PLAT1_RAT
ID PLAT1_RAT Reviewed; 167 AA.
AC D2KX21;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Phospholipase A and acyltransferase 1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9QZU4};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q9QZU4};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q9QZU4};
DE AltName: Full=HRAS-like suppressor 1;
DE Short=HRSL1;
DE AltName: Full=Phospholipid-metabolizing enzyme A-C1;
DE AltName: Full=Rat LRAT-like protein-2 {ECO:0000303|PubMed:17158102};
DE Short=RLP-2 {ECO:0000303|PubMed:17158102};
GN Name=Plaat1 {ECO:0000312|RGD:1309485};
GN Synonyms=A-C1, Hrasls {ECO:0000312|RGD:1309485}, Hrasrs,
GN RLP-2 {ECO:0000303|PubMed:17158102};
GN ORFNames=rCG_36537 {ECO:0000312|EMBL:EDL78138.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAI63212.1};
RN [1] {ECO:0000312|EMBL:BAI63212.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Uyama T., Ueda N.;
RT "Characterization of A-C1 as an enzyme related to lipid metabolism.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RX PubMed=17158102; DOI=10.1074/jbc.m606369200;
RA Jin X.H., Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Discovery and characterization of a Ca2+-independent
RT phosphatidylethanolamine N-acyltransferase generating the anandamide
RT precursor and its congeners.";
RL J. Biol. Chem. 282:3614-3623(2007).
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 (By similarity).
CC Shows O-acyltransferase activity, catalyzing the transfer of a fatty
CC acyl group from glycerophospholipid to the hydroxyl group of
CC lysophospholipid (By similarity). {ECO:0000250|UniProtKB:Q9HDD0,
CC ECO:0000250|UniProtKB:Q9QZU4}.
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:Q9QZU4};
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:Q9QZU4};
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 {ECO:0000250|UniProtKB:Q9QZU4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9QZU4}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AB510983; BAI63212.1; -; mRNA.
DR EMBL; AABR07034534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07034535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07034536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473999; EDL78138.1; -; Genomic_DNA.
DR EMBL; CH473999; EDL78140.1; -; Genomic_DNA.
DR RefSeq; NP_001099341.1; NM_001105871.1.
DR RefSeq; XP_006248572.1; XM_006248510.3.
DR AlphaFoldDB; D2KX21; -.
DR SMR; D2KX21; -.
DR STRING; 10116.ENSRNOP00000002329; -.
DR PaxDb; D2KX21; -.
DR Ensembl; ENSRNOT00000002329; ENSRNOP00000002329; ENSRNOG00000001711.
DR GeneID; 288025; -.
DR KEGG; rno:288025; -.
DR UCSC; RGD:1309485; rat.
DR CTD; 57110; -.
DR RGD; 1309485; Plaat1.
DR eggNOG; ENOG502QU0S; Eukaryota.
DR GeneTree; ENSGT00940000156634; -.
DR HOGENOM; CLU_109418_0_0_1; -.
DR InParanoid; D2KX21; -.
DR OMA; RSGYQHW; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; D2KX21; -.
DR TreeFam; TF330836; -.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR PRO; PR:D2KX21; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Proteomes; UP000234681; Chromosome 11.
DR Bgee; ENSRNOG00000001711; Expressed in quadriceps femoris and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; ISO:RGD.
DR GO; GO:0008374; F:O-acyltransferase activity; ISO:RGD.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISO:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:RGD.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0046485; P:ether lipid metabolic process; ISO:RGD.
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:RGD.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:RGD.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Nucleus; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..167
FT /note="Phospholipase A and acyltransferase 1"
FT /id="PRO_0000450338"
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"
SQ SEQUENCE 167 AA; 18521 MW; 5A7C30ED78CD19F8 CRC64;
MAVNDCFSLT YPHNPHPGDL IEVFRPCYQH WALYLGDGYV INIAPVDGIP SSFSSAKSVF
STKALVKMQL LKDVVGNDTY RINNKYDTTY PPLPVEEVIQ RSEFAIGQEV TYDLLVNNCE
HFVTLLRYGE GVSEQANRAI GTIGLVAAGI DIFTFLGLFP KRQGAKS
