IED Industry Enzyme Database

Detail Information for IndEnz0005000714
IED ID IndEnz0005000714
Enzyme Type ID lipase000714
Protein Name Patatin-like phospholipase domain-containing protein 2
EC 3.1.1.3
Adipose triglyceride lipase
Desnutrin
Gene Name Pnpla2 Atgl
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHERANGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVVEERAGEEDQLQPYRKDRILEHLPARLNEALLEACVEPKDLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGDHLPSRLSEQVELRRAQSLPSVPLSCATYSEALPNWVRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPDALRMRAPASPTAADPATPQDPPGLPPC
Enzyme Length 486
Uniprot Accession Number Q8BJ56
Absorption
Active Site ACT_SITE 47; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 166; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Activity Regulation ACTIVITY REGULATION: Stimulated by PKA-dependent PLIN phosphorylation. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:17114792}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol + H2O = a 1,2-diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:44864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:49172, ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44865; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol + H2O = a 2,3-diacyl-sn-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:38499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64615, ChEBI:CHEBI:75524; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38500; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol + H2O = 1,3-diacyl-sn-glycerol + a fatty acid + H(+); Xref=Rhea:RHEA:43732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64615, ChEBI:CHEBI:77272; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43733; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1,3-di-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75735; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z)-hexadecenoylglycerol + H2O = (9Z)-hexadecenoate + 1,3-di-(9Z)-hexadecenoylglycerol + H(+); Xref=Rhea:RHEA:38395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:75841, ChEBI:CHEBI:75849; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38396; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + H2O = (9Z,12Z)-octadecadienoate + 1,3-di-(9Z,12Z)-octadecadienoylglycerol + H(+); Xref=Rhea:RHEA:38403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75844, ChEBI:CHEBI:75850; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38404; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z,12Z,15Z)-octadecatrienoylglycerol + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1,3-di-(9Z,12Z,15Z)-octadecatrienoylglycerol + H(+); Xref=Rhea:RHEA:38411, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387, ChEBI:CHEBI:75845, ChEBI:CHEBI:75852; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38412; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z)-octadecenoyl-2-hexadecanoylglycerol + H2O = 1,3-di-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:38419, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75735, ChEBI:CHEBI:75846; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38420; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38423, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75583, ChEBI:CHEBI:75867; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38424; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38647, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75847, ChEBI:CHEBI:75868; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38648; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z)-hexadecenoylglycerol + H2O = (9Z)-hexadecenoate + 2,3-di-(9Z)-hexadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:75841, ChEBI:CHEBI:75853; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38400; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + H2O = (9Z,12Z)-octadecadienoate + 2,3-di-(9Z,12Z)-octadecadienoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75844, ChEBI:CHEBI:75854; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38408; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z,12Z,15Z)-octadecatrienoylglycerol + H2O = (9Z,12Z,15Z)-octadecatrienoate + 2,3-di-(9Z,12Z,15Z)-octadecatrienoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38415, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387, ChEBI:CHEBI:75845, ChEBI:CHEBI:75855; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38416; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z)-octadecenoyl-2-hexadecanoylglycerol + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75846, ChEBI:CHEBI:75870; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38432; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:38427, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75824, ChEBI:CHEBI:75847; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38428; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-3-hexadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38643, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75546, ChEBI:CHEBI:75583; Evidence={ECO:0000269|PubMed:23066022};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38644; Evidence={ECO:0000305|PubMed:23066022}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+) = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=a 1,3-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44440, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:47777; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44441; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacylglycerol + a 1-acylglycerol = a triacylglycerol + glycerol; Xref=Rhea:RHEA:44436, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44437; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=2 a 1-acylglycerol = a 1,2-diacylglycerol + glycerol; Xref=Rhea:RHEA:44432, ChEBI:CHEBI:17754, ChEBI:CHEBI:35759, ChEBI:CHEBI:49172; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44433; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol + all-trans-retinol = a diacylglycerol + an all-trans-retinyl ester; Xref=Rhea:RHEA:44676, ChEBI:CHEBI:17336, ChEBI:CHEBI:18035, ChEBI:CHEBI:63410, ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44677; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38331, ChEBI:CHEBI:17754, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38327, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:53753, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=2 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + glycerol; Xref=Rhea:RHEA:38323, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324; Evidence={ECO:0000250|UniProtKB:Q96AD5}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + all-trans-retinol = all-trans-retinyl 9Z-octadecenoate + di-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:39987, ChEBI:CHEBI:17336, ChEBI:CHEBI:53753, ChEBI:CHEBI:70760, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:Q96AD5};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39988; Evidence={ECO:0000250|UniProtKB:Q96AD5};
DNA Binding
EC Number 3.1.1.3
Enzyme Function FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15550674, PubMed:23066022). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone (PubMed:23066022). Also has acylglycerol transacylase activity. Acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion. {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:23066022}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
nucleotide Binding
Features Active site (2); Alternative sequence (3); Chain (1); Domain (1); Frameshift (1); Glycosylation (1); Modified residue (5); Motif (3); Mutagenesis (3); Region (1); Sequence conflict (8); Topological domain (2); Transmembrane (1)
Keywords Alternative splicing;Cell membrane;Glycoprotein;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix
Interact With
Induction INDUCTION: Transiently induced during fasting. cAMP and glucagon may not be involved in the induction during fasting. Induced by dexamethasone. Down-regulated by insulin, isoprotenerol and TNF-alfa. Expression is not affected by glucose and by growth hormone. Expression is reduced in fasted leptin deficient mouse (ob/ob), an obese mouse model. Expression is not affected in fed ob/ob mouse. {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:16009485, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16380488, ECO:0000269|PubMed:16705060}.
