ID   PLB1_MOUSE              Reviewed;        1478 AA.
AC   Q3TTY0; Q0VEX7; Q9D4Y6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Phospholipase B1, membrane-associated;
DE            Short=Phospholipase B;
DE   AltName: Full=Lysophospholipase;
DE            EC=3.1.1.5 {ECO:0000250|UniProtKB:O54728};
DE   AltName: Full=Phospholipase A2;
DE            EC=3.1.1.4 {ECO:0000250|UniProtKB:O54728};
DE   AltName: Full=Phospholipase B/lipase;
DE            Short=PLB/LIP;
DE   AltName: Full=Triacylglycerol lipase;
DE            EC=3.1.1.3 {ECO:0000250|UniProtKB:O54728};
DE   Flags: Precursor;
GN   Name=Plb1; Synonyms=Plb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1478 (ISOFORM 3).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Preferentially
CC       cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward
CC       glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains
CC       of diacylglycerols with preference for the sn-2 position and of
CC       triacylglycerols with not positional selectivity (By similarity). May
CC       also hydrolyze long chain retinyl esters such as retinyl palmitate (By
CC       similarity). May contribute to digestion of dietary phospholipids,
CC       glycerolipids and retinoids, facilitating lipid absorption at the brush
CC       border (By similarity). {ECO:0000250|UniProtKB:O54728,
CC       ECO:0000250|UniProtKB:Q05017}.
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
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:0000250|UniProtKB:O54728};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605;
CC         Evidence={ECO:0000250|UniProtKB:O54728};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342, ChEBI:CHEBI:75735;
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   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein
CC       {ECO:0000255}. Note=Present in the intestinal brush border membranes.
CC       {ECO:0000250|UniProtKB:O54728}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3TTY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TTY0-2; Sequence=VSP_032235, VSP_032236;
CC       Name=3;
CC         IsoId=Q3TTY0-3; Sequence=VSP_032237, VSP_032238;
CC       Name=4;
CC         IsoId=Q3TTY0-4; Sequence=VSP_032233, VSP_032234;
CC   -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC       {ECO:0000250|UniProtKB:O54728}.
CC   -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC       {ECO:0000250|UniProtKB:O54728}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       Phospholipase B1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI19078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK015993; BAB30072.1; -; mRNA.
DR   EMBL; AK161095; BAE36193.1; -; mRNA.
DR   EMBL; AC102372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC119077; AAI19078.1; ALT_INIT; mRNA.
DR   CCDS; CCDS39060.1; -. [Q3TTY0-1]
DR   RefSeq; NP_001074876.1; NM_001081407.1. [Q3TTY0-1]
DR   RefSeq; NP_084348.1; NM_030072.1.
DR   RefSeq; XP_006504110.1; XM_006504047.2. [Q3TTY0-1]
DR   AlphaFoldDB; Q3TTY0; -.
DR   BioGRID; 577132; 1.
DR   STRING; 10090.ENSMUSP00000144040; -.
DR   GlyCosmos; Q3TTY0; 14 sites, No reported glycans.
DR   GlyGen; Q3TTY0; 14 sites.
DR   iPTMnet; Q3TTY0; -.
DR   PhosphoSitePlus; Q3TTY0; -.
DR   SwissPalm; Q3TTY0; -.
DR   MaxQB; Q3TTY0; -.
DR   PaxDb; 10090-ENSMUSP00000098928; -.
DR   ProteomicsDB; 289521; -. [Q3TTY0-1]
DR   ProteomicsDB; 289522; -. [Q3TTY0-2]
DR   ProteomicsDB; 289523; -. [Q3TTY0-3]
DR   ProteomicsDB; 289524; -. [Q3TTY0-4]
DR   Antibodypedia; 2675; 153 antibodies from 15 providers.
DR   DNASU; 665270; -.
