {ECO:0000269|PubMed:24131983, ECO:0000269|PubMed:24616269}. Note=The
CC interaction between D14 and SLR1 takes place in the nucleus
CC (PubMed:24131983). The interaction between D14 and D3 takes place in
CC the nucleus (PubMed:24616269). {ECO:0000269|PubMed:24131983,
CC ECO:0000269|PubMed:24616269}.
CC -!- TISSUE SPECIFICITY: Expressed in the parenchyma cells of the root stele
CC and lateral roots, vascular tissues of vein and leaf sheath, ligule
CC base, auricle base and stem base. {ECO:0000269|PubMed:19542179,
CC ECO:0000269|PubMed:19603144}.
CC -!- DISRUPTION PHENOTYPE: Increased number of tillers, reduced plant
CC height, and elevated levels of strigolactones.
CC {ECO:0000269|PubMed:15659436, ECO:0000269|PubMed:17655651,
CC ECO:0000269|PubMed:19542179, ECO:0000269|PubMed:19579033}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; GQ406388; ACV30015.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF94525.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF94526.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11220.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82841.1; -; Genomic_DNA.
DR EMBL; AK070827; BAG92161.1; -; mRNA.
DR RefSeq; XP_015631400.1; XM_015775914.1.
DR PDB; 3VXK; X-ray; 1.75 A; A/B=54-318.
DR PDB; 3W04; X-ray; 1.45 A; A/B=55-318.
DR PDB; 3W05; X-ray; 1.58 A; A/B=55-318.
DR PDB; 3WIO; X-ray; 2.10 A; A/B=54-318.
DR PDB; 4IH9; X-ray; 1.55 A; A/B=51-318.
DR PDB; 4IHA; X-ray; 1.55 A; A/B=51-318.
DR PDB; 5DJ5; X-ray; 2.40 A; A/B=52-318.
DR PDB; 5YZ7; X-ray; 1.90 A; A/B=54-318.
DR PDB; 5ZHR; X-ray; 1.45 A; A/B=54-318.
DR PDB; 5ZHS; X-ray; 1.49 A; A=54-318.
DR PDB; 5ZHT; X-ray; 1.53 A; A=54-318.
DR PDB; 6AP8; X-ray; 1.27 A; A/B=52-318.
DR PDB; 6BRT; X-ray; 2.39 A; A/B/C/D/E/F/G/H=56-318.
DR PDB; 6ELX; X-ray; 1.35 A; A/B=52-318.
DR PDBsum; 3VXK; -.
DR PDBsum; 3W04; -.
DR PDBsum; 3W05; -.
DR PDBsum; 3WIO; -.
DR PDBsum; 4IH9; -.
DR PDBsum; 4IHA; -.
DR PDBsum; 5DJ5; -.
DR PDBsum; 5YZ7; -.
DR PDBsum; 5ZHR; -.
DR PDBsum; 5ZHS; -.
DR PDBsum; 5ZHT; -.
DR PDBsum; 6AP8; -.
DR PDBsum; 6BRT; -.
DR PDBsum; 6ELX; -.
DR AlphaFoldDB; Q10QA5; -.
DR SMR; Q10QA5; -.
DR STRING; 4530.OS03T0203200-01; -.
DR ESTHER; orysj-Q10QA5; RsbQ-like.
DR MEROPS; S33.A18; -.
DR PaxDb; Q10QA5; -.
DR PRIDE; Q10QA5; -.
DR EnsemblPlants; Os03t0203200-01; Os03t0203200-01; Os03g0203200.
DR GeneID; 4331983; -.
DR Gramene; Os03t0203200-01; Os03t0203200-01; Os03g0203200.
DR KEGG; osa:4331983; -.
DR eggNOG; ENOG502QVRR; Eukaryota.
DR HOGENOM; CLU_020336_30_0_1; -.
DR InParanoid; Q10QA5; -.
DR OMA; DQSVWQR; -.
DR OrthoDB; 1061420at2759; -.
DR PlantReactome; R-OSA-5654828; Strigolactone signaling.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10QA5; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010223; P:secondary shoot formation; IMP:UniProtKB.
DR GO; GO:1901601; P:strigolactone biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR031143; D14_fam.
DR PANTHER; PTHR43039:SF4; PTHR43039:SF4; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..318
FT /note="Strigolactone esterase D14"
FT /id="PRO_0000422054"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24336200"
FT ACT_SITE 268
FT /evidence="ECO:0000269|PubMed:24336200"
FT ACT_SITE 297
FT /evidence="ECO:0000269|PubMed:24336200"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470846"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470846"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26470846"
FT MUTAGEN 79
FT /note="G->R: In d88; dwarf and high tillering phenotypes."
FT /evidence="ECO:0000269|PubMed:19603144"
FT MUTAGEN 147
FT /note="S->A: Weakens interaction with D53 and attenuates
FT strigolactone-induced degradation of D53."
FT /evidence="ECO:0000269|PubMed:24336200"
FT MUTAGEN 153
FT /note="G->D: In d14; dwarf and high tillering phenotypes."
FT /evidence="ECO:0000269|PubMed:24336200"
FT MUTAGEN 186
FT /note="F->A: Loss of strigolactone-dependent interaction
FT with SLR1."
FT /evidence="ECO:0000269|PubMed:24131983"
FT MUTAGEN 205
FT /note="W->A: Decreased enzymatic activity toward
FT strigolactone and loss of strigolactone-dependent
FT interaction with SLR1."
FT /evidence="ECO:0000269|PubMed:24131983"
FT MUTAGEN 245
FT /note="F->A: Loss of strigolactone-dependent interaction
FT with SLR1."
FT /evidence="ECO:0000269|PubMed:24131983"
FT MUTAGEN 268
FT /note="D->N: Weakens interaction with D53 and attenuates
FT strigolactone-induced degradation of D53."
FT /evidence="ECO:0000269|PubMed:24336200"
FT MUTAGEN 297
FT /note="H->A: No effect on strigolactone binding, but
FT decreased enzymatic activity toward strigolactone and loss
FT of interaction with SLR1."
FT /evidence="ECO:0000269|PubMed:24131983"
FT MUTAGEN 297
FT /note="H->Y: Weakens interaction with D53 and attenuates
FT strigolactone-induced degradation of D53."
FT /evidence="ECO:0000269|PubMed:24336200"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:6AP8"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6AP8"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:6AP8"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:6AP8"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:6AP8"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:6AP8"
SQ SEQUENCE 318 AA; 33508 MW; 996A6044670563EF CRC64;
MLRSTHPPPS SPSSSSSGGG GGGGSSASSS SEKTMVGGGG GGGGGSGSAA PSGAKLLQIL
NVRVVGSGER VVVLSHGFGT DQSAWSRVLP YLTRDHRVVL YDLVCAGSVN PDHFDFRRYD
NLDAYVDDLL AILDALRIPR CAFVGHSVSA MIGILASIRR PDLFAKLVLI GASPRFLNDS
DYHGGFELEE IQQVFDAMGA NYSAWATGYA PLAVGADVPA AVQEFSRTLF NMRPDISLHV
CQTVFKTDLR GVLGMVRAPC VVVQTTRDVS VPASVAAYLK AHLGGRTTVE FLQTEGHLPH
LSAPSLLAQV LRRALARY
