PAG15_HUMAN
ID PAG15_HUMAN Reviewed; 412 AA.
AC Q8NCC3; B3KMF3; B4DUD1; Q53GZ1; Q9NPQ6; Q9UG04; Q9Y2B3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phospholipase A2 group XV;
DE AltName: Full=1-O-acylceramide synthase {ECO:0000303|PubMed:11790796};
DE Short=ACS;
DE AltName: Full=LCAT-like lysophospholipase {ECO:0000303|PubMed:10092508};
DE Short=LLPL {ECO:0000303|PubMed:10092508};
DE EC=3.1.1.5 {ECO:0000269|PubMed:10092508};
DE AltName: Full=Lysophospholipase 3;
DE AltName: Full=Lysosomal phospholipase A and acyltransferase;
DE EC=2.3.1.- {ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020, ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q8VEB4};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q8VEB4};
DE AltName: Full=Lysosomal phospholipase A2 {ECO:0000303|PubMed:11790796, ECO:0000303|PubMed:23958596};
DE Short=LPLA2 {ECO:0000303|PubMed:11790796, ECO:0000303|PubMed:23958596};
DE Flags: Precursor;
GN Name=PLA2G15 {ECO:0000312|HGNC:HGNC:17163}; Synonyms=LYPLA3;
GN ORFNames=UNQ341/PRO540;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 34-43,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Heart, and Kidney;
RX PubMed=10092508; DOI=10.1006/bbrc.1999.0411;
RA Taniyama Y., Shibata S., Kita S., Horikoshi K., Shirafuji H., Sumino Y.,
RA Fujino M.;
RT "Cloning and expression of a novel lysophospholipase which structurally
RT resembles lecithin cholesterol acyltransferase.";
RL Biochem. Biophys. Res. Commun. 257:50-56(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [9]
RP PROTEIN SEQUENCE OF 34-48.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-412 (ISOFORM 1).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP GLYCOSYLATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11790796; DOI=10.1074/jbc.m111977200;
RA Hiraoka M., Abe A., Shayman J.A.;
RT "Cloning and characterization of a lysosomal phospholipase A2, 1-O-
RT acylceramide synthase.";
RL J. Biol. Chem. 277:10090-10099(2002).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20410020; DOI=10.1194/jlr.d007146;
RA Abe A., Kelly R., Shayman J.A.;
RT "The measurement of lysosomal phospholipase A2 activity in plasma.";
RL J. Lipid Res. 51:2464-2470(2010).
RN [13]
RP GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASN-99; ASN-273; ASN-289 AND ASN-398.
RX PubMed=23958596; DOI=10.1194/jlr.m041640;
RA Hiraoka M., Okamoto K., Ohguro H., Abe A.;
RT "Role of N-glycosylation of human lysosomal phospholipase A2 for the
RT formation of catalytically active enzyme.";
RL J. Lipid Res. 54:3098-3105(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-46.
RX PubMed=29724779; DOI=10.1194/jlr.m084012;
RA Hinkovska-Galcheva V., Kelly R., Manthei K.A., Bouley R., Yuan W.,
RA Schwendeman A., Tesmer J.J.G., Shayman J.A.;
RT "Determinants of pH profile and acyl chain selectivity in lysosomal
RT phospholipase A2.";
RL J. Lipid Res. 59:1205-1218(2018).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 34-412 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION,
RP DISULFIDE BOND, MUTAGENESIS OF ASP-46; LEU-83; VAL-85; SER-198; LYS-235 AND
RP THR-362, AND GLYCOSYLATION AT ASN-99; ASN-273; ASN-289 AND ASN-398.
RX PubMed=25727495; DOI=10.1038/ncomms7250;
RA Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A.,
RA Tesmer J.J.;
RT "Structure and function of lysosomal phospholipase A2 and
RT lecithin:cholesterol acyltransferase.";
RL Nat. Commun. 6:6250-6250(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-412 IN COMPLEX WITH ZINC IONS,
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=30830753; DOI=10.1021/acs.biochem.8b01124;
RA Bouley R.A., Hinkovska-Galcheva V., Shayman J.A., Tesmer J.J.G.;
RT "Structural Basis of Lysosomal Phospholipase A2 Inhibition by Zn2.";
RL Biochemistry 58:1709-1717(2019).
