LPP60_MOUSE
ID LPP60_MOUSE Reviewed; 564 AA.
AC A0JNU3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=60 kDa lysophospholipase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:O88202};
DE AltName: Full=Lysophospholipase-transacylase {ECO:0000250|UniProtKB:O88202};
DE Includes:
DE RecName: Full=L-asparaginase;
DE EC=3.5.1.1 {ECO:0000250|UniProtKB:O88202};
DE AltName: Full=L-asparagine amidohydrolase;
DE Includes:
DE RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:O88202};
DE AltName: Full=Platelet-activating factor acetylhydrolase;
DE Short=PAF acetylhydrolase;
GN Name=Aspg;
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 [LARGE SCALE MRNA].
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
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).
CC -!- FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase
CC and asparaginase activities (By similarity). Can catalyze three types
CC of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-
CC 3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and
CC 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-
CC GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-
CC phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to
CC -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position
CC of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (By similarity).
CC Mediates the synthesis of 1-arachidonoyl species of phospholipids by
CC transferring the arachidonoyl residue from 2-arachidonoyl
CC lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (By
CC similarity). {ECO:0000250|UniProtKB:O88202}.
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40904;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40908;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41321;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41353;
CC Evidence={ECO:0000250|UniProtKB:O88202};
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:0000250|UniProtKB:O88202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40960;
CC Evidence={ECO:0000250|UniProtKB:O88202};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O88202}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase 1
CC family. {ECO:0000305}.
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DR EMBL; BC126962; AAI26963.1; -; mRNA.
DR CCDS; CCDS36567.1; -.
DR RefSeq; NP_001074638.1; NM_001081169.1.
DR AlphaFoldDB; A0JNU3; -.
DR SMR; A0JNU3; -.
DR BioGRID; 222710; 1.
DR STRING; 10090.ENSMUSP00000078369; -.
DR iPTMnet; A0JNU3; -.
DR PhosphoSitePlus; A0JNU3; -.
DR jPOST; A0JNU3; -.
DR MaxQB; A0JNU3; -.
DR PaxDb; A0JNU3; -.
DR PRIDE; A0JNU3; -.
DR ProteomicsDB; 292024; -.
DR Antibodypedia; 59083; 60 antibodies from 14 providers.
DR Ensembl; ENSMUST00000079400; ENSMUSP00000078369; ENSMUSG00000037686.
DR GeneID; 104816; -.
DR KEGG; mmu:104816; -.
DR UCSC; uc007pek.1; mouse.
DR CTD; 374569; -.
DR MGI; MGI:2144822; Aspg.
DR VEuPathDB; HostDB:ENSMUSG00000037686; -.
DR eggNOG; KOG0503; Eukaryota.
DR GeneTree; ENSGT00390000001610; -.
DR HOGENOM; CLU_019134_3_0_1; -.
DR InParanoid; A0JNU3; -.
DR OMA; NCVCYLI; -.
DR OrthoDB; 886725at2759; -.
DR PhylomeDB; A0JNU3; -.
DR TreeFam; TF315247; -.
DR BRENDA; 3.1.1.47; 3474.
DR Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR BioGRID-ORCS; 104816; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Aspg; mouse.
DR PRO; PR:A0JNU3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; A0JNU3; protein.
DR Bgee; ENSMUSG00000037686; Expressed in gastrula and 87 other tissues.
DR ExpressionAtlas; A0JNU3; baseline and differential.
DR Genevisible; A0JNU3; MM.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISO:MGI.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; ISO:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0006528; P:asparagine metabolic process; ISO:MGI.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
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; PF13857; Ank_5; 1.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
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; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..564
FT /note="60 kDa lysophospholipase"
FT /id="PRO_0000324164"
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:0007744|PubMed:21183079"
SQ SEQUENCE 564 AA; 60595 MW; 986677FD4963A55C CRC64;
MARAMGPERR LLAIYTGGTI GMRSEGGVLV PGRGLAAVLK TLHMFHDEEY AQAHSLPEDT
LVLPPASPDQ RIIYTVLECQ PLFDSSDMTI TEWVQIAQTI ERHYAQYQGF VVIHGTDTMA
FAASVLSFML ENLQKPVVLT GAQVPIHALW SDGRENLLGA LLMAGQYVIP EVCLFFQNQL
FRGNRTTKVD ARRFAAFCSP NLPPLATVGA DVTINRELVR KACGKSHLVV HSSMEPDVGL
LRLYPGIPAS LVRTFLQPPL KGVVMETFGS GNGPTKPDLL QELRVAAEQG LIIVNCTHCL
QGAVTSDYAS GMAMAGAGIV SGFDMTSEAA LAKLSYVLGQ PGLSLNDRKK LLAKDLRGEM
TLPATDVLLQ DGMLGCRVAW LLSMNGSQEA DTMKDVLLPG LALAAAHAGD LDTLQAFVEL
DRDLNLKDYS GQTPLHVAAR RGHAAVVTML LQRGADVDAR NEDGQSPLLL AVRGRHQSVI
GLLRAAGARL SPQELEDVGT ELCRLASRGD SEGLRAWWQA GADLGQPDYD GHCALQVAEA
AGNADVVALL QSFKDSVCAQ PQPH
