Detail Information for IndEnz0005000816
IED ID IndEnz0005000816
Enzyme Type ID lipase000816
Protein Name Phospholipase B1, membrane-associated
Phospholipase B
Lysophospholipase
EC 3.1.1.5
Phospholipase A2
EC 3.1.1.4
Phospholipase AdRab-B
Phospholipase B/lipase
PLB/LIP
Triacylglycerol lipase
EC 3.1.1.3
Gene Name PLB1
Organism Oryctolagus cuniculus (Rabbit)
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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit)
Enzyme Sequence MALWPSVFLLGLLPLLGRGADQIQTSSGKNTLEGQLWPESLKTFPFPCDPKTLAESVPSESVHSLRPSDIKFVAAIGNVETAPDSGADDLEEQDGTEKRPEQACMGVVTVLSDIIGRFSPSALMPLCPETRLVPRGGAEDLWMQATELVRSMRENPQLDFEHDWKLINVFFSNTSQCFPCPSAQQKGLVLGGMDKLTRTLDYLQQEVPKAFVNLVDLSELAAFSRWRQGAQLSPAAEPCRCLRETSQLTKVLTQWSYLEAWDSLLASSKYNTQESFAVVFQPFFYESSLSALLAEPPLQDPTTLALSLWNRMMEPIGRKEEPFSEKERKPLRCPTQESPYLFTYRNSGQLTRVSQPQGKLEVREGTEIRCPDKDPSDSVPTSVHRLKPADIKVIGAMGDSLTAGNGAGSQPGNILDVLTQYRGLSWSVGGDQNISTVTTLANILREFNPSLQGFSVGTGRETTSQAFFNQAVAGARADGLIPQAQRLVALMKNDTRINFQEDWKIITVFIGGNDLCDFCNDPVRYSPQNFTDNIGTALDILHAEIPRAFVNLVKVLEISKLRELYQETKVSCPRMILRSLCPCVLKFDDNSTEIASLIETIKEYQERTQQLIDSGRYDTRDDFTVVLQPFFEKVNMPKTQDGLPDNSFFAPDCFHFSSKAHAHAASALWNNMLEPVGQKTTHNDFEGAVNITCPNQVWPFLSTYKNSVQGFGTWLPCRDRSPSASPPTSVHALRPADIQVVAALGDSLTAGIGIGSKPNDLSDGTTQYRGLSYSSGGDGSLDNVTTLPNILRQFNSNLMGFAVGTGDASGTNAFFNQAVPGAKARDLMSQVQTLVQRMKDDHRVNFQEDWKVITVQIGASDLCDYCTDSNLYSAANFYDHLRDALDALHREVPRALVNLVDFMNPSVTRQVFLGNPDKCPVQQASALCNCVLSPRENSYELARLEALAQAYQSSLRELVESGRYDTREDFSVVLQPFFHSIQLPVLQDGRLDTSFFAPDCVHPNQKFHSQLSRALWRNMLEPLGGKTDALDLTAAITLTCPTQNEPFLRTFRNSDYTYPSRPAVENWGSDFLCTAWNASRGVPNSVHELQPGDIKVVAALGDSLTLAMGARPSNSSDPPMFWRGLSWSIGGDGALETHTTLPNILKKFNPSILGFSTGTLEGTMGLNVAVQGARAQDMPAQARDLVERMRNSPEIDLEKDWKLVTLFVGGNDLCHFCENPEGSSEGEYVQHIQQALDVLYEELPRTFVNVVEVMELAGLHQDQGGRCATLLAAQSHCTCFKYSQSSVEMQELKKVNWNLQSGLSRLSYSHQYVQREDFAVVVQPFFQNTLVPLNGRGDTDLTFFSDDCFHFSERGHAEMAIALWNNMLEPVGHKTTSNNFTYSRTKLKCPSPDSPYLYTLRNSRLLPDQAEADPTVLYWAVPVAAGAGLLIGILAMVAGRGMRCRPREDPPLSLSTGL
Enzyme Length 1458
Uniprot Accession Number Q05017
Absorption
Active Site ACT_SITE 400; /evidence=ECO:0000250|UniProtKB:O54728; ACT_SITE 514; /evidence=ECO:0000250|UniProtKB:O54728; ACT_SITE 655; /evidence=ECO:0000250|UniProtKB:O54728
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:O54728}; 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:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H(+); Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623, ChEBI:CHEBI:77624; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:40967, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52323, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40968; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:O54728};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75937; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000305|PubMed:8509424}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:8509424};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000305|PubMed:8509424};
DNA Binding
EC Number 3.1.1.5; 3.1.1.4; 3.1.1.3
Enzyme Function FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (PubMed:8509424). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward glycerolipid substrates (PubMed:8509424). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (PubMed:8509424). May also hydrolyze long chain retinyl esters such as retinyl palmitate (Probable). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable). {ECO:0000269|PubMed:8509424, ECO:0000305|PubMed:8509424}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Glycosylation (10); Region (2); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Glycoprotein;Hydrolase;Lipid metabolism;Membrane;Phospholipid metabolism;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. {ECO:0000250|UniProtKB:O54728}.
Modified Residue
Post Translational Modification PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000250|UniProtKB:O54728}.
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 161,344
Kinetics
Metal Binding
Rhea ID RHEA:15801; RHEA:15802; RHEA:15177; RHEA:15178; RHEA:12044; RHEA:12045; RHEA:41223; RHEA:41224; RHEA:38779; RHEA:38780; RHEA:40923; RHEA:40924; RHEA:40811; RHEA:40812; RHEA:40971; RHEA:40972; RHEA:40911; RHEA:40912; RHEA:40919; RHEA:40920; RHEA:40975; RHEA:40976; RHEA:40915; RHEA:40916; RHEA:40435; RHEA:40436; RHEA:38575; RHEA:38576; RHEA:41111; RHEA:41112; RHEA:40983; RHEA:40984; RHEA:40979; RHEA:40980; RHEA:41103; RHEA:41104; RHEA:41107; RHEA:41108; RHEA:40927; RHEA:40928; RHEA:40967; RHEA:40968; RHEA:42604; RHEA:42605; RHEA:39939; RHEA:39940; RHEA:38487; RHEA:38488; RHEA:38491; RHEA:38492
Cross Reference Brenda