CC -!- FUNCTION: Has dual calcium-independent phospholipase and O-
CC acyltransferase activities with a potential role in glycerophospholipid
CC homeostasis and remodeling of acyl groups of lipophilic alcohols
CC present in acidic cellular compartments (PubMed:10092508,
CC PubMed:11790796, PubMed:20410020, PubMed:23958596, PubMed:29724779,
CC PubMed:25727495). Catalyzes hydrolysis of the ester bond of the fatty
CC acyl group attached at sn-1 or sn-2 position of phospholipids
CC (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group
CC at the first carbon of lipophilic alcohols (O-acyltransferase activity)
CC (PubMed:10092508, PubMed:11790796, PubMed:20410020, PubMed:23958596,
CC PubMed:29724779, PubMed:25727495). Among preferred fatty acyl donors
CC are phosphatidylcholines, phosphatidylethanolamines,
CC phosphatidylglycerols and phosphatidylserines (PubMed:29724779). Favors
CC sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of
CC phosphatidylcholines and phosphatidylethanolamines (By similarity).
CC Among preferred fatty acyl acceptors are natural lipophilic alcohols
CC including short-chain ceramide N-acetyl-sphingosine (C2 ceramide),
CC alkylacylglycerols, monoacylglycerols, and acylethanolamides such as
CC anandamide and oleoylethanolamide (PubMed:29724779). Selectively
CC hydrolyzes the sn-1 fatty acyl group of truncated oxidized
CC phospholipids and may play a role in detoxification of reactive
CC oxidized phospholipids during oxidative stress (PubMed:30830753).
CC Required for normal phospholipid degradation in alveolar macrophages
CC with potential implications in pulmonary surfactant clearance (By
CC similarity). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the
CC lysophosphatidylcholines (PubMed:10092508).
CC {ECO:0000250|UniProtKB:Q8VEB4, ECO:0000269|PubMed:10092508,
CC ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020,
CC ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495,
CC ECO:0000269|PubMed:29724779, ECO:0000269|PubMed:30830753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O =
CC 2-glutaroyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:62480, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:77756, ChEBI:CHEBI:145781;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62481;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 2-nonadioyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:62464, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780;
CC Evidence={ECO:0000269|PubMed:30830753};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62465;
CC Evidence={ECO:0000305|PubMed:30830753};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:62484, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77890,
CC ChEBI:CHEBI:145782; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62485;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H2O = 2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:62488, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61042,
CC ChEBI:CHEBI:145783; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62489;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
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:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
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:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
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:10092508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:10092508};
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:10092508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:10092508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:38827, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73007, ChEBI:CHEBI:76077, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38828;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z-
CC octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphoethanolamine; Xref=Rhea:RHEA:38823, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38824;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:38831, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:76077, ChEBI:CHEBI:76090;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38832;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphoethanolamine; Xref=Rhea:RHEA:38835, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73008, ChEBI:CHEBI:76086;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38836;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38843,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:73009, ChEBI:CHEBI:76077,
CC ChEBI:CHEBI:76091; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38844;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38839,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009,
CC ChEBI:CHEBI:76080; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38840;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-
CC enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38759, ChEBI:CHEBI:46979, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071, ChEBI:CHEBI:76077;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38760;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38755, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38756;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:38811, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76077, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38812;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:38807, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:76086;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38808;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:38775, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73003, ChEBI:CHEBI:76077, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38776;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:38771, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003, ChEBI:CHEBI:76080;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38772;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-
CC hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38815,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:74963, ChEBI:CHEBI:76077,
CC ChEBI:CHEBI:76085; Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38816;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-N-(acetyl)-sphing-4-enine +
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38819,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:74963,
CC ChEBI:CHEBI:76087; Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38820;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + N-
CC (acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine +
CC 2-nonadioyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:62472,
CC ChEBI:CHEBI:46979, ChEBI:CHEBI:76077, ChEBI:CHEBI:78207,
CC ChEBI:CHEBI:145780; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62473;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-
CC enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38799, ChEBI:CHEBI:46979, ChEBI:CHEBI:75034,