Subcellular Location SUBCELLULAR LOCATION: Lipid droplet. Cell membrane; Single-pass type II membrane protein.
Modified Residue MOD_RES 374; /note="Phosphoserine; in vitro"; /evidence="ECO:0000269|PubMed:22733971"; MOD_RES 396; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:22733971"; MOD_RES 406; /note="Phosphoserine; by PKA"; /evidence="ECO:0000269|PubMed:22733971, ECO:0007744|PubMed:21183079"; MOD_RES 430; /note="Phosphoserine; in vitro"; /evidence="ECO:0000269|PubMed:22733971, ECO:0007744|PubMed:21183079"; MOD_RES 468; /note="Phosphoserine; in vitro"; /evidence="ECO:0000269|PubMed:22733971"
Post Translational Modification PTM: Phosphorylation at Ser-406 by PKA is increased during fasting and moderate intensity exercise, and moderately increases lipolytic activity. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:22733971}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 16267052; 17237500; 17245390; 17848638; 18191271; 18337240; 18390901; 18445597; 18572100; 18952573; 19010445; 19026557; 19067489; 19136649; 19190264; 19297333; 19389712; 19491295; 19692632; 19723629; 19965578; 20023287; 20107043; 20164531; 20197052; 20424161; 20842343; 20967758; 21030715; 21106876; 21196579; 21267068; 21464445; 21465509; 21543206; 21641555; 21680814; 21743036; 21757733; 21857651; 21951135; 21969372; 22039468; 22101529; 22158969; 22225876; 22374972; 22383686; 22496349; 22713505; 22993196; 23124680; 23204327; 23220585; 23296636; 23297223; 23349479; 23413028; 23583398; 23704323; 23708736; 23740967; 23835334; 23850519; 23858058; 23867907; 23878361; 23886955; 24002947; 24086110; 24096872; 24196706; 24268737; 24358267; 24440819; 24610891; 24657704; 24801391; 25086775; 25096179; 25176985; 25193997; 25316883; 25351614; 25381252; 25418045; 25422441; 25535287; 25662011; 25700221; 25732851; 25783895; 25814662; 25852007; 25879679; 25953897; 26109679; 26143381; 26196542; 26220403; 26236747; 26260790; 26263173; 26411340; 26427354; 26508640; 26569053; 27050511; 27179362; 27185873; 27185876; 27213586; 27248498; 27357546; 27396333; 27596982; 27677764; 27754788; 27759039; 27851965; 27858140; 27974211; 27986537; 28194887; 28364022; 28380348; 28400046; 28404638; 28459858; 28488768; 28510703; 28726642; 28877455; 28988821; 29232702; 29320510; 29599420; 29692363; 29932770; 30033199; 31185001; 31412256; 31757217; 31806624; 31917686; 32312867; 32376415; 32958928; 33059001; 33097799; 33231284; 33372146; 33376578; 33508319; 33605986; 33732701; 34352257; 34387896; 34489438;
Motif MOTIF 14..19; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 45..49; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 166..168; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 53,657
Kinetics
Metal Binding
Rhea ID RHEA:12044; RHEA:12045; RHEA:44864; RHEA:44865; RHEA:38499; RHEA:38500; RHEA:43732; RHEA:43733; RHEA:38387; RHEA:38388; RHEA:38395; RHEA:38396; RHEA:38403; RHEA:38404; RHEA:38411; RHEA:38412; RHEA:38419; RHEA:38420; RHEA:38423; RHEA:38424; RHEA:38647; RHEA:38648; RHEA:38391; RHEA:38392; RHEA:38399; RHEA:38400; RHEA:38407; RHEA:38408; RHEA:38415; RHEA:38416; RHEA:38431; RHEA:38432; RHEA:38427; RHEA:38428; RHEA:38643; RHEA:38644; RHEA:38379; RHEA:38381; RHEA:44440; RHEA:44441; RHEA:44436; RHEA:44437; RHEA:44432; RHEA:44433; RHEA:44676; RHEA:44677; RHEA:38331; RHEA:38332; RHEA:38327; RHEA:38328; RHEA:38323; RHEA:38324; RHEA:39987; RHEA:39988
Cross Reference Brenda 3.1.1.3;