PLAT3_HUMAN
ID PLAT3_HUMAN Reviewed; 162 AA.
AC P53816; B2R7Q4; B7XAK5; Q3SYI3; Q9HDD1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Phospholipase A and acyltransferase 3 {ECO:0000312|HGNC:HGNC:17825};
DE EC=2.3.1.- {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852};
DE EC=3.1.1.32 {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616};
DE EC=3.1.1.4 {ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616};
DE AltName: Full=Adipose-specific phospholipase A2 {ECO:0000303|PubMed:22923616};
DE Short=AdPLA {ECO:0000303|PubMed:22923616};
DE AltName: Full=Group XVI phospholipase A1/A2 {ECO:0000312|HGNC:HGNC:17825};
DE AltName: Full=H-rev 107 protein homolog {ECO:0000303|PubMed:9771974};
DE Short=H-REV107 {ECO:0000303|PubMed:9771974};
DE Short=HREV107-1 {ECO:0000303|PubMed:9771974};
DE AltName: Full=HRAS-like suppressor 1;
DE AltName: Full=HRAS-like suppressor 3 {ECO:0000303|PubMed:17374643};
DE Short=HRSL3 {ECO:0000303|PubMed:17374643};
DE AltName: Full=HREV107-3;
DE AltName: Full=Renal carcinoma antigen NY-REN-65 {ECO:0000303|PubMed:10508479};
GN Name=PLAAT3 {ECO:0000312|HGNC:HGNC:17825};
GN Synonyms=HRASLS3 {ECO:0000303|PubMed:22605381},
GN HREV107 {ECO:0000303|PubMed:9771974}, PLA2G16;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9771974; DOI=10.1038/sj.onc.1202060;
RA Husmann K., Sers C., Fietze E., Mincheva A., Lichter P., Schafer R.;
RT "Transcriptional and translational downregulation of H-REV107, a class II
RT tumour suppressor gene located on human chromosome 11q11-12.";
RL Oncogene 17:1305-1312(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kato S.;
RT "Human cDNA encoding H-REV107 protein homolog.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11526504; DOI=10.1038/sj.onc.1204658;
RA Siegrist S., Feral C., Chami M., Solhonne B., Mattei M.G.,
RA Rajpert-De Meyts E., Guellaen G., Bulle F.;
RT "hH-Rev107, a class II tumor suppressor gene, is expressed by post-meiotic
RT testicular germ cells and CIS cells but not by human testicular germ cell
RT tumors.";
RL Oncogene 20:5155-5163(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Testis;
RX PubMed=19615464; DOI=10.1016/j.bbalip.2009.07.001;
RA Uyama T., Jin X.H., Tsuboi K., Tonai T., Ueda N.;
RT "Characterization of the human tumor suppressors TIG3 and HRASLS2 as
RT phospholipid-metabolizing enzymes.";
RL Biochim. Biophys. Acta 1791:1114-1124(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [8]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11973642; DOI=10.1038/sj.onc.1205377;
RA Sers C., Husmann K., Nazarenko I., Reich S., Wiechen K., Zhumabayeva B.,
RA Adhikari P., Schroder K., Gontarewicz A., Schafer R.;
RT "The class II tumour suppressor gene H-REV107-1 is a target of interferon-
RT regulatory factor-1 and is involved in IFNgamma-induced cell death in human
RT ovarian carcinoma cells.";
RL Oncogene 21:2829-2839(2002).
RN [10]
RP INTERACTION WITH PPP2R1A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-23
RP AND CYS-113.
RX PubMed=17374643; DOI=10.1242/jcs.000018;
RA Nazarenko I., Schafer R., Sers C.;
RT "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma
RT cells.";
RL J. Cell Sci. 120:1393-1404(2007).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19047760; DOI=10.1194/jlr.m800453-jlr200;
RA Uyama T., Morishita J., Jin X.H., Okamoto Y., Tsuboi K., Ueda N.;
RT "The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent
RT cytosolic phospholipase A1/2 of the thiol hydrolase type.";
RL J. Lipid Res. 50:685-693(2009).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=19136964; DOI=10.1038/nm.1904;
RA Jaworski K., Ahmadian M., Duncan R.E., Sarkadi-Nagy E., Varady K.A.,
RA Hellerstein M.K., Lee H.Y., Samuel V.T., Shulman G.I., Kim K.H., de Val S.,
RA Kang C., Sul H.S.;
RT "AdPLA ablation increases lipolysis and prevents obesity induced by high-
RT fat feeding or leptin deficiency.";
RL Nat. Med. 15:159-168(2009).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF CYS-113.