CC ChEBI:CHEBI:76071, ChEBI:CHEBI:76074;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38800;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38795, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75034, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38796;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-
CC octadecadienoyl)-N-acetylsphing-4-enine + 1-octadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:57108, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:76086, ChEBI:CHEBI:84822;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57109;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-
CC (acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:57120, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74965, ChEBI:CHEBI:76074, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57121;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:57116, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:76080;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57117;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 2-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38767, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76054, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38768;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-N-(acetyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:38763, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74667, ChEBI:CHEBI:76077;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38764;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-
CC 4-enine + 2-octadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38791, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054,
CC ChEBI:CHEBI:76073, ChEBI:CHEBI:76076;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38792;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
CC + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-octadecanoyl-N-(acetyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:38803, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:76073, ChEBI:CHEBI:76074;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38804;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-
CC (acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-
CC enine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:38703, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:11790796, ECO:0000269|PubMed:20410020,
CC ECO:0000269|PubMed:23958596, ECO:0000269|PubMed:25727495,
CC ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38704;
CC Evidence={ECO:0000305|PubMed:11790796, ECO:0000305|PubMed:20410020,
CC ECO:0000305|PubMed:23958596, ECO:0000305|PubMed:25727495,
CC ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-
CC sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:57140, ChEBI:CHEBI:46979, ChEBI:CHEBI:76074,
CC ChEBI:CHEBI:77342, ChEBI:CHEBI:78260;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57141;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-
CC sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphoserine;
CC Xref=Rhea:RHEA:57136, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054,
CC ChEBI:CHEBI:78260, ChEBI:CHEBI:84467;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57137;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-
CC sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:57144, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72845, ChEBI:CHEBI:76074, ChEBI:CHEBI:141490;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57145;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-
CC (acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:57148, ChEBI:CHEBI:46979,
CC ChEBI:CHEBI:72827, ChEBI:CHEBI:72845, ChEBI:CHEBI:76054;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57149;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine + 2-[(5Z,8Z,11Z,14Z)-
CC eicosatetraenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38751,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:74669, ChEBI:CHEBI:76070,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38752;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(9Z-
CC octadecenoyl) ethanolamine = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 2-[(9Z)-octadecenoylamino]ethyl (9Z)-octadecenoate;
CC Xref=Rhea:RHEA:38747, ChEBI:CHEBI:71466, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:76068, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38748;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-(9Z-
CC octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol;
CC Xref=Rhea:RHEA:38743, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735,
CC ChEBI:CHEBI:75938, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38744;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-
CC octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol;
CC Xref=Rhea:RHEA:38739, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735,
CC ChEBI:CHEBI:75757, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38740;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-
CC hexadecanoylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + 1-(9Z)-octadecenoyl-2-hexadecanoylglycerol; Xref=Rhea:RHEA:38735,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:75455, ChEBI:CHEBI:76065,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38736;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-
CC hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol;
CC Xref=Rhea:RHEA:38731, ChEBI:CHEBI:64757, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:75867, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38732;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecyl-2-acetyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-O-hexadecyl-2-acetyl-3-(9Z)-octadecenoyl-sn-
CC glycerol; Xref=Rhea:RHEA:38707, ChEBI:CHEBI:74669, ChEBI:CHEBI:75936,
CC ChEBI:CHEBI:76055, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000269|PubMed:29724779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38708;
CC Evidence={ECO:0000305|PubMed:29724779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC 1-O-hexadecyl-3-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:38711,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:76061, ChEBI:CHEBI:76062,
CC ChEBI:CHEBI:76083; Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38712;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-
CC hexadecyl-2-O-methyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-O-hexadecyl-2-O-methyl-3-(9Z)-octadecenoyl-sn-
CC glycerol; Xref=Rhea:RHEA:38723, ChEBI:CHEBI:74669, ChEBI:CHEBI:76063,
CC ChEBI:CHEBI:76064, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38724;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol;
CC Xref=Rhea:RHEA:38727, ChEBI:CHEBI:74669, ChEBI:CHEBI:75542,
CC ChEBI:CHEBI:75868, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38728;
CC Evidence={ECO:0000250|UniProtKB:Q8VEB4};
CC -!- ACTIVITY REGULATION: Inhibited by zinc ions at neutral pH. Zinc ions in
CC plasma may keep the enzyme from hydrolyzing inappropriate substrates.
