BDG1_ARATH
ID BDG1_ARATH Reviewed; 469 AA.
AC Q8LFX7; Q9SGU8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Probable lysophospholipase BODYGUARD 1 {ECO:0000303|PubMed:16415209};
DE Short=AtBDG1 {ECO:0000303|PubMed:16415209};
DE EC=3.1.1.- {ECO:0000305};
DE AltName: Full=Protein 9-cis epoxycarotenoid dioxygenase defective 1 {ECO:0000303|PubMed:21610183};
DE AltName: Full=Protein COOL BREATH 5 {ECO:0000303|PubMed:26990896};
DE Flags: Precursor;
GN Name=BDG1 {ECO:0000303|PubMed:16415209};
GN Synonyms=BDG {ECO:0000303|PubMed:16415209},
GN CB5 {ECO:0000303|PubMed:26990896}, CED1 {ECO:0000303|PubMed:21610183};
GN OrderedLocusNames=At1g64670 {ECO:0000312|Araport:AT1G64670};
GN ORFNames=F1N19.24 {ECO:0000312|EMBL:AAF19684.1};
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16415209; DOI=10.1105/tpc.105.036079;
RA Kurdyukov S., Faust A., Nawrath C., Baer S., Voisin D., Efremova N.,
RA Franke R., Schreiber L., Saedler H., Metraux J.-P., Yephremov A.;
RT "The epidermis-specific extracellular BODYGUARD controls cuticle
RT development and morphogenesis in Arabidopsis.";
RL Plant Cell 18:321-339(2006).
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16299169; DOI=10.1104/pp.105.070805;
RA Suh M.C., Samuels A.L., Jetter R., Kunst L., Pollard M., Ohlrogge J.,
RA Beisson F.;
RT "Cuticular lipid composition, surface structure, and gene expression in
RT Arabidopsis stem epidermis.";
RL Plant Physiol. 139:1649-1665(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17257167; DOI=10.1111/j.1365-313x.2006.03017.x;
RA Chassot C., Nawrath C., Metraux J.-P.;
RT "Cuticular defects lead to full immunity to a major plant pathogen.";
RL Plant J. 49:972-980(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18952782; DOI=10.1105/tpc.107.055475;
RA Macgregor D.R., Deak K.I., Ingram P.A., Malamy J.E.;
RT "Root system architecture in Arabidopsis grown in culture is regulated by
RT sucrose uptake in the aerial tissues.";
RL Plant Cell 20:2643-2660(2008).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY OSMOTIC STRESS AND
RP ABSCISSIC ACID.
RC STRAIN=cv. Columbia GL1;
RX PubMed=21610183; DOI=10.1105/tpc.110.081943;
RA Wang Z.-Y., Xiong L., Li W., Zhu J.-K., Zhu J.;
RT "The plant cuticle is required for osmotic stress regulation of abscisic
RT acid biosynthesis and osmotic stress tolerance in Arabidopsis.";
RL Plant Cell 23:1971-1984(2011).
RN [11]
RP REVIEW.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=26990896; DOI=10.1111/nph.13924;
RA Jakobson L., Lindgren L.O., Verdier G., Laanemets K., Brosche M.,
RA Beisson F., Kollist H.;
RT "BODYGUARD is required for the biosynthesis of cutin in Arabidopsis.";
RL New Phytol. 211:614-626(2016).
CC -!- FUNCTION: Controls cuticle development and morphogenesis, by promoting
CC cutin and suberin monomers loading (PubMed:16415209, PubMed:17257167,
CC PubMed:18952782, PubMed:26990896). Involved in the regulation of
CC abscissic acid (ABA) biosynthesis in response to osmotic stress. Plays
CC an important role in osmotic stress and drought resistance
CC (PubMed:21610183). Required to ensure a reduced permeability of aerial
CC tissue, thus preventing transpiration (PubMed:18952782,
CC PubMed:21610183, PubMed:26990896). Regulates lateral root hair
CC development (PubMed:18952782). {ECO:0000269|PubMed:16415209,
CC ECO:0000269|PubMed:17257167, ECO:0000269|PubMed:18952782,
CC ECO:0000269|PubMed:21610183, ECO:0000269|PubMed:26990896}.
CC -!- FUNCTION: Required for infection by the pathogenic necrotrophic fungus
CC Botrytis cinerea, probably by regulating structural traits of the
CC cuticle. {ECO:0000269|PubMed:17257167}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor
CC {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:16415209}.
CC Note=Polar localization with accumulation in epidermis outermost cell
CC wall. {ECO:0000269|PubMed:16415209}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in protodermal and epidermal
CC cells of all organs, especially on adaxial sides.
CC {ECO:0000269|PubMed:16299169, ECO:0000269|PubMed:16415209}.
CC -!- DEVELOPMENTAL STAGE: In germinating seed, present in the embryo
CC epidermis, in cotyledons and in leaf primordia of the first true
CC leaves. In cotyledons, mostly expressed in guard cells and vasculature.
CC Observed in developing leaf buds, including the nodes and buds of
CC cauline leaves (PubMed:26990896). In flowers, expressed in all organs,
CC levels decreasing during flower aging. In the pistil, accumulates
CC mostly in the abaxial epidermal cells, and, to a lower extent, in the
CC septum and the inner ovary wall (PubMed:16415209, PubMed:26990896).
