PLAT1_DANRE
ID PLAT1_DANRE Reviewed; 179 AA.
AC A0A0R4IY06; Q6DGY9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Phospholipase A and acyltransferase 1;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9HDD0};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q9HDD0};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q9HDD0};
GN Name=plaat1 {ECO:0000312|ZFIN:ZDB-GENE-040718-330};
GN Synonyms=hrasls {ECO:0000312|ZFIN:ZDB-GENE-040718-330};
GN ORFNames=zgc:92715 {ECO:0000312|EMBL:AAH76195.1,
GN ECO:0000312|ZFIN:ZDB-GENE-040718-330};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 147-ALA--PHE-179.
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. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity,
CC catalyzing the calcium-independent release of fatty acids from the sn-1
CC or sn-2 position of glycerophospholipids. Shows O-acyltransferase
CC activity, catalyzing the transfer of a fatty acyl group from
CC glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-
CC acyltransferase activity, catalyzing the calcium-independent transfer
CC of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC)
CC and other glycerophospholipids to the primary amine of
CC phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine
CC (NAPE) which serves as precursor for N-acylethanolamines (NAEs) (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) (By similarity).
CC {ECO:0000250|UniProtKB:Q9HDD0, ECO:0000269|PubMed:33854238}.
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:Q9HDD0};
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:0000250|UniProtKB:Q9HDD0};
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: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:33854238}. Mitochondrion membrane
CC {ECO:0000269|PubMed:33854238}; Single-pass membrane protein
CC {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:33854238}; Single-
CC pass membrane protein {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 and lysosomes, immediately before organelle degradation. This
CC translocation is triggered by organelle membrane damage and requires
CC the C-terminal transmembrane domain. {ECO:0000269|PubMed:33854238}.
CC -!- TISSUE SPECIFICITY: Expressed in the eye lens.
CC {ECO:0000269|PubMed:33854238}.
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: Knockout animals exhibit normal growth of their
CC body and eye lens. However, the disappearance of mitochondria and the
CC endoplasmic reticulum in the lens is almost completely suppressed and
CC membranous structures persisted in the lens central region.
CC {ECO:0000269|PubMed:33854238}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH76195.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CABZ01072478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FQ323135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076195; AAH76195.1; ALT_INIT; mRNA.
DR RefSeq; NP_001002590.2; NM_001002590.1.
DR AlphaFoldDB; A0A0R4IY06; -.
DR SMR; A0A0R4IY06; -.
DR STRING; 7955.ENSDARP00000107633; -.
DR PaxDb; A0A0R4IY06; -.
DR DNASU; 436863; -.
DR Ensembl; ENSDART00000167347; ENSDARP00000140448; ENSDARG00000100021.
DR GeneID; 436863; -.
DR KEGG; dre:436863; -.
DR CTD; 57110; -.
DR ZFIN; ZDB-GENE-040718-330; plaat1.
DR eggNOG; ENOG502QU0S; Eukaryota.
DR GeneTree; ENSGT00940000156634; -.
DR OMA; RSGYQHW; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; A0A0R4IY06; -.
DR Reactome; R-DRE-1482839; Acyl chain remodelling of PE.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000100021; Expressed in head and 8 other tissues.
DR ExpressionAtlas; A0A0R4IY06; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008970; F:phospholipase A1 activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IBA:GO_Central.
DR GO; GO:1903008; P:organelle disassembly; IMP:UniProtKB.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Membrane; Mitochondrion; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..179
FT /note="Phospholipase A and acyltransferase 1"
FT /id="PRO_0000453959"
FT TOPO_DOM 1..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..179
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 30..146
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 40
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT ACT_SITE 130
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT MUTAGEN 147..179
FT /note="Missing: In the eye lens, loss of targeting to
FT mitochondria at the time of organelle rupture."
FT /evidence="ECO:0000269|PubMed:33854238"
SQ SEQUENCE 179 AA; 19845 MW; 54A038027905C8F6 CRC64;
MDNQQRRTDN MASGETDHLQ CVEEPQPGDL IEIFRPAYQH WALYLGDGYI INLTPVDEGQ
ATAVSSVKSV FSRKAVVRMQ LLKEVVGADS YRINNKYDDD HTPLPVSEII QRAQMLIGQE
VSYDLLGSNC EHFVTLLRYG EGVSEQASRA IGAISLVTAA ASAFSVLGLI NTRSRNRPF
