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   16-JUN-2009, entry version 27.
DE   RecName: Full=60 kDa lysophospholipase;
DE            EC=3.1.1.5;
DE   Includes:
DE     RecName: Full=L-asparaginase;
DE              EC=3.5.1.1;
DE     AltName: Full=L-asparagine amidohydrolase;
DE   Includes:
DE     RecName: Full=Platelet-activating factor acetylhydrolase;
DE              Short=PAF acetylhydrolase;
DE              EC=3.1.1.47;
GN   Name=Aspg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Exhibits lysophospholipase, transacylase, PAF
CC       acetylhydrolase and asparaginase activities.
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- CATALYTIC ACTIVITY: L-asparagine + H(2)O = L-aspartate + NH(3).
CC   -!- CATALYTIC ACTIVITY: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine +
CC       H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase
CC       1 family.
CC   -!- SIMILARITY: Contains 5 ANK repeats.
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DR   EMBL; BC126962; AAI26963.1; -; mRNA.
DR   IPI; IPI00341423; -.
DR   RefSeq; NP_001074638.1; -.
DR   UniGene; Mm.77133; -.
DR   PhosphoSite; A0JNU3; -.
DR   Ensembl; ENSMUSG00000037686; Mus musculus.
DR   GeneID; 104816; -.
DR   KEGG; mmu:104816; -.
DR   NMPDR; fig|10090.3.peg.27151; -.
DR   MGI; MGI:2144822; A530050D06Rik.
DR   HOVERGEN; A0JNU3; -.
DR   OMA; A0JNU3; FVIPEVC.
DR   BRENDA; 3.1.1.47; 244.
DR   BRENDA; 3.1.1.5; 244.
DR   BRENDA; 3.5.1.1; 244.
DR   NextBio; 357306; -.
DR   Bgee; A0JNU3; -.
DR   CleanEx; MM_A530050D06RIK; -.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine ester...; IEA:EC.
DR   GO; GO:0004067; F:asparaginase activity; IEA:EC.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002110; ANK.
DR   InterPro; IPR006033; AsnASEI.
DR   InterPro; IPR006034; Asp/Glutamnse.
DR   PANTHER; PTHR11707; Asp/Glutamnse; 1.
DR   Pfam; PF00023; Ank; 4.
DR   Pfam; PF00710; Asparaginase; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   ProDom; PD003221; Asp/Glutamnse; 1.
DR   SMART; SM00248; ANK; 4.
DR   TIGRFAMs; TIGR00519; asnASE_I; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; FALSE_NEG.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Hydrolase; Lipid degradation; Phosphoprotein; Repeat.
FT   CHAIN         1    564       60 kDa lysophospholipase.
FT                                /FTId=PRO_0000324164.
FT   REPEAT      141    170       ANK 1.
FT   REPEAT      396    426       ANK 2.
FT   REPEAT      430    459       ANK 3.
FT   REPEAT      463    492       ANK 4.
FT   REPEAT      530    559       ANK 5.
FT   REGION       41    350       Asparaginase.
FT   ACT_SITE     19     19       By similarity.
FT   ACT_SITE    116    116       By similarity.
FT   ACT_SITE    117    117       By similarity.
FT   ACT_SITE    187    187       By similarity.
FT   MOD_RES     387    387       Phosphoserine.
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
//