SDP1_ARATH
ID SDP1_ARATH Reviewed; 825 AA.
AC Q9LZA6; Q56WV8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Triacylglycerol lipase SDP1 {ECO:0000303|PubMed:16473965};
DE EC=3.1.1.3 {ECO:0000269|PubMed:16473965};
DE AltName: Full=Protein SUGAR-DEPENDENT 1 {ECO:0000303|PubMed:16473965};
GN Name=SDP1 {ECO:0000303|PubMed:16473965};
GN OrderedLocusNames=At5g04040 {ECO:0000312|Araport:AT5G04040};
GN ORFNames=F8F6.10, F8F6_250 {ECO:0000312|EMBL:CAB85524.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 451-825.
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF GLY-241; GLU-438 AND PRO-456, ACTIVITY
RP REGULATION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16473965; DOI=10.1105/tpc.105.040543;
RA Eastmond P.J.;
RT "SUGAR-DEPENDENT1 encodes a patatin domain triacylglycerol lipase that
RT initiates storage oil breakdown in germinating Arabidopsis seeds.";
RL Plant Cell 18:665-675(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION.
RX PubMed=19136267; DOI=10.1016/j.plaphy.2008.12.005;
RA Quettier A.L., Eastmond P.J.;
RT "Storage oil hydrolysis during early seedling growth.";
RL Plant Physiol. Biochem. 47:485-490(2009).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23686420; DOI=10.1104/pp.113.219840;
RA Kelly A.A., van Erp H., Quettier A.L., Shaw E., Menard G., Kurup S.,
RA Eastmond P.J.;
RT "The sugar-dependent1 lipase limits triacylglycerol accumulation in
RT vegetative tissues of Arabidopsis.";
RL Plant Physiol. 162:1282-1289(2013).
RN [9]
RP FUNCTION.
RX PubMed=25293755; DOI=10.1105/tpc.114.130377;
RA Fan J., Yan C., Roston R., Shanklin J., Xu C.;
RT "Arabidopsis lipins, PDAT1 acyltransferase, and SDP1 triacylglycerol lipase
RT synergistically direct fatty acids toward beta-oxidation, thereby
RT maintaining membrane lipid homeostasis.";
RL Plant Cell 26:4119-4134(2014).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=25775518; DOI=10.1073/pnas.1403322112;
RA Thazar-Poulot N., Miquel M., Fobis-Loisy I., Gaude T.;
RT "Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4158-4163(2015).
RN [11]
RP FUNCTION.
RX PubMed=27466365; DOI=10.1074/jbc.m116.748814;
RA Cui S., Hayashi Y., Otomo M., Mano S., Oikawa K., Hayashi M., Nishimura M.;
RT "Sucrose production mediated by lipid metabolism suppresses the physical
RT interaction of peroxisomes and oil bodies during germination of Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 291:19734-19745(2016).
CC -!- FUNCTION: Involved in the release of fatty acids from the oil body in
CC germinating seedlings (PubMed:16473965, PubMed:19136267,
CC PubMed:27466365). Can hydrolyze triacylglycerols and diacylglycerols
CC but not monoacylglycerols, phospholipids, galactolipids or cholesterol
CC esters (PubMed:16473965, PubMed:19136267). SDP1 lipase activity is
CC required to limit triacylglycerol accumulation in roots, leaves and
CC stems, which are vegetative tissues (PubMed:23686420). Functions
CC synergistically with PDAT1 in regulating fatty acid flow from membrane
CC lipid synthesis toward peroxisomal beta-oxidation through a transient
CC triacylglycerol pool (PubMed:25293755). {ECO:0000269|PubMed:16473965,
CC ECO:0000269|PubMed:19136267, ECO:0000269|PubMed:23686420,
CC ECO:0000269|PubMed:25293755, ECO:0000269|PubMed:27466365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:16473965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000269|PubMed:16473965};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:16473965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000269|PubMed:16473965};
CC -!- ACTIVITY REGULATION: Inhibited by diethyl-p-nitrophenyl phosphate,
CC diisopropyl fluorophosphate and [E]-6-[bromoethylene]-3-[1-
CC naphthalenyl]-2H-tetrahydropyran-2-one. {ECO:0000269|PubMed:16473965}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Broad optimum pH around 8.0. {ECO:0000269|PubMed:16473965};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16473965,
CC ECO:0000269|PubMed:25775518}. Membrane {ECO:0000269|PubMed:16473965};
CC Peripheral membrane protein {ECO:0000305}. Peroxisome
CC {ECO:0000269|PubMed:25775518}. Note=Associates with the oil body
CC membrane (PubMed:16473965). Migrates from peroxisomes to the oil body
CC surface through peroxisomal tubulation (PubMed:25775518).
CC {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:25775518}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems.
CC {ECO:0000269|PubMed:23686420}.
CC -!- DEVELOPMENTAL STAGE: Transcript levels increase at the beginning of
CC seed maturation and remain high until seed desiccation is completed.
CC High levels early in seed imbibition, but decline as the seed
CC germinates. {ECO:0000269|PubMed:16473965}.
