TMM_ARATH
ID TMM_ARATH Reviewed; 496 AA.
AC Q9SSD1; Q8GWY1;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein TOO MANY MOUTHS {ECO:0000303|PubMed:11536724};
DE AltName: Full=Receptor-like protein 17 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP17 {ECO:0000303|PubMed:18434605};
DE Flags: Precursor;
GN Name=TMM {ECO:0000303|PubMed:11536724};
GN Synonyms=RLP17 {ECO:0000303|PubMed:18434605};
GN OrderedLocusNames=At1g80080 {ECO:0000312|Araport:AT1G80080};
GN ORFNames=F18B13.16 {ECO:0000312|EMBL:AAD55468.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=11536724; DOI=10.2307/3870164;
RA Yang M., Sack F.D.;
RT "The too many mouths and four lips mutations affect stomatal production in
RT Arabidopsis.";
RL Plant Cell 7:2227-2239(1995).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9684356; DOI=10.1007/s004250050351;
RA Geisler M., Yang M., Sack F.D.;
RT "Divergent regulation of stomatal initiation and patterning in organ and
RT suborgan regions of the Arabidopsis mutants too many mouths and four
RT lips.";
RL Planta 205:522-530(1998).
RN [7]
RP FUNCTION.
RX PubMed=11090210; DOI=10.2307/3871106;
RA Geisler M., Nadeau J., Sack F.D.;
RT "Oriented asymmetric divisions that generate the stomatal spacing pattern
RT in arabidopsis are disrupted by the too many mouths mutation.";
RL Plant Cell 12:2075-2086(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12040198; DOI=10.1126/science.1069596;
RA Nadeau J.A., Sack F.D.;
RT "Control of stomatal distribution on the Arabidopsis leaf surface.";
RL Science 296:1697-1700(2002).
RN [9]
RP GENE FAMILY.
RX PubMed=15955925; DOI=10.1104/pp.104.054452;
RA Fritz-Laylin L.K., Krishnamurthy N., Toer M., Sjoelander K.V., Jones J.D.;
RT "Phylogenomic analysis of the receptor-like proteins of rice and
RT Arabidopsis.";
RL Plant Physiol. 138:611-623(2005).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [11]
RP GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=18434605; DOI=10.1104/pp.108.119487;
RA Wang G., Ellendorff U., Kemp B., Mansfield J.W., Forsyth A., Mitchell K.,
RA Bastas K., Liu C.-M., Woods-Toer A., Zipfel C., de Wit P.J.G.M.,
RA Jones J.D.G., Toer M., Thomma B.P.H.J.;
RT "A genome-wide functional investigation into the roles of receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 147:503-517(2008).
RN [12]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19513241; DOI=10.4161/psb.3.12.6254;
RA Serna L.;
RT "CAPRICE positively regulates stomatal formation in the Arabidopsis
RT hypocotyl.";
RL Plant Signal. Behav. 3:1077-1082(2008).
RN [13]
RP REVIEW.
RX PubMed=19042149; DOI=10.1016/j.pbi.2008.10.006;
RA Nadeau J.A.;
RT "Stomatal development: new signals and fate determinants.";
RL Curr. Opin. Plant Biol. 12:29-35(2009).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18979118; DOI=10.1007/s00425-008-0835-9;
RA Bhave N.S., Veley K.M., Nadeau J.A., Lucas J.R., Bhave S.L., Sack F.D.;
RT "TOO MANY MOUTHS promotes cell fate progression in stomatal development of
RT Arabidopsis stems.";
RL Planta 229:357-367(2009).
RN [15]
RP REVIEW.
RX PubMed=20705185; DOI=10.1016/s0070-2153(10)91009-0;
RA Dong J., Bergmann D.C.;
RT "Stomatal patterning and development.";
RL Curr. Top. Dev. Biol. 91:267-297(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ERECTA; ERL1 AND EPF2, AND
RP 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 [17]
RP REVIEW.
RX PubMed=22819466; DOI=10.1016/j.tplants.2012.06.013;
RA Torii K.U.;
RT "Mix-and-match: ligand-receptor pairs in stomatal development and beyond.";
RL Trends Plant Sci. 17:711-719(2012).
RN [18]
RP REVIEW.
RX PubMed=25064074; DOI=10.1016/j.pbi.2014.07.007;
RA Gust A.A., Felix G.;
RT "Receptor like proteins associate with SOBIR1-type of adaptors to form
RT bimolecular receptor kinases.";
RL Curr. Opin. Plant Biol. 21:104-111(2014).
RN [19]
RP DISRUPTION PHENOTYPE.
RX PubMed=24553751; DOI=10.1007/s00299-014-1571-1;
RA Yan L., Cheng X., Jia R., Qin Q., Guan L., Du H., Hou S.;
RT "New phenotypic characteristics of three tmm alleles in Arabidopsis
RT thaliana.";
RL Plant Cell Rep. 33:719-731(2014).
