DGLB_RAT
ID DGLB_RAT Reviewed; 668 AA.
AC P0C1S9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Diacylglycerol lipase-beta;
DE Short=DAGL-beta;
DE Short=DGL-beta {ECO:0000303|PubMed:16051747};
DE EC=3.1.1.116 {ECO:0000250|UniProtKB:Q8NCG7};
DE AltName: Full=PUFA-specific triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:Q91WC9};
DE AltName: Full=Sn1-specific diacylglycerol lipase beta;
GN Name=Daglb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16051747; DOI=10.1124/mol.105.013961;
RA Jung K.-M., Mangieri R., Stapleton C., Kim J., Fegley D., Wallace M.,
RA Mackie K., Piomelli D.;
RT "Stimulation of endocannabinoid formation in brain slice cultures through
RT activation of group I metabotropic glutamate receptors.";
RL Mol. Pharmacol. 68:1196-1202(2005).
CC -!- FUNCTION: Lipase that catalyzes the hydrolysis of arachidonic acid
CC (AA)-esterified diacylglycerols (DAGs) to produce the principal
CC endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further
CC cleaved by downstream enzymes to release arachidonic acid (AA) for
CC cyclooxygenase (COX)-mediated eicosanoid production. Preferentially
CC hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and
CC has negligible activity against other lipids including
CC monoacylglycerols and phospholipids (By similarity). Plays a key role
CC in the regulation of 2-AG and AA pools utilized by COX1/2 to generate
CC lipid mediators of macrophage and microglia inflammatory responses.
CC Functions also as a polyunsaturated fatty acids-specific
CC triacylglycerol lipase in macrophages. Plays an important role to
CC support the metabolic and signaling demands of macrophages (By
CC similarity). {ECO:0000250|UniProtKB:Q8NCG7,
CC ECO:0000250|UniProtKB:Q91WC9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:33275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:28868; EC=3.1.1.116;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33276;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + H2O = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:52392,
CC ChEBI:CHEBI:75728; Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38508;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycerol + H2O = (9Z)-octadecenoate + 2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38515,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52392, ChEBI:CHEBI:75449;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38516;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-octadecanoylglycerol + H(+); Xref=Rhea:RHEA:38519,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75448, ChEBI:CHEBI:75456;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38520;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-(9Z,12Z-octadecadienoyl)-sn-glycerol +
CC H2O = (9Z)-octadecenoate + 2-(9Z,12Z-octadecadienoyl)-glycerol +
CC H(+); Xref=Rhea:RHEA:38523, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75450, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38524;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-O-(5Z,8Z,11Z,14Z-eicosatetraenyl)-sn-
CC glycerol + H2O = (9Z)-octadecenoate + 2-O-(5Z,8Z,11Z,14Z)-
CC eicosatetraenylglycerol + H(+); Xref=Rhea:RHEA:38527,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75913, ChEBI:CHEBI:75914;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38528;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
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:0000250|UniProtKB:Q91WC9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:Q91WC9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + a di-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-glycerol + H(+); Xref=Rhea:RHEA:63432,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:147308, ChEBI:CHEBI:147309;
CC Evidence={ECO:0000250|UniProtKB:Q91WC9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63433;
CC Evidence={ECO:0000250|UniProtKB:Q91WC9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H2O =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + a di-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:63436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:77016, ChEBI:CHEBI:147310, ChEBI:CHEBI:147311;
CC Evidence={ECO:0000250|UniProtKB:Q91WC9};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8NCG7};
CC -!- ACTIVITY REGULATION: Inhibited by the 1,2,3-triazole urea covalent
CC inhibitors KT109 and KT172 (By similarity). Inhibited by p-hydroxy-
CC mercuri-benzoate and HgCl(2), but not by PMSF. Also inhibited by
CC RHC80267, a drug that blocks 2-AG formation (By similarity).
CC {ECO:0000250|UniProtKB:Q8NCG7, ECO:0000250|UniProtKB:Q91WC9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NCG7};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in corticostriatal and hippocampal
CC slices. Highly expressed in striatal neurons (at protein level).
CC {ECO:0000269|PubMed:16051747}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AABR03083354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03082268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03083835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03083932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03084256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03083962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03083512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C1S9; -.
DR SMR; P0C1S9; -.
DR STRING; 10116.ENSRNOP00000062663; -.
DR ESTHER; rat-dglb; Lipase_3.
DR iPTMnet; P0C1S9; -.
DR PhosphoSitePlus; P0C1S9; -.
DR SwissPalm; P0C1S9; -.
DR jPOST; P0C1S9; -.
DR PaxDb; P0C1S9; -.
DR PRIDE; P0C1S9; -.
DR RGD; 1310193; Daglb.
DR eggNOG; KOG2088; Eukaryota.
DR InParanoid; P0C1S9; -.
DR PhylomeDB; P0C1S9; -.
DR TreeFam; TF312928; -.
DR Reactome; R-RNO-426048; Arachidonate production from DAG.
DR PRO; PR:P0C1S9; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001079; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; P0C1S9; baseline and differential.
DR Genevisible; P0C1S9; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0071926; P:endocannabinoid signaling pathway; IBA:GO_Central.
DR GO; GO:0006690; P:icosanoid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..668
FT /note="Diacylglycerol lipase-beta"
FT /id="PRO_0000248352"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..58
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NCG7"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WC9"
SQ SEQUENCE 668 AA; 73771 MW; B47999973A10E7EF CRC64;
MPGMVLFGRR WSLASDDLVF PGSFELFLRV LWWIASLTLY LMHRRKLDCP GGVLLSTYLI
VLLVLLAVII GIVLAIVCVS MRGTICNPGP RKSMSKLLYI RLALFLPEMV WASLGAAWVA
KGIQCDRTVV IGIIATVIVS WIVIAATMVT IVFVFDPLGG KMAPYPPCIP EHLDSNSSNH
LLTGLRTAAK SVWETRVQCC CCCIGQDDNT RVAFSSTADL FSTYFSDTDL VPSDIAAGFT
LLHQQQDKIS HSREPSEVVT HTPGQPQETE LDAEVENCHH YMPFSPVCSP WPVCVLNSSR
VELCRTGNNF CRGRDIEYDA VEGDEHHCHF ASILKTTGLQ YRDFIHVSFH DKVYELPFIV
VLDHRKESVV VAVRGTMSLQ DVLTDLSAES ENLELDIELQ DCVAHKGIAQ AARYIYRRLV
NDGILSQAFS VAPEYRLVVV GHSLGAGAAA LLAIMLRGAY PQVRAYAFSP PRGLLSKSLF
EYSKDFVVSL ILGMDVIPRL SVANMEDLKR RILRVIANCN KPKYKILLHG CWYSVFGGSP
DNFPTELDEG NQGALTQPLL GEQTLLTRCS PGYCSGDSPL DSPKYPTLYP PGRIIHLEEE
GGSGRFGCCS AAQYRARWAH ETEFSKILIG PKMLIDHMPD VMIRALDRVV ADRTACVSCP
GQGGSNVP