DR   Ensembl; ENSMUST00000101376.3; ENSMUSP00000098927.3; ENSMUSG00000029134.15. [Q3TTY0-1]
DR   Ensembl; ENSMUST00000202201.4; ENSMUSP00000144401.2; ENSMUSG00000029134.15. [Q3TTY0-2]
DR   Ensembl; ENSMUST00000202220.4; ENSMUSP00000144040.2; ENSMUSG00000029134.15. [Q3TTY0-1]
DR   GeneID; 665270; -.
DR   KEGG; mmu:665270; -.
DR   UCSC; uc008wzk.1; mouse. [Q3TTY0-4]
DR   UCSC; uc008wzl.1; mouse. [Q3TTY0-3]
DR   UCSC; uc008wzm.1; mouse. [Q3TTY0-2]
DR   UCSC; uc008wzn.1; mouse. [Q3TTY0-1]
DR   AGR; MGI:1922406; -.
DR   CTD; 151056; -.
DR   MGI; MGI:1922406; Plb1.
DR   VEuPathDB; HostDB:ENSMUSG00000029134; -.
DR   eggNOG; KOG3670; Eukaryota.
DR   GeneTree; ENSGT00530000063883; -.
DR   InParanoid; Q3TTY0; -.
DR   OMA; FCSDPVH; -.
DR   OrthoDB; 6003at2759; -.
DR   PhylomeDB; Q3TTY0; -.
DR   TreeFam; TF314942; -.
DR   BRENDA; 3.1.1.5; 3474.
DR   Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR   BioGRID-ORCS; 665270; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Pln; mouse.
DR   PRO; PR:Q3TTY0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q3TTY0; Protein.
DR   Bgee; ENSMUSG00000029134; Expressed in spermatid and 75 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISO:MGI.
DR   GO; GO:0004622; F:lysophospholipase activity; ISO:MGI.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; ISO:MGI.
DR   GO; GO:0050253; F:retinyl-palmitate esterase activity; ISO:MGI.
DR   GO; GO:0004806; F:triglyceride lipase activity; ISO:MGI.
DR   GO; GO:0046340; P:diacylglycerol catabolic process; ISO:MGI.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; ISO:MGI.
DR   GO; GO:0046338; P:phosphatidylethanolamine catabolic process; ISO:MGI.
DR   GO; GO:0034478; P:phosphatidylglycerol catabolic process; ISO:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:MGI.
DR   GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
DR   GO; GO:0019433; P:triglyceride catabolic process; ISO:MGI.
DR   CDD; cd01824; Phospholipase_B_like; 4.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 2.
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; PHOSPHOLIPASE B, PLB1; 1.
DR   PANTHER; PTHR21325:SF52; PHOSPHOLIPASE B1, MEMBRANE-ASSOCIATED; 1.
DR   Pfam; PF00657; Lipase_GDSL; 3.
DR   SUPFAM; SSF52266; SGNH hydrolase; 3.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 2.
