BDG4_ARATH
ID BDG4_ARATH Reviewed; 417 AA.
AC Q700D5; B3H685; Q9FN74;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable lysophospholipase BODYGUARD 4 {ECO:0000303|PubMed:16415209};
DE Short=AtBDG4 {ECO:0000303|PubMed:16415209};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=BDG4 {ECO:0000303|PubMed:16415209};
GN OrderedLocusNames=At5g17780 {ECO:0000312|Araport:AT5G17780};
GN ORFNames=MVA3.14 {ECO:0000312|EMBL:BAB09577.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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].
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [4]
RP TISSUE SPECIFICITY.
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 [5]
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 [6]
RP INDUCTION BY UV-B.
RX PubMed=16829591; DOI=10.1105/tpc.105.040097;
RA Oravecz A., Baumann A., Mate Z., Brzezinska A., Molinier J., Oakeley E.J.,
RA Adam E., Schaefer E., Nagy F., Ulm R.;
RT "CONSTITUTIVELY PHOTOMORPHOGENIC1 is required for the UV-B response in
RT Arabidopsis.";
RL Plant Cell 18:1975-1990(2006).
RN [7]
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q700D5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q700D5-2; Sequence=VSP_058509;
CC -!- TISSUE SPECIFICITY: Expressed in epidermal cells.
CC {ECO:0000269|PubMed:16299169}.
CC -!- INDUCTION: By UV-B. {ECO:0000269|PubMed:16829591}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09577.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB006706; BAB09577.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED92467.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92468.1; -; Genomic_DNA.
DR EMBL; AJ630490; CAG25863.1; -; mRNA.
DR EMBL; AY568662; AAS79552.1; -; mRNA.
DR RefSeq; NP_001119241.1; NM_001125769.2. [Q700D5-2]
DR RefSeq; NP_197280.2; NM_121784.2. [Q700D5-1]
DR AlphaFoldDB; Q700D5; -.
DR SMR; Q700D5; -.
DR STRING; 3702.AT5G17780.2; -.
DR ESTHER; arath-Q9FN74; Bodyguard.
DR MEROPS; S33.A73; -.
DR PRIDE; Q700D5; -.
DR ProteomicsDB; 240777; -. [Q700D5-1]
DR EnsemblPlants; AT5G17780.1; AT5G17780.1; AT5G17780. [Q700D5-1]
DR EnsemblPlants; AT5G17780.2; AT5G17780.2; AT5G17780. [Q700D5-2]
DR GeneID; 831646; -.
DR Gramene; AT5G17780.1; AT5G17780.1; AT5G17780. [Q700D5-1]
DR Gramene; AT5G17780.2; AT5G17780.2; AT5G17780. [Q700D5-2]
DR KEGG; ath:AT5G17780; -.
DR Araport; AT5G17780; -.
DR TAIR; locus:2175911; AT5G17780.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_051935_0_0_1; -.
DR OMA; CGGAKFM; -.
DR OrthoDB; 616687at2759; -.
DR PhylomeDB; Q700D5; -.
DR PRO; PR:Q700D5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q700D5; 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 GO; GO:0010224; P:response to UV-B; IEP: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 Alternative splicing; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Secreted; Signal.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT CHAIN 50..417
FT /note="Probable lysophospholipase BODYGUARD 4"
FT /id="PRO_0000437271"
FT DOMAIN 150..259
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 154
FT /evidence="ECO:0000255"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 395
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT LIPID 50
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT VAR_SEQ 139
FT /note="R -> RET (in isoform 2)"
FT /id="VSP_058509"
SQ SEQUENCE 417 AA; 47456 MW; 5B860F2289A51218 CRC64;
MSFPRKFGTA IHAALSFIVF FFLDLLDAIL CVVYEFVDEI LEENSTGCYC TAAAPQSQTT
DENELSSETL FGRRNIFRGM WFLGFAREFK SKLSRKLRKS KIHQESVNRW SDCGCKSCKS
WTKNEDGNLH VVVKDSTSRE YSVQEPSENV IFIHGFMGSS HFWTETVFEH IQKDDYRLLA
IDLLGFGESP KPRDSLYTLK DHVDTIERSV IKPYQLDSFH VVAHSMGCLI ALALAAKHSN
IVKSVTLVAP PYFPSSVEGS VLNRIARKRL WPPLAFGTAV MSWYEHIGRC VCFIICKHHK
IWEWLIKLCI GKREIHWKIK DITRHTHHSA WHSMHNVICG GSKVADEHLE TLIKSGVKIH
LMQGDCDQIV PSHCSGNMKR TFPAVEVDII TGADHDSMIS GRGEEFAEKL ESIWCSC
