BDG5_ARATH
ID BDG5_ARATH Reviewed; 443 AA.
AC Q9FN79;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable lysophospholipase BODYGUARD 5 {ECO:0000303|PubMed:16415209};
DE Short=AtBDG5 {ECO:0000303|PubMed:16415209};
DE EC=3.1.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=BDG5 {ECO:0000303|PubMed:16415209};
GN OrderedLocusNames=At5g17720 {ECO:0000312|Araport:AT5G17720};
GN ORFNames=MVA3.7 {ECO:0000312|EMBL:BAB09571.1};
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 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 [4]
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; AB006706; BAB09571.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92460.1; -; Genomic_DNA.
DR RefSeq; NP_197274.1; NM_121778.1.
DR AlphaFoldDB; Q9FN79; -.
DR STRING; 3702.AT5G17720.1; -.
DR ESTHER; arath-Q9FN79; Bodyguard.
DR MEROPS; S33.A76; -.
DR MetOSite; Q9FN79; -.
DR PaxDb; Q9FN79; -.
DR PRIDE; Q9FN79; -.
DR EnsemblPlants; AT5G17720.1; AT5G17720.1; AT5G17720.
DR GeneID; 831639; -.
DR Gramene; AT5G17720.1; AT5G17720.1; AT5G17720.
DR KEGG; ath:AT5G17720; -.
DR Araport; AT5G17720; -.
DR TAIR; locus:2175936; AT5G17720.
DR eggNOG; KOG1454; Eukaryota.
DR HOGENOM; CLU_051935_0_0_1; -.
DR InParanoid; Q9FN79; -.
DR OMA; HEVANRW; -.
DR OrthoDB; 616687at2759; -.
DR PhylomeDB; Q9FN79; -.
DR PRO; PR:Q9FN79; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN79; 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 3: Inferred from homology;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Hydrolase;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Secreted; Signal.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..443
FT /note="Probable lysophospholipase BODYGUARD 5"
FT /id="PRO_0000437272"
FT DOMAIN 163..268
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 167
FT /evidence="ECO:0000255"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT LIPID 53
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 443 AA; 50180 MW; 023EF3503C837248 CRC64;
MITSSFSEKC TSVINGAPSW AVFFLFDLLD YFLCIVFRFL DEVMEEKSES CHCNNPREKT
HFAEYEFLSE TLYRRRNVFR QAGFLRFANK LPEITKKIGI VTFLRKFLFP HTMNKVSHEV
ANRWSDCGCK TCVSWINTDK LNVIVKQPSI SDLSISNKPV ENVIFVHGFL ASSSFWTNTV
FKYLPETTEG TNYRFFAIDL LGFGDSPKPR ASQYSLKEHV EMIEKSVILP NNLTSFHVVA
HSMGCIIGIA LAAKFSDSVK SVALVAPPYF ADSKGGASCA ALDVVAKKKL WPPASFFTAM
MCWYEHIGRG VCLVFCRHHR TWERIIKIVT WRRKLPTAIM DFTKHTHQSG WHSMHNVICG
GAKFTDKHLE TLIKSGVKIN VMQGDKDVVV PIDCLSNMKG KFPAVEVEVI AGTDHSTVIM
SRREVFAANL VSLWATSEKK QKV