RX PubMed=28077878; DOI=10.1038/nature21032;
RA Staring J., von Castelmur E., Blomen V.A., van den Hengel L.G.,
RA Brockmann M., Baggen J., Thibaut H.J., Nieuwenhuis J., Janssen H.,
RA van Kuppeveld F.J., Perrakis A., Carette J.E., Brummelkamp T.R.;
RT "PLA2G16 represents a switch between entry and clearance of
RT Picornaviridae.";
RL Nature 541:412-416(2017).
RN [14]
RP STRUCTURE BY NMR OF 1-125, AND ACTIVE SITE.
RX PubMed=20837014; DOI=10.1016/j.febslet.2010.09.015;
RA Ren X., Lin J., Jin C., Xia B.;
RT "Solution structure of the N-terminal catalytic domain of human H-REV107
RT -- a novel circular permutated NlpC/P60 domain.";
RL FEBS Lett. 584:4222-4226(2010).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22825852; DOI=10.1074/jbc.m112.368712;
RA Uyama T., Ikematsu N., Inoue M., Shinohara N., Jin X.H., Tsuboi K.,
RA Tonai T., Tokumura A., Ueda N.;
RT "Generation of N-acylphosphatidylethanolamine by members of the
RT phospholipase A/acyltransferase (PLA/AT) family.";
RL J. Biol. Chem. 287:31905-31919(2012).
RN [16]
RP REVIEW.
RX PubMed=26503625; DOI=10.1186/s12929-015-0210-7;
RA Mardian E.B., Bradley R.M., Duncan R.E.;
RT "The HRASLS (PLA/AT) subfamily of enzymes.";
RL J. Biomed. Sci. 22:99-99(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 1-132, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=22605381; DOI=10.1074/jbc.m112.361550;
RA Golczak M., Kiser P.D., Sears A.E., Lodowski D.T., Blaner W.S.,
RA Palczewski K.;
RT "Structural basis for the acyltransferase activity of lecithin:retinol
RT acyltransferase-like proteins.";
RL J. Biol. Chem. 287:23790-23807(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-134, FUNCTION, CATALYTIC
RP ACTIVITY, AND ACTIVE SITE.
RX PubMed=22923616; DOI=10.1074/jbc.m112.398859;
RA Pang X.Y., Cao J., Addington L., Lovell S., Battaile K.P., Zhang N.,
RA Rao J.L., Dennis E.A., Moise A.R.;
RT "Structure/Function relationships of adipose phospholipase A2 containing a
RT cys-his-his catalytic triad.";
RL J. Biol. Chem. 287:35260-35274(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-38 AND 59-129, AND MUTAGENESIS
RP OF 39-PRO--LYS-57.
RX PubMed=25383759; DOI=10.1038/nchembio.1687;
RA Golczak M., Sears A.E., Kiser P.D., Palczewski K.;
RT "LRAT-specific domain facilitates vitamin A metabolism by domain swapping
RT in HRASLS3.";
RL Nat. Chem. Biol. 11:26-32(2015).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (PubMed:19615464, PubMed:19047760, PubMed:22825852,
CC PubMed:22605381, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2
CC (PLA2) activity, catalyzing the calcium-independent release of fatty
CC acids from the sn-1 or sn-2 position of glycerophospholipids
CC (PubMed:19615464, PubMed:19047760, PubMed:22825852, PubMed:22605381,
CC PubMed:22923616). For most substrates, PLA1 activity is much higher
CC than PLA2 activity (PubMed:19615464). Shows O-acyltransferase
CC activity,catalyzing the transfer of a fatty acyl group from
CC glycerophospholipid to the hydroxyl group of lysophospholipid
CC (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the
CC calcium-independent transfer of a fatty acyl group at the sn-1 position
CC of phosphatidylcholine (PC) and other glycerophospholipids to the
CC primary amine of phosphatidylethanolamine (PE), forming N-
CC acylphosphatidylethanolamine (NAPE), which serves as precursor for N-
CC acylethanolamines (NAEs) (PubMed:19615464, PubMed:19047760,
CC PubMed:22825852, PubMed:22605381). Exhibits high N-acyltransferase
CC activity and low phospholipase A1/2 activity (PubMed:22825852).
