OBL1_RICCO
ID OBL1_RICCO Reviewed; 526 AA.
AC Q5VKJ7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Triacylglycerol lipase OBL1 {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000269|PubMed:15322116};
DE AltName: Full=Oil body lipase 1 {ECO:0000303|PubMed:15322116};
DE Short=RcOBL1 {ECO:0000303|PubMed:15322116};
DE AltName: Full=Triacylglycerol acidic lipase OBL1 {ECO:0000303|PubMed:15322116};
GN Name=OBL1 {ECO:0000303|PubMed:15322116};
GN ORFNames=RCOM_1098580 {ECO:0000312|EMBL:EEF28563.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15322116; DOI=10.1074/jbc.m408686200;
RA Eastmond P.J.;
RT "Cloning and characterization of the acid lipase from castor beans.";
RL J. Biol. Chem. 279:45540-45545(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Venegas-Caleron M., Garces R., Martinez-Force E.;
RT "Characterization of triacylglycerol acidic lipases expressed during castor
RT (Ricinus communis L.) seed germination.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- FUNCTION: Acid lipase that can hydrolyze a range of triacylglycerols
CC but is not active on phospholipids (PubMed:15322116). In vitro,
CC hydrolyzes triolein, trilinolein, triricinolein, tripalmitin, trilaurin
CC and tricaprin (PubMed:15322116). May play a role in the regulation of
CC lipolysis in germinating seeds (PubMed:15322116).
CC {ECO:0000269|PubMed:15322116}.
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:15322116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000269|PubMed:15322116};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-4.5. {ECO:0000269|PubMed:15322116};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Note=Associates with the oil body membrane in
CC seed endosperm. {ECO:0000269|PubMed:15322116}.
CC -!- DEVELOPMENTAL STAGE: Expressed in dry seeds and germinating seeds until
CC 4 days after soaking (at protein level). {ECO:0000269|PubMed:15322116}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AY360220; AAR15173.1; -; mRNA.
DR EMBL; JQ945176; AFQ93680.1; -; mRNA.
DR EMBL; EQ974603; EEF28563.1; -; Genomic_DNA.
DR RefSeq; NP_001310695.1; NM_001323766.1.
DR AlphaFoldDB; Q5VKJ7; -.
DR SMR; Q5VKJ7; -.
DR ESTHER; ricco-q5vkj7; Triacylglycerol-lipase-OBL1-like.
DR PRIDE; Q5VKJ7; -.
DR GeneID; 8284735; -.
DR KEGG; rcu:8284735; -.
DR eggNOG; KOG4569; Eukaryota.
DR InParanoid; Q5VKJ7; -.
DR OrthoDB; 772353at2759; -.
DR BRENDA; 3.1.1.3; 1204.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
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 metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Triacylglycerol lipase OBL1"
FT /id="PRO_0000450284"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 338..342
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:F4JFU8"
FT ACT_SITE 340
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:F4JFU8"
FT ACT_SITE 404
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
FT ACT_SITE 497
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q948R1"
SQ SEQUENCE 526 AA; 59627 MW; 31F02B1A7085460E CRC64;
MDDAGKITST SHLIVSPDEG TFLDLFKHIV LSDLGSGAKF FRASDQRVPA TAAYYSRWPV
SVFICKILQL FQMPAAMLGH LTDFLLNFYY QNHGFLGILR NIFLIRLKIP KRGEADFIST
IGYLDSRMDL HGTPMVSHQA DEVISNADNP SLKEGHNSKI KGALGNRSLM DLCIMASKLA
YENTKVVERV VAEHWKMHFV ADYGGMNYFQ DARNTHAFIF CDKPKDANLI VISFRGTGPF
SIPNWCTDFD FSLVGLGDAG SVHVGFLEAM GLGHRNSISS FETSINTKSP GSITELRKES
EMAPDHLVWA YDGVYFLAAS TLKGLLKDHK NAKFVVTGHS LGGALAILFT CILEIQQETE
VLDRLLNVYT FGQPRIGNYN LGYFMQNRLN FPERRYFRVV YCNDMVPRVP FDDVFFTFEH
FGTCIYYDSR FFGYFTKEEP SRNPFGIENA ISAHITAWWE LWRSFILNHV YGAEYKETWE
SRMFRILGLF LPGVAAHSPV NYVNSVRLGR ELAIPLMSLK MMAQGY
