LPP60_RAT
ID LPP60_RAT Reviewed; 564 AA.
AC O88202; Q4G088;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=60 kDa lysophospholipase;
DE EC=3.1.1.5 {ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212};
DE AltName: Full=Lysophospholipase-transacylase {ECO:0000303|PubMed:10320809, ECO:0000303|PubMed:8119970, ECO:0000303|PubMed:9575212};
DE Includes:
DE RecName: Full=L-asparaginase;
DE EC=3.5.1.1 {ECO:0000269|PubMed:9575212};
DE AltName: Full=L-asparagine amidohydrolase;
DE Includes:
DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE EC=3.1.1.47 {ECO:0000269|PubMed:9575212};
DE AltName: Full=Platelet-activating factor acetylhydrolase {ECO:0000303|PubMed:9575212};
DE Short=PAF acetylhydrolase {ECO:0000303|PubMed:9575212};
GN Name=Aspg;
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:BAA31197.1};
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31197.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 226-233 AND 428-440, TISSUE
RP SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=9575212; DOI=10.1074/jbc.273.20.12536;
RA Sugimoto H., Odani S., Yamashita S.;
RT "Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase
RT containing an asparaginase-like region and ankyrin repeat.";
RL J. Biol. Chem. 273:12536-12542(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP ACTIVITY REGULATION.
RX PubMed=8119970; DOI=10.1016/s0021-9258(17)37595-6;
RA Sugimoto H., Yamashita S.;
RT "Purification, characterization, and inhibition by phosphatidic acid of
RT lysophospholipase transacylase from rat liver.";
RL J. Biol. Chem. 269:6252-6258(1994).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10320809; DOI=10.1016/s1388-1981(99)00059-1;
RA Sugimoto H., Yamashita S.;
RT "Characterization of the transacylase activity of rat liver 60-kDa
RT lysophospholipase-transacylase. Acyl transfer from the sn-2 to the sn-1
RT position.";
RL Biochim. Biophys. Acta 1438:264-272(1999).
CC -!- FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase
CC and asparaginase activities (PubMed:9575212, PubMed:8119970,
CC PubMed:10320809). Can catalyze three types of transacylation reactions:
CC (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC)
CC to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3)
CC transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of
CC 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and
CC other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer
CC from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2
CC to -1 transfer) (PubMed:10320809). Mediates the synthesis of 1-
CC arachidonoyl species of phospholipids by transferring the arachidonoyl
CC residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-
CC acyl lysophospholipid (PubMed:10320809). {ECO:0000269|PubMed:10320809,
CC ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970,
CC ECO:0000269|PubMed:9575212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970,
CC ECO:0000305|PubMed:9575212};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000269|PubMed:9575212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017;
CC Evidence={ECO:0000305|PubMed:9575212};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000269|PubMed:9575212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000305|PubMed:9575212};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:8119970, ECO:0000305|PubMed:9575212};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC octadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40887,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:73858;
CC Evidence={ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888;
CC Evidence={ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = H(+) +
CC hexadecanoate + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892;
CC Evidence={ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-
CC sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40899, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73005;
CC Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine
CC + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40903,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40904;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40907, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40908;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(9Z)-octadecenoyl-2-O-acetyl-sn-glycero-3-phosphocholine +
CC H2O = (9Z)-octadecenoate + 2-acetyl-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:41320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78044, ChEBI:CHEBI:78045;
CC Evidence={ECO:0000269|PubMed:8119970};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41321;
CC Evidence={ECO:0000305|PubMed:8119970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-hexadecanoyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:41352, ChEBI:CHEBI:16870, ChEBI:CHEBI:64771,
CC ChEBI:CHEBI:64874, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41353;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphocholine = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40959, ChEBI:CHEBI:16870, ChEBI:CHEBI:60657,
CC ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40960;
CC Evidence={ECO:0000305|PubMed:10320809};
CC -!- ACTIVITY REGULATION: Inhibited by phosphatidic acid.