CC Required for complete organelle rupture and degradation that occur
CC during eye lens terminal differentiation, when fiber cells that compose
CC the lens degrade all membrane-bound organelles in order to provide lens
CC with transparency to allow the passage of light. Organelle membrane
CC degradation is probably catalyzed by the phospholipase activity (By
CC similarity). {ECO:0000250|UniProtKB:Q8R3U1,
CC ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464,
CC ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852,
CC ECO:0000269|PubMed:22923616, ECO:0000303|PubMed:26503625}.
CC -!- FUNCTION: (Microbial infection) Acts as a host factor for
CC picornaviruses: required during early infection to promote viral genome
CC release into the cytoplasm (PubMed:28077878). May act as a cellular
CC sensor of membrane damage at sites of virus entry, which relocalizes to
CC sites of membrane rupture upon virus unfection (PubMed:28077878).
CC Facilitates safe passage of the RNA away from LGALS8, enabling viral
CC genome translation by host ribosome (PubMed:28077878). May also be
CC involved in initiating pore formation, increasing pore size or in
CC maintaining pores for genome delivery (PubMed:28077878). The lipid-
CC modifying enzyme activity is required for this process
CC (PubMed:28077878). {ECO:0000269|PubMed:28077878}.
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:19047760, ECO:0000269|PubMed:19615464,
CC ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
CC ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:19615464};
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:0000269|PubMed:19047760, ECO:0000269|PubMed:19615464,
CC ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
CC ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:19615464};
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:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000269|PubMed:19615464};
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:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000269|PubMed:19615464};
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:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:45164,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:76090;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45165;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-
CC acyl-sn-glycero-3-phosphocholine + H(+) + hexanoate;
CC Xref=Rhea:RHEA:53496, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57875, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53497;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexanoyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:53500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:78215, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53501;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53524, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:74667, ChEBI:CHEBI:138218, ChEBI:CHEBI:138220;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53525;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-(9Z-octadecenoyl)-ethanolamine
CC + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53528, ChEBI:CHEBI:15378, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:138218, ChEBI:CHEBI:138222;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53529;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + 2-heptanoyl-
CC sn-glycero-3-phosphocholine = 1-hexanoyl-2-heptanoyl-sn-glycero-3-
CC phosphocholine + hexanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:54544, ChEBI:CHEBI:138197, ChEBI:CHEBI:138216,
CC ChEBI:CHEBI:138266, ChEBI:CHEBI:138267;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54545;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:56432, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73000; Evidence={ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56433;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 2-octadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:56436, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73000,
CC ChEBI:CHEBI:76076; Evidence={ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56437;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:56440, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75026; Evidence={ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56441;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:56444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75026,
CC ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56445;
CC Evidence={ECO:0000269|PubMed:22923616};
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:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000269|PubMed:22923616};
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:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:56448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76071;
CC Evidence={ECO:0000269|PubMed:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:19047760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000269|PubMed:19047760};
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:22923616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000269|PubMed:22923616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-
CC sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000250|UniProtKB:P53817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361;
CC Evidence={ECO:0000250|UniProtKB:P53817};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC H2O = (9Z,12Z)-octadecadienoate + 1-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28733,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:42027;
CC Evidence={ECO:0000250|UniProtKB:Q8R3U1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56429;
CC Evidence={ECO:0000250|UniProtKB:Q8R3U1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for dipalmitoyl-PC {ECO:0000269|PubMed:19615464};
CC Vmax=2.57 umol/min/mg enzyme with dipalmitoyl-PC as substrate
CC {ECO:0000269|PubMed:19615464};
CC Vmax=267 nmol/min/mg enzyme with dipalmitoyl-PE as substrate
CC {ECO:0000269|PubMed:19615464};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:19615464};
CC -!- SUBUNIT: Interacts with PPP2R1A; this interaction might decrease PP2A
CC activity. {ECO:0000269|PubMed:17374643}.