DR   Genevisible; Q3TTY0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW   Lipid metabolism; Membrane; Phospholipid metabolism; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..1478
FT                   /note="Phospholipase B1, membrane-associated"
FT                   /id="PRO_0000324385"
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..1478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          43..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          43..1407
FT                   /note="4 X 308-326 AA approximate repeats"
FT                   /evidence="ECO:0000255"
FT   REGION          1408..1450
FT                   /note="Necessary for membrane localization"
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   REGION          1451..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   ACT_SITE        518
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   ACT_SITE        659
FT                   /evidence="ECO:0000250|UniProtKB:O54728"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        525
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        715
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        764
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        830
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        1227
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        1289
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   VAR_SEQ         387..394
FT                   /note="VHSLRPAD -> GTWLSCSV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032233"
FT   VAR_SEQ         395..1478
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032234"
FT   VAR_SEQ         778
FT                   /note="S -> R (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032235"
FT   VAR_SEQ         779..1478
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032236"
FT   VAR_SEQ         929
FT                   /note="S -> R (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032237"
FT   VAR_SEQ         930..1478
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032238"
SQ   SEQUENCE   1478 AA;  164541 MW;  B5361AED29BA49E6 CRC64;
     MELYPGVSPV GLLLLLLLGQ GPSQIHGSSG ENTLAWQSQQ VFWTLKNFPF PCKPKKLELS
     VLSESVHSLR PSDIKLVAAI GNPEIPLAPG SGTINMEKPQ SIKNQPQDVC MGIMTVLSDI
     IRHFSPSVLM PTCSPGKGTA VHTTAEDLWI QAKELVRRLK DNPQLDFEKD WKLITVFFSN
     TSQCHLCPSA QQKSHLMRHM EMLWGVLDYL HHEVPRAFVN LVDLSEVLAM DLQHQETGFS
     PAPEVCKCTE TTTLSKAVMQ WSYQEAWEDL LASSKFNKHE TFAVVFQPFF DEIEPPLKRS
     SPQDPTTLAL RIWNSMMEPV GQKDGLLNTA ERKTMKCPSE ESPYLFTYKN SNYQARRLKP
     ITKLQMKEGS EFTCPDKNPS NSIPTTVHSL RPADIKIIGA LGDSLTAGNG AGASPWNILD
     VLTEYRGLSW SVGGDETIKT VTTLPNILRE FNPSLKGFSV GTGKESTSRA SFNQAVAGAK
     SDGLAGQARK LVDLMKADKT INFQEDWKII TVFIGGNDLC ASCSNSTRFS PQNFIDNIKN
     ALDILHAEVP RAFVNMAMVM EITPLRELFN EPTVSCPRNI LSRLCPCVLG LGDNSEELSS
     LVQRNRDYQK KTEELINSGR YDTRDNFTVV VQPLFENVSM PRTPEGVPDK SFFAPDCFHF
     NAKTHARSAI ALWKNMLEPV GHKTRHNNFE IKAPIVCPNQ ASPFLSTTKN SNLGNGTWMV
     CEERAPSASP PTSVHTLRPA DIQVVAALGD SLTAGNGISS QEGNLTDVST QYRGLSYSAG
     GDKTLENVTT LPNILRKFNG NLTGYSVGTG DSSSANAFLN QAVPGAKAEN LTSQVRTLVQ
     KMKSDNRVNF NRDWKVITVM IGASDLCDFC TDSNHYSAAN FFDHLQNALD ILHKEVPRAL
     VNLVDFINPS IIREVFLKNP DKCPVNQSSV LCNCVLTPRK DSYELARLEA FTKSYQSSML
     QLVESGRYDT REDFSVVLQP FLLNTKLPVL ENGKPDTSFF APDCIHLNQK FHTQLARALW
     ANMLEPLGKK TDTLDPKGHI SLACPTKDQP FLRTFRNSNY KYPTKPAIEN WGSDFLCTEK
     SPSSQVPTSV HELRPADIKV VAAMGDFLTT ATGARPSGYK RLATPWRGLS WSIGGDGKLE
     THTTLPNILK KFNPSITGFS TGTLDNKAGL NVAEEGARAQ DMPAQAKTLV KKMKSTPTIN
     LQEDWKLITL LIGNNDLCLY CENPEDNSTK EYVKYIQQAL DILYEELPRV FINVVEVMEL
     AGLHHVQGGK CAMPLAVQKN CSCLRHSQNL TAMQELKKLN WNLQSGISEL SYWHRYMERE
     DFAVTVQPFF RNTFIPLNER EGLDLTFFSE DCFYFSDRGH AEMAIALWNN MLEPVGWKTS
     SNNFIYNRTK LKCPSPERPF LYTLRNSQLL PDKAEEPSNA LYWAVPVAAI GGLAVGILGV
     MLWRTVKPVQ QEEEEEDTLP NTSVTQDAVS EKRLKAGN
//