CC Also expressed in the stigmatic papillae and vasculature of the sepals,
CC petals and stamens. Accumulates in embryo during seed dehydration.
CC Present in the central cylinder of the roots. In addition, detected in
CC suberized tissues, such as siliques abscission zone and seed
CC chalaza/micropyle region (PubMed:26990896).
CC {ECO:0000269|PubMed:16415209, ECO:0000269|PubMed:26990896}.
CC -!- INDUCTION: Induced by osmotic stress and abscissic acid (ABA).
CC {ECO:0000269|PubMed:21610183}.
CC -!- DISRUPTION PHENOTYPE: Defects characteristic of the loss of cuticle
CC structure associated with an enhanced accumulation of cell wall-bound
CC lipids and epicuticular waxes (PubMed:16415209, PubMed:17257167,
CC PubMed:18952782, PubMed:26990896). Reduced expression of abscissic acid
CC (ABA) biosynthesis genes (e.g. NCED3) in response to osmotic stress
CC (e.g. polyethylene glycol) leading to reduced levels of ABA and high
CC sensitivity to osmotic stress and drought, especially during seed
CC germination and early seedling development (PubMed:21610183). Increased
CC aerial tissue permeability to the toluidine blue (TB) dye
CC (PubMed:18952782). Enhanced transpiration. Strong decrease in total
CC cutin monomer load in young leaves and flowers. Reduced levels of
CC suberin in roots (PubMed:26990896). Pleiotropic effect on growth,
CC viability, and cell differentiation, leading to abnormalities such as
CC long root hairs, excessively branched roots, shrinking of epidermal
CC cells, and flattened/misshapen trichomes (PubMed:16415209). Strong
CC increase of total lateral root lengths (TOT) on mild osmotic stress
CC conditions (PubMed:18952782). Total immunity to the pathogenic
CC necrotrophic fungus Botrytis cinerea accompanied by the release of a
CC fungitoxic activity and increased expression of defense genes
CC (PubMed:17257167). {ECO:0000269|PubMed:16415209,
CC ECO:0000269|PubMed:17257167, ECO:0000269|PubMed:18952782,
CC ECO:0000269|PubMed:21610183, ECO:0000269|PubMed:26990896}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19684.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ781319; CAH03662.1; -; Genomic_DNA.
DR EMBL; AC009519; AAF19684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34272.1; -; Genomic_DNA.
DR EMBL; AK119137; BAC43707.1; -; mRNA.
DR EMBL; BT005382; AAO63446.1; -; mRNA.
DR EMBL; AY084590; AAM61155.1; -; mRNA.
DR RefSeq; NP_564837.1; NM_105142.4.
DR AlphaFoldDB; Q8LFX7; -.
DR SMR; Q8LFX7; -.
DR STRING; 3702.AT1G64670.1; -.
DR ESTHER; arath-Q9SGU8; Bodyguard.
DR MEROPS; S33.A27; -.
DR PaxDb; Q8LFX7; -.
DR PRIDE; Q8LFX7; -.
DR ProteomicsDB; 240721; -.
DR EnsemblPlants; AT1G64670.1; AT1G64670.1; AT1G64670.
DR GeneID; 842775; -.
DR Gramene; AT1G64670.1; AT1G64670.1; AT1G64670.
DR KEGG; ath:AT1G64670; -.
DR Araport; AT1G64670; -.
DR TAIR; locus:2019464; AT1G64670.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_051935_0_0_1; -.
DR InParanoid; Q8LFX7; -.
DR OMA; WEFITKC; -.
DR PRO; PR:Q8LFX7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LFX7; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0048527; P:lateral root development; IMP:UniProtKB.
DR GO; GO:1901959; P:positive regulation of cutin biosynthetic process; IMP:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0010115; P:regulation of abscisic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0010345; P:suberin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010148; P:transpiration; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Abscisic acid biosynthesis; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..469
FT /note="Probable lysophospholipase BODYGUARD 1"
FT /id="PRO_0000437268"
FT DOMAIN 185..439
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 189
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 410
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 438
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT LIPID 46
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 469 AA; 53428 MW; 7DBCBBB9D8B58B58 CRC64;
MGFSRSLNRT VGVFVFFILD IVDFLLCFTY KTLDFFFESE WKPCYCCPPP EAKPISAGGN
RGGKMIVSER SGDYSKVVSL TRTKIYLDEI SDTLYSRPSL LTKLTKLVKC FKKDVVKCCD
ESKKRSPSTK KTLLTVNSTV VEKLQRTPRW SDCHCTFCTS WLSSSNQSLF VNVQQPTDNK
AQENVVFIHG FLSSSTFWTE TLFPNFSDSA KSNYRFLAVD LLGYGKSPKP NDSLYTLKEH
LEMIERSVIS QFRLKTFHLV AHSLGCILAL ALAVKHPGAI KSLTLLAPPY YSVPKGVQGT
QYVMRRLAPK EVWPPMAFGA SVASWYEHIS RTVSLVLCKN HHLLEFLTRL LTRNRMRTYL
IEGFLCHTHN ASWHTLHNII FGSGSKVEAY LDHVRDNVDC EVAVFHGGRD ELIPVECSYG
VKRKVPRARI HVVPDKDHIT IVVGRQKEFA RELELIWRRS TTPQLHSIN