RN [20]
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 [21]
RP INTERACTION WITH EPFL9.
RX PubMed=26083750; DOI=10.1038/nature14561;
RA Lee J.S., Hnilova M., Maes M., Lin Y.C., Putarjunan A., Han S.K., Avila J.,
RA Torii K.U.;
RT "Competitive binding of antagonistic peptides fine-tunes stomatal
RT patterning.";
RL Nature 522:439-443(2015).
RN [22]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26203655; DOI=10.1371/journal.pgen.1005374;
RA Horst R.J., Fujita H., Lee J.S., Rychel A.L., Garrick J.M., Kawaguchi M.,
RA Peterson K.M., Torii K.U.;
RT "Molecular framework of a regulatory circuit initiating two-dimensional
RT spatial patterning of stomatal lineage.";
RL PLoS Genet. 11:E1005374-E1005374(2015).
RN [23]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=27446127; DOI=10.3389/fpls.2016.00897;
RA Jorda L., Sopena-Torres S., Escudero V., Nunez-Corcuera B.,
RA Delgado-Cerezo M., Torii K.U., Molina A.;
RT "ERECTA and BAK1 receptor like kinases interact to regulate immune
RT responses in arabidopsis.";
RL Front. Plant Sci. 7:897-897(2016).
RN [24]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH ERECTA AND ERL1.
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: Promotes cell fate progression in stomatal development. In
CC leaves, needed to correctly orient spacing divisions, to limit the
CC number of asymmetric divisions in neighbor cells, and to promote the
CC asymmetric (amplifying) divisions of meristemoids. In stems, promotes
CC the conversion of meristemoids into guard mother cells (GMC)
CC (PubMed:11090210, PubMed:12040198, PubMed:18979118). Positively
CC regulates CAPRICE (CPC) expression in differentiating stomaless-forming
CC cell files (PubMed:19513241). Forms constitutive complexes with ERECTA
CC and ERL1 involved in the recognition of the stomatal regulatory
CC peptides EPF1, EPF2 and EPFL9/STOMAGEN (PubMed:28536146). Modulates the
CC activity of the ligand-receptor pairs EPF2-ERECTA and EPF1-ERL1 in
CC stomatal development (PubMed:16002616, PubMed:22241782). Functions in a
CC combinatorial specific manner with the ERECTA-family (ERf) receptor
CC kinases in the regulation of the immune response (PubMed:27446127).
CC {ECO:0000269|PubMed:11090210, ECO:0000269|PubMed:12040198,
CC ECO:0000269|PubMed:16002616, ECO:0000269|PubMed:18979118,
CC ECO:0000269|PubMed:19513241, ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:27446127, ECO:0000269|PubMed:28536146}.
CC -!- SUBUNIT: Forms heterodimer with ERECTA or ERL1 through their
CC extracellular domains (PubMed:22241782, PubMed:28536146). Not able to
CC form homodimer (PubMed:22241782). Interacts with EPF2 but not with EPF1
CC (PubMed:22241782). Interacts with SERK1, SERK2, SERK3/BAK1 and SERK4
CC (PubMed:26320950). Interacts with EPFL9/STOMAGEN (PubMed:26083750).
CC {ECO:0000269|PubMed:22241782, ECO:0000269|PubMed:26083750,
CC ECO:0000269|PubMed:26320950, ECO:0000269|PubMed:28536146}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22241782,
CC ECO:0000303|PubMed:12040198}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In epidermal cells of developing shoots and leaves,
CC but not in roots. Expressed in the stomatal cell lineage in the
CC developing epidermis. Accumulates strongly in meristemoid mother cells
CC (MMC) and meristemoids, somewhat less in meristemoid sister cells
CC (stomatal-lineage ground cells, SLGC), and is barely detected in
CC pavement cells (PubMed:26203655). {ECO:0000269|PubMed:16002616,
CC ECO:0000269|PubMed:18979118, ECO:0000269|PubMed:26203655}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the stomatal precursor cells and in
CC immature stomata (PubMed:19513241). Decreases as leaves matured and no
CC expression in fully expanded leaves (PubMed:18979118).
CC {ECO:0000269|PubMed:18979118, ECO:0000269|PubMed:19513241}.
CC -!- INDUCTION: Up-regulated by SPCH-SCRM module.
CC {ECO:0000269|PubMed:26203655}.
