PLAT3_MOUSE
ID PLAT3_MOUSE Reviewed; 162 AA.
AC Q8R3U1; B7X6T3; Q3V3C3; Q8BWF7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phospholipase A and acyltransferase 3 {ECO:0000250|UniProtKB:P53816};
DE EC=2.3.1.- {ECO:0000269|PubMed:19047760};
DE EC=3.1.1.32 {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920};
DE EC=3.1.1.4 {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920};
DE AltName: Full=Adipose-specific phospholipase A2 {ECO:0000312|MGI:MGI:2179715};
DE Short=AdPLA {ECO:0000303|PubMed:18614531};
DE AltName: Full=Group XVI phospholipase A2 {ECO:0000312|MGI:MGI:2179715};
DE AltName: Full=H-rev 107 protein homolog {ECO:0000250|UniProtKB:P53816};
DE AltName: Full=HRAS-like suppressor 3 {ECO:0000250|UniProtKB:P53816};
DE Short=HRSL3 {ECO:0000250|UniProtKB:P53816};
GN Name=Plaat3 {ECO:0000250|UniProtKB:P53816};
GN Synonyms=H-rev107 {ECO:0000250|UniProtKB:P53816},
GN Hrasls3 {ECO:0000250|UniProtKB:P53816},
GN Hrev107 {ECO:0000250|UniProtKB:P53816},
GN Pla2g16 {ECO:0000312|MGI:MGI:2179715};
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 [MRNA] (ISOFORM 1).
RA Morishita J., Okamoto Y., Jin X.H., Tsuboi K., Ueda N.;
RT "Purification and characterization of LRAT-like protein 3.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Kidney, Spinal cord, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=12055182; DOI=10.1074/jbc.m111891200;
RA Roder K., Latasa M.-J., Sul H.S.;
RT "Silencing of the mouse H-rev107 gene encoding a class II tumor suppressor
RT by CpG methylation.";
RL J. Biol. Chem. 277:30543-30550(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-23; ASN-112; CYS-113
RP AND GLN-129.
RX PubMed=18614531; DOI=10.1074/jbc.m804146200;
RA Duncan R.E., Sarkadi-Nagy E., Jaworski K., Ahmadian M., Sul H.S.;
RT "Identification and functional characterization of adipose-specific
RT phospholipase A2 (AdPLA).";
RL J. Biol. Chem. 283:25428-25436(2008).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Pancreas, and Spleen;
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).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-113.
RX PubMed=22134920; DOI=10.1074/jbc.m111.267575;
RA Uyama T., Ichi I., Kono N., Inoue A., Tsuboi K., Jin X.H., Araki N.,
RA Aoki J., Arai H., Ueda N.;
RT "Regulation of peroxisomal lipid metabolism by catalytic activity of tumor
RT suppressor H-rev107.";
RL J. Biol. Chem. 287:2706-2718(2012).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-113.
RX PubMed=33854238; DOI=10.1038/s41586-021-03439-w;
RA Morishita H., Eguchi T., Tsukamoto S., Sakamaki Y., Takahashi S., Saito C.,
RA Koyama-Honda I., Mizushima N.;
RT "Organelle degradation in the lens by PLAAT phospholipases.";
RL Nature 592:634-638(2021).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (PubMed:19047760). Shows phospholipase A1 (PLA1) and A2
CC (PLA2), catalyzing the calcium-independent release of fatty acids from
CC the sn-1 or sn-2 position of glycerophospholipids (PubMed:18614531,
CC PubMed:19047760, PubMed:19136964, PubMed:22134920). For most
CC substrates, PLA1 activity is much higher than PLA2 activity (By
CC similarity). Shows O-acyltransferase activity, catalyzing the transfer
CC of a fatty acyl group from glycerophospholipid to the hydroxyl group of
CC lysophospholipid (By similarity). Shows N-acyltransferase
CC activity,catalyzing the calcium-independent transfer of a fatty acyl
CC group at the sn-1 position of phosphatidylcholine (PC) and other
CC glycerophospholipids to the primary amine of phosphatidylethanolamine
CC (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as
CC precursor for N-acylethanolamines (NAEs) (PubMed:19047760). Exhibits
CC high N-acyltransferase activity and low phospholipase A1/2 activity (By
CC similarity). Required for complete organelle rupture and degradation
CC that occur during eye lens terminal differentiation, when fiber cells
CC that compose the lens degrade all membrane-bound organelles in order to
CC provide lens with transparency to allow the passage of light
CC (PubMed:33854238). Organelle membrane degradation is probably catalyzed
CC by the phospholipase activity (PubMed:33854238).
