BDG2_ARATH
ID BDG2_ARATH Reviewed; 471 AA.
AC Q9FJ24;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable lysophospholipase BODYGUARD 2 {ECO:0000303|PubMed:16415209};
DE Short=AtBDG2 {ECO:0000303|PubMed:16415209};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=BDG2 {ECO:0000303|PubMed:16415209};
GN OrderedLocusNames=At5g41900 {ECO:0000312|Araport:AT5G41900};
GN ORFNames=K16L22.19 {ECO:0000312|EMBL:BAB10665.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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=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 [4]
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 [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 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; AB016871; BAB10665.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94741.1; -; Genomic_DNA.
DR EMBL; AK117277; BAC41950.1; -; mRNA.
DR EMBL; BT005385; AAO63449.1; -; mRNA.
DR RefSeq; NP_199005.1; NM_123555.3.
DR AlphaFoldDB; Q9FJ24; -.
DR SMR; Q9FJ24; -.
DR STRING; 3702.AT5G41900.1; -.
DR ESTHER; arath-At5g41900; Bodyguard.
DR MEROPS; S33.A28; -.
DR iPTMnet; Q9FJ24; -.
DR PaxDb; Q9FJ24; -.
DR PRIDE; Q9FJ24; -.
DR ProteomicsDB; 241211; -.
DR EnsemblPlants; AT5G41900.1; AT5G41900.1; AT5G41900.
DR GeneID; 834195; -.
DR Gramene; AT5G41900.1; AT5G41900.1; AT5G41900.
DR KEGG; ath:AT5G41900; -.
DR Araport; AT5G41900; -.
DR TAIR; locus:2153010; AT5G41900.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_051935_0_0_1; -.
DR InParanoid; Q9FJ24; -.
DR OMA; VVESCDH; -.
DR OrthoDB; 616687at2759; -.
DR PhylomeDB; Q9FJ24; -.
DR PRO; PR:Q9FJ24; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ24; 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 PRINTS; PR00111; ABHYDROLASE.
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..45
FT /evidence="ECO:0000255"
FT CHAIN 46..471
FT /note="Probable lysophospholipase BODYGUARD 2"
FT /id="PRO_0000437269"
FT DOMAIN 193..296
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 197
FT /evidence="ECO:0000255"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 446
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 471 AA; 53645 MW; C9E1988EA72B82A8 CRC64;
MGIARWLNRT VGFFVFALLD IADFLLCYTY KTLDYFLESE RKPCYCSSPP EAKAKTEKII
VSERGGYSKV VSLTRSKIHF DEISDTLYSR GPSLLTRLSK LVRSVKCFNY KGLIMRGNVV
ESCDHHESKK KISKGKKRLM TLNSTVIEKS STAPRWSDCH CSFCTSWLTS TNRDSLFVKV
QQPKDNKKAR DNVVFIHGFV SSSAFWTETL FPNFSDSAKS NYRFIAVDLL GYGRSPKPND
SLYTLREHLE MIEKSVISKF KLKTFHIVAH SLGCILALAL AVKHPGAIKS LTLLAPPYYK
VPKGVQPAQY VMREVARKEV WPPMQFGASV LSWYEHLGRT IGLVLIKNHQ LIEFVTRLLT
LNRMRTYLIE GFLCHTHNGS FHTLHNIIFG SGAKLDSYLD HVRDHVDCDV AIFHGGKDEL
IPVECSYSVK SKVPRATVHV IPDKDHITIV VGRQKDFARE LELIWQRTKS T