CC {ECO:0000269|PubMed:30830753}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-4.5. {ECO:0000269|PubMed:29724779};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:23958596}. Secreted
CC {ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:20410020}. Membrane
CC {ECO:0000269|PubMed:25727495}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25727495}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NCC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NCC3-2; Sequence=VSP_056689, VSP_056690;
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:10092508, PubMed:20410020). Ubiquitous. Highly expressed in
CC heart, placenta, skeletal muscle, kidney and pancreas. Detected at
CC lower levels in spleen, thymus, prostate, testis, ovary, small
CC intestine, colon and peripheral blood leukocytes (PubMed:10092508).
CC {ECO:0000269|PubMed:10092508, ECO:0000269|PubMed:20410020}.
CC -!- PTM: N-glycosylated (PubMed:11790796, PubMed:23958596). N-glycosylation
CC is important for maturation of the enzyme and normal subcellular
CC location (PubMed:23958596). {ECO:0000269|PubMed:11790796,
CC ECO:0000269|PubMed:23958596}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AB017494; BAA76877.1; -; mRNA.
DR EMBL; AY358425; AAQ88791.1; -; mRNA.
DR EMBL; AK001705; BAG50965.1; -; mRNA.
DR EMBL; AK074828; BAC11233.1; -; mRNA.
DR EMBL; AK300596; BAG62293.1; -; mRNA.
DR EMBL; AK222790; BAD96510.1; -; mRNA.
DR EMBL; AL110209; CAB53675.1; ALT_INIT; mRNA.
DR EMBL; AC020978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83217.1; -; Genomic_DNA.
DR EMBL; BC011640; AAH11640.2; -; mRNA.
DR EMBL; BC062605; AAH62605.1; -; mRNA.
DR EMBL; AL389957; CAB97531.1; -; mRNA.
DR CCDS; CCDS10864.1; -. [Q8NCC3-1]
DR PIR; T14755; T14755.
DR RefSeq; NP_036452.1; NM_012320.3. [Q8NCC3-1]
DR PDB; 4X90; X-ray; 1.84 A; A/B/C/D=34-412.
DR PDB; 4X91; X-ray; 2.30 A; A/B/C/D=34-412.
DR PDB; 4X92; X-ray; 3.00 A; A=34-412.
DR PDB; 4X93; X-ray; 2.60 A; A/B=34-412.
DR PDB; 4X94; X-ray; 2.70 A; A=34-412.
DR PDB; 4X95; X-ray; 3.08 A; A/B=34-412.
DR PDB; 4X97; X-ray; 2.65 A; A/B/C/D=34-412.
DR PDB; 6MTW; X-ray; 2.00 A; A/B=34-412.
DR PDBsum; 4X90; -.
DR PDBsum; 4X91; -.
DR PDBsum; 4X92; -.
DR PDBsum; 4X93; -.
DR PDBsum; 4X94; -.
DR PDBsum; 4X95; -.
DR PDBsum; 4X97; -.
DR PDBsum; 6MTW; -.
DR AlphaFoldDB; Q8NCC3; -.
DR SMR; Q8NCC3; -.
DR BioGRID; 117181; 22.
DR IntAct; Q8NCC3; 2.
DR STRING; 9606.ENSP00000219345; -.
DR BindingDB; Q8NCC3; -.
DR ChEMBL; CHEMBL4986; -.
DR SwissLipids; SLP:000001924; -.
DR ESTHER; human-PLA2G15; PC-sterol_acyltransferase.
DR GlyConnect; 1292; 4 N-Linked glycans (2 sites).
DR GlyGen; Q8NCC3; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q8NCC3; -.
DR PhosphoSitePlus; Q8NCC3; -.
DR BioMuta; PLA2G15; -.
DR DMDM; 44888104; -.
DR EPD; Q8NCC3; -.
DR jPOST; Q8NCC3; -.
DR MassIVE; Q8NCC3; -.
DR MaxQB; Q8NCC3; -.
DR PaxDb; Q8NCC3; -.
DR PeptideAtlas; Q8NCC3; -.
DR PRIDE; Q8NCC3; -.
DR ProteomicsDB; 5176; -.
DR ProteomicsDB; 72871; -. [Q8NCC3-1]
DR Antibodypedia; 29747; 106 antibodies from 18 providers.
DR DNASU; 23659; -.
