OBL1_ARATH
ID OBL1_ARATH Reviewed; 518 AA.
AC F4JFU8; A0A178V8G3; Q8H1D5; Q93ZZ5; Q9LUL3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Triacylglycerol lipase OBL1 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:29178188};
DE AltName: Full=Oil body lipase 1 {ECO:0000303|PubMed:29178188};
DE Short=AtOBL1 {ECO:0000303|PubMed:29178188};
GN Name=OBL1 {ECO:0000303|PubMed:29178188};
GN OrderedLocusNames=At3g14360 {ECO:0000312|Araport:AT3G14360};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] OF 7-518 AND 50-518.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-339, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29178188; DOI=10.1111/nph.14902;
RA Mueller A.O., Ischebeck T.;
RT "Characterization of the enzymatic activity and physiological function of
RT the lipid droplet-associated triacylglycerol lipase AtOBL1.";
RL New Phytol. 217:1062-1076(2018).
CC -!- FUNCTION: Acid lipase that can hydrolyze a range of triacylglycerols
CC without a clear preference for acyl-chains (PubMed:29178188). Can also
CC cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol,
CC but not phospatidylcholine, phosphatidylethanolamine, or sterol esters
CC (PubMed:29178188). Required for pollen tube growth (PubMed:29178188).
CC Triacylglycerol hydrolysis by OBL1 may provide acyl groups for the
CC synthesis of membrane lipids in growing pollen tubes (Probable).
CC {ECO:0000269|PubMed:29178188, ECO:0000305|PubMed:29178188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000269|PubMed:29178188};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381;
CC Evidence={ECO:0000269|PubMed:29178188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:29178188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000269|PubMed:29178188};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:29178188};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:29178188}.
CC Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC Note=Associates with the oil body membrane.
CC {ECO:0000305|PubMed:29178188}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen grains, pollen tubes,
CC developing embryos, developing seeds and germinating seeds.
CC {ECO:0000269|PubMed:29178188}.
CC -!- DISRUPTION PHENOTYPE: Reduced pollen tube growth.
CC {ECO:0000269|PubMed:29178188}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL07239.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB01041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB022220; BAB01041.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75507.1; -; Genomic_DNA.
DR EMBL; AY056160; AAL07239.1; ALT_INIT; mRNA.
DR EMBL; AY150508; AAN13024.1; -; mRNA.
DR RefSeq; NP_566484.2; NM_112294.5.
DR AlphaFoldDB; F4JFU8; -.
DR SMR; F4JFU8; -.
DR STRING; 3702.AT3G14360.1; -.
DR SwissLipids; SLP:000001943; -.
DR ESTHER; arath-At3g14360; Triacylglycerol-lipase-OBL1-like.
DR PaxDb; F4JFU8; -.
DR PRIDE; F4JFU8; -.
DR ProteomicsDB; 208150; -.
DR EnsemblPlants; AT3G14360.1; AT3G14360.1; AT3G14360.
DR GeneID; 820657; -.
DR Gramene; AT3G14360.1; AT3G14360.1; AT3G14360.
DR KEGG; ath:AT3G14360; -.
DR Araport; AT3G14360; -.
DR TAIR; locus:2091025; AT3G14360.
DR eggNOG; KOG4569; Eukaryota.
DR HOGENOM; CLU_032957_2_0_1; -.
DR InParanoid; F4JFU8; -.
DR OMA; EYLNAVW; -.
DR OrthoDB; 772353at2759; -.
DR PRO; PR:F4JFU8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JFU8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:TAIR.
DR GO; GO:0033878; F:hormone-sensitive lipase activity; IDA:TAIR.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR044819; OBL-like.
DR PANTHER; PTHR46086; PTHR46086; 2.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Triacylglycerol lipase OBL1"
FT /id="PRO_0000450282"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 337..341
FT /note="GXSXG"
FT /evidence="ECO:0000305|PubMed:29178188"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29178188"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 496
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 339
FT /note="S->A: Loss of catalytic activity; reduces pollen
FT tube growth."
FT /evidence="ECO:0000269|PubMed:29178188"
FT CONFLICT 305
FT /note="L -> H (in Ref. 3; AAL07239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 59607 MW; 370829EEEE3A5029 CRC64;
MHKDNDSGSG SNPGQVSNYL IVRPHRGGYI DLFRYGVRDD QTSKAKFLEM PDNREWSTIT
IDEEAEDHRW VIVVSILVRK IIRLLRTPME FTGFVVDFFL NLFSANGGFF GLLLRLIQAK
VVIPERGSVT FVSTIGQLDG RISLYKEWNF VEHLEGIDSV DSGRVKIELG SRGLMDLCVM
ASKLAYENAK VVENVVDLHW KMNLVEFLDC WNDYQKQMST QVFVFTDKQK DANLIVISFR
GTEPFDADDW GTDFDYSWYE VPNVGKLHMG FLEAMGLGNR DDTTTFHYNL FEQTSSEEEN
SKKNLLDMVE RSAYYAVRVI LKRLLSEHEN ARFVVTGHSL GGALAILFPT LLVLNEETEI
MKRLLGVYTF GQPRIGNREV GLFMKAQLNQ PVDRYFRVVY CNDIVPRLPY DDKTFLYKHF
GLCLFYDSFY NETKAEDEPD PNPYGLRYKI LGHVIAVWEL VRGLTMGYTH GPDYKEGWFR
ILFRLMGLVI PGLSDHCMTD YVNSVRLGPD NELQMSSL
