PLB1_RAT
ID PLB1_RAT Reviewed; 1450 AA.
AC O54728;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phospholipase B1, membrane-associated;
DE Short=Phospholipase B;
DE AltName: Full=Lysophospholipase;
DE EC=3.1.1.5 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE AltName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE AltName: Full=Phospholipase B/lipase;
DE Short=PLB/LIP;
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
DE Flags: Precursor;
GN Name=Plb1; Synonyms=Phlpb;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PROTEOLYTIC PROCESSING, DOMAIN, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Ileal mucosa;
RX PubMed=9442065; DOI=10.1074/jbc.273.4.2222;
RA Takemori H., Zolotaryov F.N., Ting L., Urbain T., Komatsubara T.,
RA Hatano O., Okamoto M., Tojo H.;
RT "Identification of functional domains of rat intestinal phospholipase
RT B/lipase. Its cDNA cloning, expression, and tissue distribution.";
RL J. Biol. Chem. 273:2222-2231(1998).
RN [2]
RP PROTEIN SEQUENCE OF 368-380 AND 529-559, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9442064; DOI=10.1074/jbc.273.4.2214;
RA Tojo H., Ichida T., Okamoto M.;
RT "Purification and characterization of a catalytic domain of rat intestinal
RT phospholipase B/lipase associated with brush border membranes.";
RL J. Biol. Chem. 273:2214-2221(1998).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=1716922; DOI=10.1139/o91-054;
RA Pind S., Kuksis A.;
RT "Further characterization of a novel phospholipase B (phospholipase A2-
RT lysophospholipase) from intestinal brush-border membranes.";
RL Biochem. Cell Biol. 69:346-357(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF SER-404;
RP SER-414; SER-429; SER-459; ASP-518; HIS-659; HIS-665 AND HIS-686.
RX PubMed=11401559; DOI=10.1021/bi010237n;
RA Lu T., Ito M., Tchoua U., Takemori H., Okamoto M., Tojo H.;
RT "Identification of essential residues for catalysis of rat intestinal
RT phospholipase B/lipase.";
RL Biochemistry 40:7133-7139(2001).
CC -!- FUNCTION: Calcium-independent membrane-associated phospholipase that
CC catalyzes complete diacylation of phospholipids by hydrolyzing both sn-
CC 1 and sn-2 fatty acyl chains attached to the glycerol backbone
CC (phospholipase B activity) (By similarity). Has dual phospholipase and
CC lysophospholipase activities toward diacylphospholipids
CC (PubMed:9442065, PubMed:9442064, PubMed:11401559). Preferentially
CC cleaves sn-2 ester bonds over sn-1 bonds (PubMed:9442064). Acts as a
CC lipase toward glycerolipid substrates (PubMed:9442065, PubMed:9442064,
CC PubMed:11401559). Hydrolyzes fatty acyl chains of diacylglycerols with
CC preference for the sn-2 position and of triacylglycerols with not
CC positional selectivity (PubMed:9442065, PubMed:9442064,
CC PubMed:11401559). May also hydrolyze long chain retinyl esters such as
CC retinyl palmitate (By similarity). May contribute to digestion of
CC dietary phospholipids, glycerolipids and retinoids, facilitating lipid
CC absorption at the brush border (Probable).
CC {ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:11401559,
CC ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065,
CC ECO:0000305|PubMed:9442064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
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:11401559, ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:11401559,
CC ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2
CC H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112,
CC ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:11401559, ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:11401559, ECO:0000305|PubMed:9442064,
CC ECO:0000305|PubMed:9442065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-
CC octadecenoate + 1,3-dihexadecanoylglycerol + H(+);
CC Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)glycerol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-
CC glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623,
CC ChEBI:CHEBI:77624; Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O =
CC (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938;
CC Evidence={ECO:0000269|PubMed:9442064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605;
CC Evidence={ECO:0000305|PubMed:9442064};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
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:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- ACTIVITY REGULATION: Up-regulated by bile acids such as deoxycholate
CC (PubMed:9442065, PubMed:9442064). Inhibited by diisopropyl
CC fluorophosphate (PubMed:9442065, PubMed:9442064).
CC {ECO:0000269|PubMed:9442064, ECO:0000269|PubMed:9442065}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:9442064};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9442064,
CC ECO:0000269|PubMed:9442065}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Present in the intestinal brush border membranes.
CC -!- TISSUE SPECIFICITY: Expressed in the ileum mucosa, Paneth cells
CC spermatocytes, spermatids and sperm (at protein level). Expressed in
CC the ileum, jejunum, esophagus and testis. {ECO:0000269|PubMed:1716922,
CC ECO:0000269|PubMed:9442065}.
CC -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC {ECO:0000269|PubMed:9442065}.
CC -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC {ECO:0000269|PubMed:9442065}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Phospholipase B1 subfamily. {ECO:0000305}.
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DR EMBL; D63648; BAA23813.1; -; mRNA.
DR RefSeq; NP_620253.1; NM_138898.1.
DR AlphaFoldDB; O54728; -.
DR STRING; 10116.ENSRNOP00000057888; -.
DR SwissLipids; SLP:000000624; -.
DR CarbonylDB; O54728; -.
DR GlyGen; O54728; 14 sites.
DR iPTMnet; O54728; -.
DR PhosphoSitePlus; O54728; -.
DR PaxDb; O54728; -.
DR PRIDE; O54728; -.
DR Ensembl; ENSRNOT00000061176; ENSRNOP00000057888; ENSRNOG00000026037.
DR GeneID; 192259; -.
DR KEGG; rno:192259; -.
DR CTD; 151056; -.
DR RGD; 621565; Plb1.
DR eggNOG; KOG3670; Eukaryota.
