BDG3_ARATH
ID BDG3_ARATH Reviewed; 498 AA.
AC O22977;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Probable lysophospholipase BODYGUARD 3 {ECO:0000303|PubMed:16415209};
DE Short=AtBDG3 {ECO:0000303|PubMed:16415209};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=BDG3 {ECO:0000303|PubMed:16415209};
GN OrderedLocusNames=At4g24140 {ECO:0000312|Araport:AT4G24140};
GN ORFNames=T19F6.6 {ECO:0000312|EMBL:AAB63611.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [4]
RP GENE 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 [5]
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).
CC -!- FUNCTION: Involved in cuticle development and morphogenesis.
CC {ECO:0000250|UniProtKB:Q8LFX7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor
CC {ECO:0000255}. Secreted, cell wall {ECO:0000250|UniProtKB:Q8LFX7}.
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DR EMBL; AC002343; AAB63611.1; -; Genomic_DNA.
DR EMBL; AL109619; CAB51657.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81332.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84854.1; -; Genomic_DNA.
DR EMBL; AY090352; AAL91257.1; -; mRNA.
DR EMBL; BT002263; AAN72274.1; -; mRNA.
DR PIR; T13462; T13462.
DR RefSeq; NP_194145.1; NM_118546.4.
DR AlphaFoldDB; O22977; -.
DR STRING; 3702.AT4G24140.1; -.
DR ESTHER; arath-T19F06.6; Bodyguard.
DR MEROPS; S33.A26; -.
DR PaxDb; O22977; -.
DR PRIDE; O22977; -.
DR ProteomicsDB; 240618; -.
DR EnsemblPlants; AT4G24140.1; AT4G24140.1; AT4G24140.
DR GeneID; 828514; -.
DR Gramene; AT4G24140.1; AT4G24140.1; AT4G24140.
DR KEGG; ath:AT4G24140; -.
DR Araport; AT4G24140; -.
DR TAIR; locus:2134976; AT4G24140.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_051935_0_0_1; -.
DR InParanoid; O22977; -.
DR OMA; YLFEAEW; -.
DR OrthoDB; 616687at2759; -.
DR PhylomeDB; O22977; -.
DR PRO; PR:O22977; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O22977; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Hydrolase;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Secreted; Signal.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT CHAIN 56..498
FT /note="Probable lysophospholipase BODYGUARD 3"
FT /id="PRO_0000437270"
FT DOMAIN 220..326
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /evidence="ECO:0000255"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 446
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 474
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT LIPID 56
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 498 AA; 56211 MW; D28F8D75D7D317E3 CRC64;
MAVMKIKGAA TVAGTWLNEA VSFVVFCILD IVDSFLCLLY KAADYLFEAE WKPCYCLSDK
EPITTTRGKI LLSHNNGESK ILTLSPLQEL GGRSKIELED ISETLYTRPS LISDISTISV
NELNKRFVKV TRSESECSGH NEKTKNKRRR SLTKSSLTVN FTVVEMLRGK IRPQNLNHDI
SRWSDCDCGF CTSWASTSDK NHSLFVKTQI PNGVTAKEDV LFIHGFISSS AFWTETVFPS
LSASSSTHRL FAVDLLGFGK SPKPADSLYT LREHVEMIEK SVLHKYNVKS FHIVAHSLGC
ILALSLAARH GGLIKSLTLL APPYYPVPKG EKKPRQYVMK KVAPRKVWPP IALGASMACW
YEHISRTICL LICKHHRVWQ FIAGVLTRNN RTVNFLIEGF MCHTHNAAWH TLHNIICGTG
SKLDTYLDIV RDKLKCNVTI FHGGDDELIP VECSYNVKQR IPRARVKVIE HKDHITMVVG
RQDEFARELQ EIWKTSSC
