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 22-FEB-2023, entry version 130. 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}; 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; 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 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; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR PANTHER; PTHR43689; HYDROLASE; 1. DR PANTHER; PTHR43689:SF25; LYSOPHOSPHOLIPASE BODYGUARD 1-RELATED; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 //