CC -!- INTERACTION:
CC P53816; P30153: PPP2R1A; NbExp=7; IntAct=EBI-746318, EBI-302388;
CC P53816; Q9UMX0: UBQLN1; NbExp=7; IntAct=EBI-746318, EBI-741480;
CC P53816; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-746318, EBI-10173939;
CC P53816; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-746318, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P53817};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:17374643}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8R3U1}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8R3U1}. Peroxisome membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R3U1};
CC Single-pass membrane protein {ECO:0000305}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q8R3U1}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8R3U1}; Single-pass membrane protein
CC {ECO:0000305}. Note=During eye lens differentiation, recruited from the
CC cytosol to various organelles, including mitochondria, endoplasmic
CC reticulum, nuclear envelope and lysosomes, immediately before organelle
CC degradation. This translocation is triggered by organelle membrane
CC damage and requires the C-terminal transmembrane domain.
CC {ECO:0000250|UniProtKB:Q8R3U1}.
CC -!- TISSUE SPECIFICITY: Widely expressed. low expression, if any, in
CC hematopoietic cells and thymus. In testis, confined to round
CC spermatids. Expressed in normal ovarian epithelial cells. Down-
CC regulated in some ovarian carcinomas and testicular germ cell tumors.
CC Highly expressed in white adipose tissue (PubMed:19136964).
CC {ECO:0000269|PubMed:11526504, ECO:0000269|PubMed:11973642,
CC ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:19615464,
CC ECO:0000269|PubMed:9771974}.
CC -!- INDUCTION: By IFNG and IRF1. {ECO:0000269|PubMed:11973642}.
CC -!- DOMAIN: The C-terminal transmembrane domain is required for the
CC targeting of the protein to damaged organelles.
CC {ECO:0000250|UniProtKB:Q8R3U1}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The makings of transparency
CC - Issue 241 of November 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/241/";
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DR EMBL; X92814; CAA63423.1; -; mRNA.
DR EMBL; AB030814; BAB08108.1; -; mRNA.
DR EMBL; AF317086; AAL26892.1; -; mRNA.
DR EMBL; AB439591; BAH08749.1; -; mRNA.
DR EMBL; AK313075; BAG35901.1; -; mRNA.
DR EMBL; CH471076; EAW74158.1; -; Genomic_DNA.
DR EMBL; BC001387; AAH01387.1; -; mRNA.
DR EMBL; BC103807; AAI03808.1; -; mRNA.
DR CCDS; CCDS8047.1; -.
DR RefSeq; NP_001121675.1; NM_001128203.1.
DR RefSeq; NP_009000.2; NM_007069.3.
DR RefSeq; XP_006718489.1; XM_006718426.1.
DR PDB; 2KYT; NMR; -; A=1-125.
DR PDB; 4DOT; X-ray; 1.96 A; A=1-132.
DR PDB; 4FA0; X-ray; 2.65 A; A=1-134.
DR PDB; 4Q95; X-ray; 2.20 A; A/B=2-38, A/B=59-129.
DR PDB; 7C3Z; X-ray; 1.96 A; A=5-125.
DR PDB; 7C41; X-ray; 2.28 A; D=65-74.
DR PDBsum; 2KYT; -.
DR PDBsum; 4DOT; -.
DR PDBsum; 4FA0; -.
DR PDBsum; 4Q95; -.
DR PDBsum; 7C3Z; -.
DR PDBsum; 7C41; -.
DR AlphaFoldDB; P53816; -.
DR BMRB; P53816; -.
DR SMR; P53816; -.
DR BioGRID; 116317; 23.
DR IntAct; P53816; 4.
DR STRING; 9606.ENSP00000320337; -.
DR BindingDB; P53816; -.
DR ChEMBL; CHEMBL3831244; -.
DR SwissLipids; SLP:000001077; -.
DR iPTMnet; P53816; -.
DR PhosphoSitePlus; P53816; -.
DR BioMuta; PLA2G16; -.
DR DMDM; 20141767; -.
DR EPD; P53816; -.
DR jPOST; P53816; -.
DR MassIVE; P53816; -.
DR MaxQB; P53816; -.
DR PaxDb; P53816; -.
DR PeptideAtlas; P53816; -.
DR PRIDE; P53816; -.
