OBL1_TOBAC
ID OBL1_TOBAC Reviewed; 572 AA.
AC A0A1S3ZP85;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 21.
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=NtOBL1 {ECO:0000303|PubMed:29178188};
GN Name=OBL1 {ECO:0000303|PubMed:29178188};
GN ORFNames=LOC107788962 {ECO:0000312|RefSeq:XP_016466196.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-393.
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 -!- 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 and pollen tubes.
CC {ECO:0000269|PubMed:29178188}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR RefSeq; XP_016466196.1; XM_016610710.1.
DR RefSeq; XP_016466197.1; XM_016610711.1.
DR AlphaFoldDB; A0A1S3ZP85; -.
DR SMR; A0A1S3ZP85; -.
DR ESTHER; tabac-OBL1; Triacylglycerol-lipase-OBL1-like.
DR GeneID; 107788962; -.
DR KEGG; nta:107788962; -.
DR OMA; EYLNAVW; -.
DR OrthoDB; 772353at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; IEA:InterPro.
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; 1.
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..572
FT /note="Triacylglycerol lipase OBL1"
FT /id="PRO_0000450283"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 320..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 391..395
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:F4JFU8"
FT COMPBIAS 320..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:F4JFU8"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT MUTAGEN 393
FT /note="S->A: Reduces pollen tube growth."
FT /evidence="ECO:0000269|PubMed:29178188"
SQ SEQUENCE 572 AA; 65270 MW; 2790651093436630 CRC64;
MASTKIDDKV SIPGPVTGTG NSRFLIVSHE NGGIWDLVRF GVWGNKESGD KFLHYSAGGG
LLEEHLVRSD DSGGGDDRGG EVPDHRWVIF VSIIVRKLIA IFGKPMEWTG YLVEFFLNLF
SLNGNFLGLL YNILHGKVVM PHRGSETFIS AIGHLDGRIN LYKSETLTKE IGEPDFWQKI
GIGHRDLMDL CMMASKLAYE NEKVVRNVVN LHWKMHFVDF YNCWNDFEKE MSTQVFLLCD
KPKDANLILV SFRGTEPFDA DDWITDFDYS WYEIPKLGKV HMGFLEALGL GNRTNASTFH
EQLFVNNLKF ANLENVHATI PPSESSKSST SFSDSDAHTG SDLSSDSERP TDTRKKKFRL
EIPERTAYYV VRSKLKRLLK EHKNAKFVVT GHSLGGALAI LFPAVLVLHE EVDVMERLLG
IYTYGQPRVG NRQLGRFMEA HLEHPVPKYF RVVYCNDLVP RLPYDNKTFL FKHFGICQYY
NSLYIEQNIN EEPNPNYFGM RFLVPLYLNA GWELIRSFTM GYMYGSEYEE CWESVMLRAL
GLFLPGISAH SPVDYVNSIR LGKARSTQMS SF