CC -!- DISRUPTION PHENOTYPE: Lack of stomata in stem, hypocotyl and on the
CC adaxial side of the sepal. By contrast, cotyledons, anthers and abaxial
CC side of the sepal have excess stomata, with many in direct contact and
CC producing clusters. Altered responses to abscisic acid (ABA)
CC (PubMed:18434605, PubMed:24553751). Enhanced susceptibility to the
CC necrotrophic fungus Plectosphaerella cucumerina BMM (PcBMM)
CC (PubMed:27446127). {ECO:0000269|PubMed:11536724,
CC ECO:0000269|PubMed:18434605, ECO:0000269|PubMed:18979118,
CC ECO:0000269|PubMed:24553751, ECO:0000269|PubMed:27446127,
CC ECO:0000269|PubMed:9684356}.
CC -!- MISCELLANEOUS: TMM lacks an intracellular kinase domain and may
CC participate in active signal transduction only through physical
CC interaction with other proteins (PubMed:12040198). Overexpression of
CC TMM leads to altered formation of trichomes (PubMed:24553751).
CC {ECO:0000269|PubMed:24553751, ECO:0000303|PubMed:12040198}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009322; AAD55468.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36354.1; -; Genomic_DNA.
DR EMBL; AK118563; BAC43164.1; -; mRNA.
DR EMBL; BT005892; AAO64827.1; -; mRNA.
DR PIR; C96832; C96832.
DR RefSeq; NP_178125.1; NM_106657.3.
DR PDB; 5XJO; X-ray; 2.63 A; C/D=52-425.
DR PDB; 5XJX; X-ray; 3.06 A; C/D/F/H/J/L=28-460.
DR PDB; 5XKJ; X-ray; 3.48 A; C/D=28-460.
DR PDBsum; 5XJO; -.
DR PDBsum; 5XJX; -.
DR PDBsum; 5XKJ; -.
DR AlphaFoldDB; Q9SSD1; -.
DR SMR; Q9SSD1; -.
DR BioGRID; 29566; 5.
DR IntAct; Q9SSD1; 1.
DR STRING; 3702.AT1G80080.1; -.
DR PaxDb; Q9SSD1; -.
DR PRIDE; Q9SSD1; -.
DR ProteomicsDB; 234436; -.
DR EnsemblPlants; AT1G80080.1; AT1G80080.1; AT1G80080.
DR GeneID; 844348; -.
DR Gramene; AT1G80080.1; AT1G80080.1; AT1G80080.
DR KEGG; ath:AT1G80080; -.
DR Araport; AT1G80080; -.
DR TAIR; locus:2016319; AT1G80080.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_25_1; -.
DR InParanoid; Q9SSD1; -.
DR OMA; HEQEAVY; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9SSD1; -.
DR PRO; PR:Q9SSD1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SSD1; baseline and differential.
DR Genevisible; Q9SSD1; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
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:0042277; F:peptide binding; IPI:TAIR.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905034; P:regulation of antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0010376; P:stomatal complex formation; IMP:UniProtKB.
DR GO; GO:0010375; P:stomatal complex patterning; IMP:UniProtKB.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; Plant defense; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..496
FT /note="Protein TOO MANY MOUTHS"
FT /id="PRO_0000022557"
FT TOPO_DOM 24..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 158..182
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 183..208
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 210..228
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 229..252
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 254..276
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 277..300
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 302..325
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 326..350
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 351..373
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 375..401
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REGION 438..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="I -> F (in Ref. 3; BAC43164 and 4; AAO64827)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="L -> F (in Ref. 3; BAC43164 and 4; AAO64827)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="N -> S (in Ref. 3; BAC43164 and 4; AAO64827)"
FT /evidence="ECO:0000305"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5XJO"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:5XJX"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:5XJO"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:5XJO"
SQ SEQUENCE 496 AA; 54505 MW; BC4A7958FD3153F2 CRC64;
MARYEFFRQI FIVLSIVSPL VRSFTVITSD STAPSALIDG PQTGFTMTND GARTEPDEQD
AVYDIMRATG NDWAAAIPDV CRGRWHGIEC MPDQDNVYHV VSLSFGALSD DTAFPTCDPQ
RSYVSESLTR LKHLKALFFY RCLGRAPQRI PAFLGRLGSS LQTLVLRENG FLGPIPDELG
NLTNLKVLDL HKNHLNGSIP LSFNRFSGLR SLDLSGNRLT GSIPGFVLPA LSVLDLNQNL
LTGPVPPTLT SCGSLIKIDL SRNRVTGPIP ESINRLNQLV LLDLSYNRLS GPFPSSLQGL
NSLQALMLKG NTKFSTTIPE NAFKGLKNLM ILVLSNTNIQ GSIPKSLTRL NSLRVLHLEG
NNLTGEIPLE FRDVKHLSEL RLNDNSLTGP VPFERDTVWR MRRKLRLYNN AGLCVNRDSD
LDDAFGSKSG STVRLCDAET SRPAPSGTVQ HLSREEDGAL PDGATDVSST SKSLGFSYLS
AFFLVFPNFI FMLISS