DR ProteomicsDB; 56634; -.
DR Antibodypedia; 28982; 342 antibodies from 24 providers.
DR DNASU; 11145; -.
DR Ensembl; ENST00000323646.9; ENSP00000320337.5; ENSG00000176485.13.
DR Ensembl; ENST00000415826.3; ENSP00000389124.1; ENSG00000176485.13.
DR GeneID; 11145; -.
DR KEGG; hsa:11145; -.
DR MANE-Select; ENST00000415826.3; ENSP00000389124.1; NM_001128203.2; NP_001121675.1.
DR UCSC; uc001nxh.4; human.
DR CTD; 11145; -.
DR DisGeNET; 11145; -.
DR GeneCards; PLAAT3; -.
DR HGNC; HGNC:17825; PLAAT3.
DR HPA; ENSG00000176485; Tissue enhanced (adipose tissue, brain).
DR MIM; 613867; gene.
DR neXtProt; NX_P53816; -.
DR OpenTargets; ENSG00000176485; -.
DR VEuPathDB; HostDB:ENSG00000176485; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR GeneTree; ENSGT00940000154853; -.
DR HOGENOM; CLU_109418_0_1_1; -.
DR InParanoid; P53816; -.
DR OMA; VRDAIMV; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; P53816; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:HS11053-MON; -.
DR PathwayCommons; P53816; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR SignaLink; P53816; -.
DR SIGNOR; P53816; -.
DR BioGRID-ORCS; 11145; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; PLA2G16; human.
DR GeneWiki; HRASLS3; -.
DR GenomeRNAi; 11145; -.
DR Pharos; P53816; Tchem.
DR PRO; PR:P53816; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P53816; protein.
DR Bgee; ENSG00000176485; Expressed in C1 segment of cervical spinal cord and 202 other tissues.
DR ExpressionAtlas; P53816; baseline and differential.
DR Genevisible; P53816; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; TAS:Reactome.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
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:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0030397; P:membrane disassembly; ISS:UniProtKB.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR GO; GO:1904177; P:regulation of adipose tissue development; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
DR DisProt; DP02684; -.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Host-virus interaction; Hydrolase; Lipid degradation; Lipid metabolism;
KW Lysosome; Membrane; Mitochondrion; Nucleus; Peroxisome; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..162
FT /note="Phospholipase A and acyltransferase 3"
FT /id="PRO_0000152484"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 13..129
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
FT ECO:0000269|PubMed:22923616"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
FT ECO:0000269|PubMed:22923616"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:20837014, ECO:0000269|PubMed:22605381,
FT ECO:0000269|PubMed:22923616"
FT MUTAGEN 23
FT /note="H->A: No effect on PPP2R1A-binding."
FT /evidence="ECO:0000269|PubMed:17374643"
FT MUTAGEN 39..57
FT /note="PSEVAGAGAASVMSALTDK->DILLALTDDMGRTQKVVSNKRLILGVIVKV:
FT Induces a major structural rearrangement accompanied by
FT domain-swapping dimerization and changes in substrate-
FT specificity."
FT /evidence="ECO:0000269|PubMed:25383759"
FT MUTAGEN 113
FT /note="C->S: No effect on PPP2R1A-binding. Impaired ability
FT to act as a host factor for picornaviruses."
FT /evidence="ECO:0000269|PubMed:17374643,
FT ECO:0000269|PubMed:28077878"
FT CONFLICT 90
FT /note="S -> T (in Ref. 1; CAA63423 and 4; BAH08749)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:7C3Z"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:7C3Z"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:7C3Z"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2KYT"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2KYT"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2KYT"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:7C3Z"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:7C3Z"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:7C3Z"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:7C3Z"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:7C3Z"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:4Q95"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:7C3Z"
SQ SEQUENCE 162 AA; 17937 MW; 3565BFC756A6DA3C CRC64;
MRAPIPEPKP GDLIEIFRPF YRHWAIYVGD GYVVHLAPPS EVAGAGAASV MSALTDKAIV
KKELLYDVAG SDKYQVNNKH DDKYSPLPCS KIIQRAEELV GQEVLYKLTS ENCEHFVNEL
RYGVARSDQV RDVIIAASVA GMGLAAMSLI GVMFSRNKRQ KQ
