PLAT1_MOUSE
ID PLAT1_MOUSE Reviewed; 167 AA.
AC Q9QZU4; Q5D099; Q9D0S3;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Phospholipase A and acyltransferase 1 {ECO:0000250|UniProtKB:Q9HDD0};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9HDD0};
DE EC=3.1.1.32 {ECO:0000269|PubMed:21880860};
DE EC=3.1.1.4 {ECO:0000269|PubMed:21880860};
DE AltName: Full=HRAS-like suppressor 1 {ECO:0000312|MGI:MGI:1351473};
DE Short=HRSL1;
DE AltName: Full=Phospholipid-metabolizing enzyme A-C1;
GN Name=Plaat1 {ECO:0000250|UniProtKB:Q9HDD0};
GN Synonyms=Hrasls {ECO:0000312|MGI:MGI:1351473}, Hrasrs;
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), TISSUE SPECIFICITY (ISOFORM 1), AND
RP SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=10542256; DOI=10.1074/jbc.274.45.32192;
RA Akiyama H., Hiraki Y., Noda M., Shigeno C., Ito H., Nakamura T.;
RT "Molecular cloning and biological activity of a novel Ha-Ras suppressor
RT gene predominantly expressed in skeletal muscle, heart, brain, and bone
RT marrow by differential display using clonal mouse EC cells, ATDC5.";
RL J. Biol. Chem. 274:32192-32197(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), AND CATALYTIC
RP ACTIVITY (ISOFORM 1).
RX PubMed=21880860; DOI=10.1194/jlr.m015081;
RA Shinohara N., Uyama T., Jin X.H., Tsuboi K., Tonai T., Houchi H., Ueda N.;
RT "Enzymological analysis of the tumor suppressor A-C1 reveals a novel group
RT of phospholipid-metabolizing enzymes.";
RL J. Lipid Res. 52:1927-1935(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal cord;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1
RP AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RX PubMed=27623847; DOI=10.1194/jlr.m071290;
RA Hussain Z., Uyama T., Kawai K., Rahman I.A., Tsuboi K., Araki N., Ueda N.;
RT "Comparative analyses of isoforms of the calcium-independent
RT phosphatidylethanolamine N-acyltransferase PLAAT-1 in humans and mice.";
RL J. Lipid Res. 57:2051-2060(2016).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2)
CC activity, catalyzing the calcium-independent release of fatty acids
CC from the sn-1 or sn-2 position of glycerophospholipids
CC (PubMed:21880860). Shows O-acyltransferase activity, catalyzing the
CC transfer of a fatty acyl group from glycerophospholipid to the hydroxyl
CC group of 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) (By similarity).
CC {ECO:0000250|UniProtKB:Q9HDD0, ECO:0000269|PubMed:21880860}.
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:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
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:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
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:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
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:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
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:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
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:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-
CC phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:77369;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365;
CC Evidence={ECO:0000250|UniProtKB:Q9HDD0};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10542256,
CC ECO:0000269|PubMed:27623847}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:27623847}. Cytoplasm {ECO:0000269|PubMed:27623847}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PLAAT-1S {ECO:0000303|PubMed:27623847};
CC IsoId=Q9QZU4-1; Sequence=Displayed;
CC Name=2; Synonyms=PLAAT-1L {ECO:0000303|PubMed:27623847};
CC IsoId=Q9QZU4-2; Sequence=VSP_060191;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in skeletal muscle, heart,
CC brain, bone marrow and testis. {ECO:0000269|PubMed:10542256,
CC ECO:0000269|PubMed:27623847}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Abundantly expressed in brain, heart,
CC and skeletal muscle. {ECO:0000269|PubMed:27623847}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AF163095; AAF13304.1; -; mRNA.
DR EMBL; AB510982; BAI63211.1; -; mRNA.
DR EMBL; AK004528; BAB23348.1; -; mRNA.
DR EMBL; AK039471; BAC30361.1; -; mRNA.
DR EMBL; AC154448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97707.1; -; Genomic_DNA.
DR EMBL; CH466521; EDK97708.1; -; Genomic_DNA.
DR EMBL; BC048482; AAH48482.1; -; mRNA.
DR CCDS; CCDS28094.1; -. [Q9QZU4-1]
DR RefSeq; NP_038779.2; NM_013751.5.
DR RefSeq; XP_006522267.1; XM_006522204.1.
DR RefSeq; XP_017172511.1; XM_017317022.1.
DR AlphaFoldDB; Q9QZU4; -.
DR SMR; Q9QZU4; -.
DR STRING; 10090.ENSMUSP00000087257; -.
DR iPTMnet; Q9QZU4; -.
DR PhosphoSitePlus; Q9QZU4; -.
DR PaxDb; Q9QZU4; -.
DR PRIDE; Q9QZU4; -.
DR DNASU; 27281; -.
DR GeneID; 27281; -.
DR KEGG; mmu:27281; -.
DR UCSC; uc007yvw.1; mouse. [Q9QZU4-1]
DR CTD; 57110; -.
DR MGI; MGI:1351473; Plaat1.
DR eggNOG; ENOG502QU0S; Eukaryota.
DR InParanoid; Q9QZU4; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q9QZU4; -.
DR TreeFam; TF330836; -.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR BioGRID-ORCS; 27281; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Hrasls; mouse.
DR PRO; PR:Q9QZU4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QZU4; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
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:0008374; F:O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; IDA:MGI.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISO:MGI.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IDA:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:MGI.
DR GO; GO:0001558; P:regulation of cell growth; TAS:MGI.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Nucleus; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="Phospholipase A and acyltransferase 1"
FT /id="PRO_0000152482"
FT TOPO_DOM 1..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 20..135
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 30
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT ACT_SITE 119
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT VAR_SEQ 1
FT /note="M -> MPEACLEDLGGGEGAGLGRAPKTRGRRQGPQDAVWQARARNPRRDQR
FT WRGARTLALTQRREAVVALAVALASGRCGWSHPGSASGTAASPWRTREARHCLQGTKTT
FT QLEQM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:27623847"
FT /id="VSP_060191"
FT CONFLICT 105
FT /note="P -> A (in Ref. 1; BAB23348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 18810 MW; 619C43691DCC86C8 CRC64;
MAVNDCFSLT YPHNPHPGDL IEVFRPCYQH WALYLGDGYV INIAPIDGIR SSFTSAKSVF
STKALVKMQL LKDVVGNDTY RINNKYDTTY PPLPVEEVIQ RSEFPIGQEV AYDLLVNNCE
HFVTLLRYGE GVSEQANRAI GTIGLVAAGI DIFTFLGLFP KRQRTKY