CC {ECO:0000250|UniProtKB:P53816, ECO:0000269|PubMed:18614531,
CC ECO:0000269|PubMed:19047760, ECO:0000269|PubMed:19136964,
CC ECO:0000269|PubMed:22134920, ECO:0000269|PubMed:33854238}.
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).
CC {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:18614531, ECO:0000269|PubMed:19047760,
CC ECO:0000269|PubMed:19136964, ECO:0000269|PubMed:22134920};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:18614531};
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:18614531, ECO:0000269|PubMed:19047760,
CC ECO:0000269|PubMed:19136964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:18614531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:18614531};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:18614531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000269|PubMed:18614531};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45165;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53497;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53501;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53525;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53529;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54545;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56433;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56437;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56441;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56445;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:18614531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000269|PubMed:18614531};
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:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000250|UniProtKB:P53816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000250|UniProtKB:P53816};
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:0000269|PubMed:18614531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56429;
CC Evidence={ECO:0000269|PubMed:18614531};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PC)
CC {ECO:0000269|PubMed:18614531};
CC Vmax=7.8 umol/min/mg enzyme with 1-palmitoyl-2-linoleoyl-PC as
CC substrate (in the presence of 2 mM calcium)
CC {ECO:0000269|PubMed:18614531};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:18614531};
CC -!- SUBUNIT: Interacts with PPP2R1A; this interaction might decrease PP2A
CC activity. {ECO:0000250|UniProtKB:P53816}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P53817};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:18614531, ECO:0000269|PubMed:33854238}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:33854238}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18614531}. Peroxisome membrane
CC {ECO:0000269|PubMed:22134920}; Single-pass membrane protein
CC {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:33854238};
CC Single-pass membrane protein {ECO:0000305}. Nucleus envelope
CC {ECO:0000269|PubMed:33854238}. Lysosome membrane
CC {ECO:0000269|PubMed:33854238}; Single-pass membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:33854238}; 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:0000269|PubMed:33854238}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3U1-2; Sequence=VSP_013542;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues but down-
CC regulated in primary carcinomas or in many cell lines derived from
CC tumors (PubMed:12055182). Highly expressed in white adipose tissue and
CC in adipocytes (PubMed:18614531, PubMed:19136964). Expressed at lower
CC levels in brown adipose tissue (PubMed:18614531, PubMed:19136964).
CC {ECO:0000269|PubMed:12055182, ECO:0000269|PubMed:18614531,
CC ECO:0000269|PubMed:19136964}.
CC -!- DOMAIN: The C-terminal transmembrane domain is required for the
CC targeting of the protein to damaged organelles.
CC {ECO:0000269|PubMed:33854238}.
CC -!- DISRUPTION PHENOTYPE: Mice display resistance to diet-induced obesity:
CC they show strongly reduced adipose tissue mass and triglyceride content
CC but normal adipogenesis accompanied by higher energy expenditure and
CC increased fatty acid oxidation in adipocytes (PubMed:19136964). Mice
CC show resistance to infection by picornaviruses, such as coxsackievirus
CC A10, probably due to reduced viral genome release into the host
CC cytoplasm (PubMed:28077878). The eye lens of knockout animals shows no
CC growth defect, but the degradation of mitochondria, the endoplasmic
CC reticulum and lysosomes is almost completely suppressed at postnatal
CC day 0.5 and at 2 months and membranous organelles persisted at this
CC time point (PubMed:33854238). {ECO:0000269|PubMed:19136964,
CC ECO:0000269|PubMed:28077878, ECO:0000269|PubMed:33854238}.
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; AB298806; BAH08635.1; -; mRNA.
DR EMBL; AK039703; BAE20550.1; -; mRNA.
DR EMBL; AK042007; BAE20615.1; -; mRNA.
DR EMBL; AK052657; BAC35085.1; -; mRNA.
DR EMBL; AK163505; BAE37375.1; -; mRNA.
DR EMBL; CH466612; EDL33312.1; -; Genomic_DNA.
DR EMBL; CH466612; EDL33314.1; -; Genomic_DNA.
DR EMBL; BC024581; AAH24581.1; -; mRNA.