CC {ECO:0000269|PubMed:8119970}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=91 uM for 1-palmitoyl-glycerophosphocholine
CC {ECO:0000269|PubMed:8119970};
CC Vmax=12.9 nmol/min/mg enzyme for 1-palmitoyl-glycerophosphocholine
CC {ECO:0000269|PubMed:8119970};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:8119970};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8119970}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in liver and kidney and at
CC a low level in stomach. Barely detectable in lung, heart, spleen and
CC brain. {ECO:0000269|PubMed:9575212}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase 1
CC family. {ECO:0000305}.
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DR EMBL; AB009372; BAA31197.1; -; mRNA.
DR EMBL; BC098655; AAH98655.1; -; mRNA.
DR RefSeq; NP_653351.1; NM_144750.2.
DR AlphaFoldDB; O88202; -.
DR SMR; O88202; -.
DR STRING; 10116.ENSRNOP00000017454; -.
DR SwissLipids; SLP:000000623; -.
DR iPTMnet; O88202; -.
DR PhosphoSitePlus; O88202; -.
DR PaxDb; O88202; -.
DR GeneID; 246266; -.
DR KEGG; rno:246266; -.
DR UCSC; RGD:708388; rat.
DR CTD; 374569; -.
DR RGD; 708388; Aspg.
DR eggNOG; KOG0503; Eukaryota.
DR InParanoid; O88202; -.
DR OrthoDB; 886725at2759; -.
DR PhylomeDB; O88202; -.
DR TreeFam; TF315247; -.
DR Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR PRO; PR:O88202; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IMP:RGD.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0006528; P:asparagine metabolic process; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR CDD; cd08963; L-asparaginase_I; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR006033; AsnA_fam.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR041725; L-asparaginase_I.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00519; asnASE_I; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ANK repeat; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..564
FT /note="60 kDa lysophospholipase"
FT /id="PRO_0000171092"
FT DOMAIN 9..355
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT REPEAT 141..170
FT /note="ANK 1"
FT REPEAT 396..426
FT /note="ANK 2"
FT REPEAT 430..459
FT /note="ANK 3"
FT REPEAT 463..492
FT /note="ANK 4"
FT REPEAT 530..559
FT /note="ANK 5"
FT REGION 41..350
FT /note="Asparaginase"
FT ACT_SITE 19
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0JNU3"
FT CONFLICT 280
FT /note="I -> L (in Ref. 2; AAH98655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 60795 MW; 9DBB2F8FA8B1C477 CRC64;
MARATGPEQR LLAIYTGGTI GMRSEGGVLV PGRGLAAVLR TLHMLHDEEY ARAHSLPEDT
LVLPPASSDQ RIIYKVLECQ PLFDSSDMTI TEWVQIAQTI ERHYTQYQGF VVIHGTDTMA
FAASVLSFML ENLQKPVILT GAQVPIHELW SDGRENLLGA LLMAGQYVIP EVCLFFQNQL
FRGNRTTKVD ARRFAAFCSP NLPPLATVGA DVTINRELVR KASWKSHLVV HSNMEPDVGL
LRLYPGIPAS LVRTFLQPPL KGVVMETFGS GNGPTKPDLI QELRAAAERG LIIVNCTHCL
QGAVTSDYAP GMAMAGAGII SGFDMTSEAA LAKLSYVLGQ PGLSLSDRKK LLAKDLRGEM
TLPTTDDLLG DDMLGCRATW LLSMNGSQDA DAMKDVLLPG LALAAAHAGD LDTLQAFVEL
GRDLNLKDYS GQTPLHVAAR RGHASVVAML LQKGVDVDAC NEDGQSPLLL AVRGRHQSVI
RLLRAAGAHL SPQELEDVGT ELCRLASRAD SEGLRAWWQA GADLGQPDYD GHCALQVAEA
AGNADVVALL QSLEDRVSAQ PQPH