CC -!- DISRUPTION PHENOTYPE: Not impaired in germination, but much slower rate
CC of postgerminative growth. {ECO:0000269|PubMed:16473965}.
CC -!- MISCELLANEOUS: Transcript levels do not correlate positively with
CC enzyme activity, suggesting a post-transcriptional regulation.
CC {ECO:0000269|PubMed:16473965}.
CC -!- SIMILARITY: Belongs to the PLPL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94338.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL162873; CAB85524.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90687.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71199.1; -; Genomic_DNA.
DR EMBL; AY136470; AAM97135.1; -; mRNA.
DR EMBL; AK221922; BAD94338.1; ALT_INIT; mRNA.
DR PIR; T48431; T48431.
DR RefSeq; NP_001332745.1; NM_001342744.1.
DR RefSeq; NP_196024.1; NM_120486.7.
DR AlphaFoldDB; Q9LZA6; -.
DR STRING; 3702.AT5G04040.1; -.
DR SwissLipids; SLP:000001944; -.
DR iPTMnet; Q9LZA6; -.
DR PaxDb; Q9LZA6; -.
DR PRIDE; Q9LZA6; -.
DR ProteomicsDB; 232951; -.
DR EnsemblPlants; AT5G04040.1; AT5G04040.1; AT5G04040.
DR EnsemblPlants; AT5G04040.2; AT5G04040.2; AT5G04040.
DR GeneID; 830283; -.
DR Gramene; AT5G04040.1; AT5G04040.1; AT5G04040.
DR Gramene; AT5G04040.2; AT5G04040.2; AT5G04040.
DR KEGG; ath:AT5G04040; -.
DR Araport; AT5G04040; -.
DR TAIR; locus:2150645; AT5G04040.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_013822_0_0_1; -.
DR InParanoid; Q9LZA6; -.
DR OMA; PRDNTRG; -.
DR OrthoDB; 425613at2759; -.
DR PhylomeDB; Q9LZA6; -.
DR BioCyc; ARA:AT5G04040-MON; -.
DR BioCyc; MetaCyc:AT5G04040-MON; -.
DR PRO; PR:Q9LZA6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZA6; baseline and differential.
DR Genevisible; Q9LZA6; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:TAIR.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:TAIR.
DR GO; GO:0006641; P:triglyceride metabolic process; IGI:TAIR.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Glycerol metabolism; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid droplet; Lipid metabolism; Membrane; Peroxisome; Reference proteome.
FT CHAIN 1..825
FT /note="Triacylglycerol lipase SDP1"
FT /id="PRO_0000398610"
FT DOMAIN 232..437
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 632..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 263..267
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 703..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 424
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 241
FT /note="G->D: In sdp1-3; loss of activity."
FT /evidence="ECO:0000269|PubMed:16473965"
FT MUTAGEN 438
FT /note="E->K: In sdp1-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:16473965"
FT MUTAGEN 456
FT /note="P->S: In sdp1-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:16473965"
SQ SEQUENCE 825 AA; 92092 MW; A80717BD5971F144 CRC64;
MDISNEASVD PFSIGPSSIM GRTIAFRVLF CRSMSQLRRD LFRFLLHWFL RFKLTVSPFV
SWFHPRNPQG ILAVVTIIAF VLKRYTNVKI KAEMAYRRKF WRNMMRTALT YEEWAHAAKM
LEKETPKMNE SDLYDEELVK NKLQELRHRR QEGSLRDIMF CMRADLVRNL GNMCNSELHK
GRLQVPRHIK EYIDEVSTQL RMVCNSDSEE LSLEEKLSFM HETRHAFGRT ALLLSGGASL
GAFHVGVVRT LVEHKLLPRI IAGSSVGSII CAVVASRSWP ELQSFFENSL HSLQFFDQLG
GVFSIVKRVM TQGALHDIRQ LQCMLRNLTS NLTFQEAYDM TGRILGITVC SPRKHEPPRC
LNYLTSPHVV IWSAVTASCA FPGLFEAQEL MAKDRSGEIV PYHPPFNLDP EVGTKSSSGR
RWRDGSLEVD LPMMQLKELF NVNHFIVSQA NPHIAPLLRL KDLVRAYGGR FAAKLAHLVE
MEVKHRCNQV LELGFPLGGL AKLFAQEWEG DVTVVMPATL AQYSKIIQNP THVELQKAAN
QGRRCTWEKL SAIKSNCGIE LALDDSVAIL NHMRRLKKSA ERAATATSSS HHGLASTTRF
NASRRIPSWN VLARENSTGS LDDLVTDNNL HASSGRNLSD SETESVELSS WTRTGGPLMR
TASANKFIDF VQSLDIDIAL VRGFSSSPNS PAVPPGGSFT PSPRSIAAHS DIESNSNSNN
LGTSTSSITV TEGDLLQPER TSNGFVLNVV KRENLGMPSI GNQNTELPES VQLDIPEKEM
DCSSVSEHEE DDNDNEEEHN GSSLVTVSSE DSGLQEPVSG SVIDA