DR Ensembl; ENST00000219345.10; ENSP00000219345.5; ENSG00000103066.13. [Q8NCC3-1]
DR Ensembl; ENST00000413021.2; ENSP00000394197.2; ENSG00000103066.13. [Q8NCC3-2]
DR GeneID; 23659; -.
DR KEGG; hsa:23659; -.
DR MANE-Select; ENST00000219345.10; ENSP00000219345.5; NM_012320.4; NP_036452.1.
DR UCSC; uc002evr.4; human. [Q8NCC3-1]
DR CTD; 23659; -.
DR DisGeNET; 23659; -.
DR GeneCards; PLA2G15; -.
DR HGNC; HGNC:17163; PLA2G15.
DR HPA; ENSG00000103066; Tissue enhanced (skeletal).
DR MIM; 609362; gene.
DR neXtProt; NX_Q8NCC3; -.
DR OpenTargets; ENSG00000103066; -.
DR PharmGKB; PA164724567; -.
DR VEuPathDB; HostDB:ENSG00000103066; -.
DR eggNOG; KOG2369; Eukaryota.
DR GeneTree; ENSGT00940000157499; -.
DR HOGENOM; CLU_075830_0_0_1; -.
DR InParanoid; Q8NCC3; -.
DR OMA; PNENKQF; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; Q8NCC3; -.
DR TreeFam; TF313258; -.
DR BRENDA; 3.1.1.4; 2681.
DR PathwayCommons; Q8NCC3; -.
DR Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR SignaLink; Q8NCC3; -.
DR BioGRID-ORCS; 23659; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; PLA2G15; human.
DR GeneWiki; LYPLA3_(gene); -.
DR GenomeRNAi; 23659; -.
DR Pharos; Q8NCC3; Tbio.
DR PRO; PR:Q8NCC3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NCC3; protein.
DR Bgee; ENSG00000103066; Expressed in gastrocnemius and 134 other tissues.
DR ExpressionAtlas; Q8NCC3; baseline and differential.
DR Genevisible; Q8NCC3; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; TAS:ProtInc.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; TAS:ProtInc.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; ISS:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing;
KW Direct protein sequencing; Disulfide bond; Fatty acid metabolism;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Secreted; Signal; Transferase;
KW Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:10092508,
FT ECO:0000269|PubMed:15340161"
FT CHAIN 34..412
FT /note="Phospholipase A2 group XV"
FT /id="PRO_0000017808"
FT ACT_SITE 198
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X97"
FT ACT_SITE 360
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:25727495"
FT ACT_SITE 392
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:25727495"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25727495,
FT ECO:0007744|PDB:4X97"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30830753"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:25727495,
FT ECO:0007744|PDB:4X95"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30830753"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30830753"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:30830753"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X90, ECO:0007744|PDB:4X91,
FT ECO:0007744|PDB:4X92, ECO:0007744|PDB:4X93,
FT ECO:0007744|PDB:4X94, ECO:0007744|PDB:4X95,
FT ECO:0007744|PDB:4X97"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X90, ECO:0007744|PDB:4X91,
FT ECO:0007744|PDB:4X92, ECO:0007744|PDB:4X93,
FT ECO:0007744|PDB:4X94, ECO:0007744|PDB:4X95,
FT ECO:0007744|PDB:4X97"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X90, ECO:0007744|PDB:4X91,
FT ECO:0007744|PDB:4X92, ECO:0007744|PDB:4X93,
FT ECO:0007744|PDB:4X94, ECO:0007744|PDB:4X95,
FT ECO:0007744|PDB:4X97"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X90, ECO:0007744|PDB:4X91,
FT ECO:0007744|PDB:4X92, ECO:0007744|PDB:4X93,
FT ECO:0007744|PDB:4X94, ECO:0007744|PDB:4X95,
FT ECO:0007744|PDB:4X97"
FT DISULFID 65..89
FT /evidence="ECO:0000269|PubMed:25727495,
FT ECO:0007744|PDB:4X90, ECO:0007744|PDB:4X91,
FT ECO:0007744|PDB:4X92, ECO:0007744|PDB:4X93,
FT ECO:0007744|PDB:4X94, ECO:0007744|PDB:4X95,
FT ECO:0007744|PDB:4X97"
FT VAR_SEQ 43..114
FT /note="VPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNI
FT RLVYNKTSRATQFPDGVDVR -> GWFTTKHPGPPSFLMVWMYVSLALGRPSHWSSWTP
FT AKAAWVPISTPWWRALWAGATHGVRMSEGLPMTGAEP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056689"
FT VAR_SEQ 115..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056690"
FT MUTAGEN 46
FT /note="D->A,C: Decreases membrane binding, phospholipase
FT and transacylase activity at acidic pH."