DR GeneTree; ENSGT00530000063883; -.
DR InParanoid; O54728; -.
DR OrthoDB; 1232962at2759; -.
DR PhylomeDB; O54728; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:O54728; -.
DR Proteomes; UP000002494; Chromosome 6.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:RGD.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IDA:RGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:RGD.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
DR CDD; cd01824; Phospholipase_B_like; 4.
DR Gene3D; 3.40.50.1110; -; 3.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR035547; Phospholipase_B.
DR InterPro; IPR038885; PLB1.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR21325; PTHR21325; 3.
DR Pfam; PF00657; Lipase_GDSL; 3.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Lipid metabolism; Membrane; Phospholipid metabolism;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1450
FT /note="Phospholipase B1, membrane-associated"
FT /id="PRO_0000324386"
FT TOPO_DOM 28..1422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1423..1443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1444..1450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 41..351
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 366..711
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 712..1058
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 1068..1407
FT /note="4"
FT /evidence="ECO:0000255"
FT REGION 41..1407
FT /note="4 X 308-326 AA approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 708..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1450
FT /note="Necessary for membrane localization"
FT /evidence="ECO:0000269|PubMed:9442065"
FT ACT_SITE 404
FT /evidence="ECO:0000305|PubMed:11401559"
FT ACT_SITE 518
FT /evidence="ECO:0000305|PubMed:11401559"
FT ACT_SITE 659
FT /evidence="ECO:0000305|PubMed:11401559"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 880
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 404
FT /note="S->A,C: Loss of PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 414
FT /note="S->A: No effect on lysophospholipase to PLA2
FT activity ratio."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 429
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 459
FT /note="S->A: Decrease in PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 518
FT /note="D->A,V: Loss of PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 518
FT /note="D->E,N: Impairs PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 659
FT /note="H->A: Loss of PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 665
FT /note="H->A: Impairs PLA2, lysophospholipase and lipase
FT activities."
FT /evidence="ECO:0000269|PubMed:11401559"
FT MUTAGEN 686
FT /note="H->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11401559"
SQ SEQUENCE 1450 AA; 161089 MW; 4555898C8FD91F45 CRC64;
MESWPGVSLV GLLLLLLLGQ GPSQIHGSSG ENTSQPQQVF RTLKNFSFPC KPKKLELSVL
SKSVHSLRPS DIKLVAAIGN LETPPAPGSG VVNMEKPQSL ESELQNVCIG IMTALSDIIR
HFNPSVLMPT CSPGKGTAGH TTIAEDLWIQ AKELVRHLKD NPELDFEKDW KLITVLFSNT
SQCHLCSSDQ QKRHLMKHME MLSGVLDYLH REVPRAFVNL VDLSEVLTMA QQHQETGFSP
APEICKCSEE ITKLSKAVMQ WSYQEAWEDL LASSKFNKHE TFAVVFQSFF SEVELPLERP
SPQDSTTLAL RIWNSMMEPV GRKDGTLNEA ERKTMKCPSQ ESPYLFTYRN SNYQARQLKP
IGKFQMKEGT KFTCPDKDPS DSIPTTVHRL RPADIKVIGA MGDSLTAGNG AGSSPGNVLD
VLTQYRGLSW SVGGDETIET VTTLANILRE FNPSLKGFSV GTGKENTPRA SFNQAVAGAK
SDGLAAQAKK LVSLMKDDKT INFQEDWKII TVFIGGNDLC GSCNNLARFS PQTFTDNIKT
ALDILHAEVP RAFVNMVSVI EITPLRELFN EPKVSCPRMI LRSLCPCVLN LGENSAELAQ
LVERNRQYQE ETGKLIESGR YDTRDDFTVV LQPMFENVVM PRTLEGLPDS SFFAPDCFHF
NVKTHARSAI ALWKNMLEPV GRKTRHQNFE IKVPIMCPNQ TSPFLSTTKN SNLGHGTSMS
CEEKAPSASP PTSVHTLRPA DIQVVAALGD SVTAGNGISS QEGDLADVTT QYRGLSYSAG
GDKFLENVTT LPNILREFNG NLTGYSVGTG DVNSASAFLN QAVPGAKAEN LASQVQTLIQ
KMKNDTRVNF HQDWKVITVM IGASDLCDFC KDSNRYSAAN FSDHLRNALD ILHKEVPRAL
VNLVDFMNPS IIRQVFLKNP DKCPVNQTSV LCNCVLTPGE DSHELARLEA FTKSYQSSML
QLVESGRYDT REDFSVVLQP FLFNIRLPIL ENGNPDTSFF APDCILLSQK FHTQLARALW
ANMLEPLGKK MDTLDPKELI ALACPTKDKP FLRTFRNSNY TYPIKPAIEN WGSDFLCTEQ
SPSSKVPTSV HELRPSDIKV VAAMGDFLTT ATGARPSESS SLDTPWRGLS WSIGGDGTLE
THTTLPNILK KFNPSILGFS TGTLENTAGL NVAEEGARAQ DMPAQAQALV KKMKSTPTIN
IQEDWKLITL LIGNNDLCLY CEDPENYSTR EYVKYIQHAL DIFYEELPRV FINVVEVMEL
SGLLHDQGGK CAMPLAVQKN CSCLKRSQNL MAMQELKKVN GNLQSALSEL SYWHRYMQRE
DFAVTVQPFF RNTFVPLDER GGLDLTFFSE DCFHFSVRGH AEMAIALWNN MLEPVGKKTT
SNNFTYNRTK LKCPSPENPF LYTVRNSQIL LDKAKENSNT LYWAVPVAAV GGLVVGILGM
MLWRTVRLVQ