DR CCDS; CCDS29528.1; -. [Q8R3U1-1]
DR RefSeq; NP_644675.2; NM_139269.2. [Q8R3U1-1]
DR RefSeq; XP_006526984.1; XM_006526921.2.
DR AlphaFoldDB; Q8R3U1; -.
DR SMR; Q8R3U1; -.
DR STRING; 10090.ENSMUSP00000025925; -.
DR SwissLipids; SLP:000001902; -.
DR iPTMnet; Q8R3U1; -.
DR PhosphoSitePlus; Q8R3U1; -.
DR EPD; Q8R3U1; -.
DR MaxQB; Q8R3U1; -.
DR PaxDb; Q8R3U1; -.
DR PeptideAtlas; Q8R3U1; -.
DR PRIDE; Q8R3U1; -.
DR ProteomicsDB; 287758; -. [Q8R3U1-1]
DR ProteomicsDB; 287759; -. [Q8R3U1-2]
DR Antibodypedia; 28982; 342 antibodies from 24 providers.
DR DNASU; 225845; -.
DR Ensembl; ENSMUST00000025925; ENSMUSP00000025925; ENSMUSG00000060675. [Q8R3U1-1]
DR Ensembl; ENSMUST00000136465; ENSMUSP00000119403; ENSMUSG00000060675. [Q8R3U1-2]
DR Ensembl; ENSMUST00000136756; ENSMUSP00000115151; ENSMUSG00000060675. [Q8R3U1-1]
DR GeneID; 225845; -.
DR KEGG; mmu:225845; -.
DR UCSC; uc008glh.1; mouse. [Q8R3U1-2]
DR UCSC; uc008gli.1; mouse. [Q8R3U1-1]
DR CTD; 11145; -.
DR MGI; MGI:2179715; Plaat3.
DR VEuPathDB; HostDB:ENSMUSG00000060675; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR GeneTree; ENSGT00940000154853; -.
DR HOGENOM; CLU_109418_0_1_1; -.
DR InParanoid; Q8R3U1; -.
DR OMA; VRDAIMV; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q8R3U1; -.
DR TreeFam; TF330836; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR BioGRID-ORCS; 225845; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Plaat3; mouse.
DR PRO; PR:Q8R3U1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R3U1; protein.
DR Bgee; ENSMUSG00000060675; Expressed in white adipose tissue and 237 other tissues.
DR ExpressionAtlas; Q8R3U1; baseline and differential.
DR Genevisible; Q8R3U1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA: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:0016410; F:N-acyltransferase activity; ISS: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:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IMP:UniProtKB.
DR GO; GO:0030397; P:membrane disassembly; IDA:UniProtKB.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:1903008; P:organelle disassembly; IMP:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IMP:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR GO; GO:1904177; P:regulation of adipose tissue development; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:UniProtKB.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; Membrane;
KW Mitochondrion; Nucleus; Peroxisome; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..162
FT /note="Phospholipase A and acyltransferase 3"
FT /id="PRO_0000152485"
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:0000305|PubMed:18614531"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000305|PubMed:18614531, ECO:0000305|PubMed:33854238"
FT VAR_SEQ 131..162
FT /note="RDAVKAVGIAGVGLAALGLVGVMLSRNKKQKQ -> CHRPCTLTLGVRSFSQ
FT LPVAGPECGWRQNYKQDDNSLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013542"
FT MUTAGEN 23
FT /note="H->A,Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18614531,
FT ECO:0000269|PubMed:22134920"
FT MUTAGEN 112
FT /note="N->A,Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18614531"
FT MUTAGEN 113
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18614531"
FT MUTAGEN 113
FT /note="C->S: Loss of phospholipase activity and loss of
FT organelle membrane rupture."
FT /evidence="ECO:0000269|PubMed:18614531,
FT ECO:0000269|PubMed:33854238"
FT MUTAGEN 129
FT /note="Q->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:18614531"
FT CONFLICT 42
FT /note="I -> V (in Ref. 4; AAH24581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17872 MW; E688128CF00AADAB CRC64;
MLAPIPEPKP GDLIEIFRPM YRHWAIYVGD GYVIHLAPPS EIAGAGAASI MSALTDKAIV
KKELLCHVAG KDKYQVNNKH DEEYTPLPLS KIIQRAERLV GQEVLYRLTS ENCEHFVNEL
RYGVPRSDQV RDAVKAVGIA GVGLAALGLV GVMLSRNKKQ KQ
