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 02-NOV-2016, entry version 102. 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|TAIR:AT1G64670}; GN ORFNames=F1N19.24 {ECO:0000312|EMBL:AAF19684.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, GENE RP FAMILY, AND 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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 RT in 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 RT by 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 RT abscisic acid biosynthesis and osmotic stress tolerance in RT 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., RA Miquel M., Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., RA Wada H., 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 CC promoting cutin and suberin monomers loading (PubMed:16415209, CC PubMed:17257167, PubMed:18952782, PubMed:26990896). Involved in CC the regulation of abscissic acid (ABA) biosynthesis in response to CC osmotic stress. Plays an important role in osmotic stress and CC drought resistance (PubMed:21610183). Required to ensure a reduced CC permeability of aerial tissue, thus preventing transpiration CC (PubMed:18952782, PubMed:21610183, PubMed:26990896). Regulates CC lateral root hair development (PubMed:18952782). CC {ECO:0000269|PubMed:16415209, ECO:0000269|PubMed:17257167, CC ECO:0000269|PubMed:18952782, ECO:0000269|PubMed:21610183, CC ECO:0000269|PubMed:26990896}. CC -!- FUNCTION: Required for infection by the pathogenic necrotrophic CC fungus Botrytis cinerea, probably by regulating structural traits CC of the 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 CC cell wall. {ECO:0000269|PubMed:16415209}. CC -!- TISSUE SPECIFICITY: Expressed exclusively in protodermal and CC epidermal 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 CC vasculature. Observed in developing leaf buds, including the nodes CC and buds of cauline leaves (PubMed:26990896). In flowers, CC expressed in all organs, levels decreasing during flower aging. In CC the pistil, accumulates mostly in the abaxial epidermal cells, CC and, to a lower extent, in the septum and the inner ovary wall CC (PubMed:16415209, PubMed:26990896). Also expressed in the CC stigmatic papillae and vasculature of the sepals, petals and CC stamens. Accumulates in embryo during seed dehydration. Present in CC 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 CC cuticle structure associated with an enhanced accumulation of cell CC wall-bound lipids and epicuticular waxes (PubMed:16415209, CC PubMed:17257167, PubMed:18952782, PubMed:26990896). Reduced CC expression of abscissic acid (ABA) biosynthesis genes (e.g. NCED3) CC in response to osmotic stress (e.g. polyethylene glycol) leading CC to reduced levels of ABA and high sensitivity to osmotic stress CC and drought, especially during seed germination and early seedling CC development (PubMed:21610183). Increased aerial tissue CC permeability to the toluidine blue (TB) dye (PubMed:18952782). CC Enhanced transpiration. Strong decrease in total cutin monomer CC load in young leaves and flowers. Reduced levels of suberin in CC roots (PubMed:26990896). Pleiotropic effect on growth, viability, CC and cell differentiation, leading to abnormalities such as long CC 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 CC stress conditions (PubMed:18952782). Total immunity to the CC pathogenic necrotrophic fungus Botrytis cinerea accompanied by the CC release of a fungitoxic activity and increased expression of CC defense genes (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 -!- SIMILARITY: Contains 1 AB hydrolase-1 (Alpha/Beta hydrolase fold CC 1) domain. {ECO:0000255}. 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_105142.3. DR UniGene; At.35974; -. DR ProteinModelPortal; Q8LFX7; -. DR STRING; 3702.AT1G64670.1; -. DR ESTHER; arath-Q9SGU8; Bodyguard. DR MEROPS; S33.A27; -. DR EnsemblPlants; AT1G64670.1; AT1G64670.1; AT1G64670. DR GeneID; 842775; -. DR Gramene; AT1G64670.1; AT1G64670.1; AT1G64670. DR KEGG; ath:AT1G64670; -. DR TAIR; AT1G64670; -. DR eggNOG; KOG1454; Eukaryota. DR eggNOG; COG0596; LUCA. DR HOGENOM; HOG000243550; -. DR OMA; CTSWISS; -. DR Proteomes; UP000006548; Chromosome 1. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR. DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central. 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; IEP:UniProtKB. 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; Complete proteome; Hydrolase; KW Lipoprotein; Membrane; Palmitate; Plant defense; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 45 {ECO:0000255}. FT CHAIN 46 469 Probable lysophospholipase BODYGUARD 1. FT /FTId=PRO_0000437268. FT DOMAIN 185 439 AB hydrolase-1. {ECO:0000255}. FT ACT_SITE 189 189 {ECO:0000255}. FT ACT_SITE 263 263 Nucleophile. FT {ECO:0000250|UniProtKB:P04180}. FT ACT_SITE 410 410 Charge relay system. FT {ECO:0000250|UniProtKB:P04180}. FT ACT_SITE 438 438 Charge relay system. FT {ECO:0000250|UniProtKB:P04180}. FT LIPID 46 46 N-palmitoyl cysteine. FT {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 //