DSEL_ARATH
ID DSEL_ARATH Reviewed; 419 AA.
AC O49523; Q8GXS9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phospholipase A1-IIgamma;
DE EC=3.1.1.-;
DE AltName: Full=DAD1-like seedling establishment-related lipase;
DE Short=AtDSEL;
DE Short=Phospholipase DSEL;
GN Name=DSEL; OrderedLocusNames=At4g18550; ORFNames=F28J12.210;
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;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-419.
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130548; DOI=10.1016/j.tplants.2004.03.004;
RA Ryu S.B.;
RT "Phospholipid-derived signaling mediated by phospholipase A in plants.";
RL Trends Plant Sci. 9:229-235(2004).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=21477884; DOI=10.1016/j.jplph.2011.03.004;
RA Kim E.Y., Seo Y.S., Kim W.T.;
RT "AtDSEL, an Arabidopsis cytosolic DAD1-like acylhydrolase, is involved in
RT negative regulation of storage oil mobilization during seedling
RT establishment.";
RL J. Plant Physiol. 168:1705-1709(2011).
CC -!- FUNCTION: Acylhydrolase that catalyzes the hydrolysis of 1,3-
CC diacylglycerol (1,3-DAG) and 1-monoacylglycerol (1-MAG) at the sn-1
CC position. High activity toward 1,3-DAG and 1-MAG, but low activity
CC toward 1,2-diacylglycerol (1,2-DAG) and 1-lysophosphatidylcholine (1-
CC LPC), and no activity toward phosphatidylcholine (PC),
CC monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG),
CC triacylglycerol (TAG) and 2-monoacylglycerol (2-MAG). May be involved
CC in the negative regulation of seedling establishment by inhibiting the
CC breakdown, beta-oxidation and mobilization of seed storage oils.
CC {ECO:0000269|PubMed:21477884}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-6 with 1,3-DAG as substrate and at 30 degrees
CC Celsius. {ECO:0000269|PubMed:21477884};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21477884}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, stems and siliques, and, to
CC a lower extent, in flowers. {ECO:0000269|PubMed:21477884}.
CC -!- DISRUPTION PHENOTYPE: Mildly fast-growing seedlings regardless of the
CC presence of an exogenous carbon source, accompanied by a better beta-
CC oxidation and mobilization of seed storage oils.
CC {ECO:0000269|PubMed:21477884}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42692.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL021710; CAA16735.1; -; Genomic_DNA.
DR EMBL; AL161548; CAB78857.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84060.1; -; Genomic_DNA.
DR EMBL; BT030056; ABN04794.1; -; mRNA.
DR EMBL; AK118061; BAC42692.1; ALT_INIT; mRNA.
DR PIR; T04551; T04551.
DR RefSeq; NP_193590.1; NM_117969.3.
DR PDB; 2YIJ; X-ray; 2.00 A; A/B=1-419.
DR PDB; 7X0C; X-ray; 1.80 A; A/B=1-419.
DR PDBsum; 2YIJ; -.
DR PDBsum; 7X0C; -.
DR AlphaFoldDB; O49523; -.
DR SMR; O49523; -.
DR STRING; 3702.AT4G18550.1; -.
DR ESTHER; arath-At4g18550; Plant_phospholipase.
DR PaxDb; O49523; -.
DR PRIDE; O49523; -.
DR ProteomicsDB; 221911; -.
DR EnsemblPlants; AT4G18550.1; AT4G18550.1; AT4G18550.
DR GeneID; 827587; -.
DR Gramene; AT4G18550.1; AT4G18550.1; AT4G18550.
DR KEGG; ath:AT4G18550; -.
DR Araport; AT4G18550; -.
DR TAIR; locus:2124529; AT4G18550.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_018841_0_0_1; -.
DR InParanoid; O49523; -.
DR PhylomeDB; O49523; -.
DR BioCyc; ARA:AT4G18550-MON; -.
DR BioCyc; MetaCyc:AT4G18550-MON; -.
DR PRO; PR:O49523; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49523; baseline and differential.
DR Genevisible; O49523; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:TAIR.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IDA:TAIR.
DR GO; GO:0019915; P:lipid storage; IMP:TAIR.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR033556; PLA.
DR PANTHER; PTHR31828; PTHR31828; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1..419
FT /note="Phospholipase A1-IIgamma"
FT /id="PRO_0000409361"
FT COILED 1..21
FT /evidence="ECO:0000255"
FT COILED 207..227
FT /evidence="ECO:0000255"
FT ACT_SITE 236
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 302
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 27..34
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 41..59
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:2YIJ"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 237..251
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:2YIJ"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2YIJ"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2YIJ"
SQ SEQUENCE 419 AA; 47792 MW; 3B2B13089146482C CRC64;
MKRKKKEEEE EKLIVTREFA KRWRDLSGQN HWKGMLQPLD QDLREYIIHY GEMAQAGYDT
FNINTESQFA GASIYSRKDF FAKVGLEIAH PYTKYKVTKF IYATSDIHVP ESFLLFPISR
EGWSKESNWM GYVAVTDDQG TALLGRRDIV VSWRGSVQPL EWVEDFEFGL VNAIKIFGER
NDQVQIHQGW YSIYMSQDER SPFTKTNARD QVLREVGRLL EKYKDEEVSI TICGHSLGAA
LATLSATDIV ANGYNRPKSR PDKSCPVTAF VFASPRVGDS DFRKLFSGLE DIRVLRTRNL
PDVIPIYPPI GYSEVGDEFP IDTRKSPYMK SPGNLATFHC LEGYLHGVAG TQGTNKADLF
RLDVERAIGL VNKSVDGLKD ECMVPGKWRV LKNKGMAQQD DGSWELVDHE IDDNEDLDF