FT /evidence="ECO:0000269|PubMed:25727495,
FT ECO:0000269|PubMed:29724779"
FT MUTAGEN 46
FT /note="D->F: Has no effect on membrane binding or
FT transacylase activity at acidic pH. Increases membrane
FT binding and transacylase activity at neutral pH by 2-fold
FT and 8-fold, respectively."
FT /evidence="ECO:0000269|PubMed:29724779"
FT MUTAGEN 83
FT /note="L->S: No effect on phospholipase activity. Strongly
FT decreases transacylase activity and association with
FT membranes."
FT /evidence="ECO:0000269|PubMed:25727495"
FT MUTAGEN 85
FT /note="V->S: No effect on phospholipase activity. Strongly
FT decreases transacylase activity and association with
FT membranes."
FT /evidence="ECO:0000269|PubMed:25727495"
FT MUTAGEN 99
FT /note="N->A: Loss of glycosylation site. Leads to retention
FT in the endoplasmic reticulum and nearly abolishes the
FT production of the mature, active enzyme."
FT /evidence="ECO:0000269|PubMed:23958596"
FT MUTAGEN 198
FT /note="S->A: Abolishes phospholipase and transacylase
FT activity. Abolishes association with membranes."
FT /evidence="ECO:0000269|PubMed:25727495"
FT MUTAGEN 235
FT /note="K->A: No effect on phospholipase activity. Abolishes
FT transacylase activity. Has no effect on association with
FT membranes."
FT /evidence="ECO:0000269|PubMed:25727495"
FT MUTAGEN 273
FT /note="N->A: Loss of glycosylation site. Mildly reduces
FT production of the mature, active enzyme."
FT /evidence="ECO:0000269|PubMed:23958596"
FT MUTAGEN 289
FT /note="N->A: Loss of glycosylation site. Mildly reduces
FT production of the mature, active enzyme."
FT /evidence="ECO:0000269|PubMed:23958596"
FT MUTAGEN 362
FT /note="T->A: No effect on phospholipase activity. Strongly
FT decreases transacylase activity and abolishes association
FT with membranes."
FT /evidence="ECO:0000269|PubMed:25727495"
FT MUTAGEN 398
FT /note="N->A: Loss of glycosylation site. Slightly reduces
FT production of the mature, active enzyme."
FT /evidence="ECO:0000269|PubMed:23958596"
FT CONFLICT 94
FT /note="I -> T (in Ref. 4; BAD96510)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Q -> R (in Ref. 3; BAC11233)"
FT /evidence="ECO:0000305"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4X90"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:4X90"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:4X90"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6MTW"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:4X90"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 353..364
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 368..374
FT /evidence="ECO:0007829|PDB:4X90"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:4X90"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:4X90"
FT HELIX 399..410
FT /evidence="ECO:0007829|PDB:4X90"
SQ SEQUENCE 412 AA; 46658 MW; 1FEA8A5783AF050A CRC64;
MGLHLRPYRV GLLPDGLLFL LLLLMLLADP ALPAGRHPPV VLVPGDLGNQ LEAKLDKPTV
VHYLCSKKTE SYFTIWLNLE LLLPVIIDCW IDNIRLVYNK TSRATQFPDG VDVRVPGFGK
TFSLEFLDPS KSSVGSYFHT MVESLVGWGY TRGEDVRGAP YDWRRAPNEN GPYFLALREM
IEEMYQLYGG PVVLVAHSMG NMYTLYFLQR QPQAWKDKYI RAFVSLGAPW GGVAKTLRVL
ASGDNNRIPV IGPLKIREQQ RSAVSTSWLL PYNYTWSPEK VFVQTPTINY TLRDYRKFFQ
DIGFEDGWLM RQDTEGLVEA TMPPGVQLHC LYGTGVPTPD SFYYESFPDR DPKICFGDGD
GTVNLKSALQ CQAWQSRQEH QVLLQELPGS EHIEMLANAT TLAYLKRVLL GP
