SDP1L_ARATH
ID SDP1L_ARATH Reviewed; 801 AA.
AC Q9M1I6;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Triacylglycerol lipase SDP1L {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000269|PubMed:19136267};
DE AltName: Full=Protein SDP1-LIKE {ECO:0000303|PubMed:19136267};
GN Name=SDP1L {ECO:0000303|PubMed:19136267};
GN OrderedLocusNames=At3g57140 {ECO:0000312|Araport:AT3G57140};
GN ORFNames=F24I3.220 {ECO:0000312|EMBL:CAB72184.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May be involved in the release of fatty acids from the oil
CC body in germinating seedlings. Can hydrolyze triacylglycerols in vitro.
CC {ECO:0000269|PubMed:19136267}.
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:19136267};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9LZA6}.
CC Membrane {ECO:0000250|UniProtKB:Q9LZA6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9LZA6}. Note=Associates with the oil body
CC membrane. {ECO:0000250|UniProtKB:Q9LZA6}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mature pollen.
CC {ECO:0000269|PubMed:19136267}.
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DR EMBL; AL138655; CAB72184.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79619.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79620.1; -; Genomic_DNA.
DR EMBL; AK117921; BAC42559.1; -; mRNA.
DR EMBL; BT005969; AAO64904.1; -; mRNA.
DR PIR; T47774; T47774.
DR RefSeq; NP_191273.1; NM_115573.4.
DR RefSeq; NP_974449.1; NM_202720.2.
DR AlphaFoldDB; Q9M1I6; -.
DR STRING; 3702.AT3G57140.2; -.
DR PaxDb; Q9M1I6; -.
DR PRIDE; Q9M1I6; -.
DR ProteomicsDB; 234516; -.
DR EnsemblPlants; AT3G57140.1; AT3G57140.1; AT3G57140.
DR EnsemblPlants; AT3G57140.2; AT3G57140.2; AT3G57140.
DR GeneID; 824881; -.
DR Gramene; AT3G57140.1; AT3G57140.1; AT3G57140.
DR Gramene; AT3G57140.2; AT3G57140.2; AT3G57140.
DR KEGG; ath:AT3G57140; -.
DR Araport; AT3G57140; -.
DR TAIR; locus:2080610; AT3G57140.
DR eggNOG; KOG2214; Eukaryota.
DR HOGENOM; CLU_013822_0_0_1; -.
DR InParanoid; Q9M1I6; -.
DR OMA; AQMFTDY; -.
DR OrthoDB; 425613at2759; -.
DR PhylomeDB; Q9M1I6; -.
DR BioCyc; ARA:AT3G57140-MON; -.
DR PRO; PR:Q9M1I6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1I6; baseline and differential.
DR Genevisible; Q9M1I6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
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 Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..801
FT /note="Triacylglycerol lipase SDP1L"
FT /id="PRO_0000433128"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 233..436
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 648..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..268
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 801 AA; 89934 MW; 6A8AE5662C4E7712 CRC64;
MDISNEAGVD AFSIIGPTTI IGRTIAVRIL FCNSVSIFRH KVFRILKFFL RGGRVLLSPF
VSLLHPRNPQ GILVMVTTMA FLLNRYTSLK AKAEMAYRRK FWRNMMRAAL TYEEWSHAAK
MLDKETPKVN ETDLFDVELV SNKLDELKHR RHEGSLRDII FCMRADLVRN LGNMCNPELH
KGRLHVPRLI KEYIDEVSTQ LRMVCDMDTE ELSLEEKLSF MHETRHAYGR TALLLSGGAS
LGAFHLGVVK TLVEHKLLPR IIAGSSVGSV MCAVVGTRSW PELQSFFEGS WHALQFFDQM
GGIFTTVKRV MTQGAVHEIR HLQWKLRNLT NNLTFQEAYD ITGRILGITV CSLRKHEPPR
CLNYLTSPHV VIWSAVTASC AFPGLFEAQE LMAKDRTGEI VPYHPPFNLD PEEGSASVRR
WRDGSLEMDL PMIQLKELFN VNHFIVSQAN PHIAPFLRMK EFVRACGGRF AAKLAQLAEM
EVKHRCNQVL ELGLPLREVA SLFAQEWEGD VTIVMPATFS QYLKIIQNPS NVEIQKAANQ
GRRCTWEKLA VIKANFGIEL ALDECVTVLN HMRRLKRSAE RAAAFSAISS SPPSKHLLAG
TNRFNASKRI PSWNCIARQN SSGSVDDDVL AEASRLYQHI VVGSGRNSNR TSNLSHTYDA
GSECDSPEAE DWTRSGGPLM RTNSAQMFTD YVQNLDAVDP EQIRASENDS IVAASSSSHS
ITVTEGDYLQ TGRTHNGFVL NLVRGENLRM NSEPEDSQNE SEIPETPESV QLDSPEKDII
DGESSASEDG DAQANLIHDH E
