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 16-JUN-2009, entry version 68. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 226-233 AND 428-440, RP TISSUE SPECIFICITY, AND ENZYME ACTIVITY. RC TISSUE=Liver; RX MEDLINE=98241627; 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 RT lysophospholipase containing an asparaginase-like region and ankyrin RT 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP CHARACTERIZATION. RX MEDLINE=94164994; PubMed=8119970; RA Sugimoto H., Yamashita S.; RT "Purification, characterization, and inhibition by phosphatidic acid RT of lysophospholipase transacylase from rat liver."; RL J. Biol. Chem. 269:6252-6258(1994). 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 -!- ENZYME REGULATION: Inhibited by phosphatidic acid. CC -!- SUBUNIT: Monomer. CC -!- TISSUE SPECIFICITY: Expressed at high levels in liver and kidney CC and at a low level in stomach. Barely detectable in lung, heart, CC spleen and brain. CC -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase CC 1 family. CC -!- SIMILARITY: Contains 5 ANK repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009372; BAA31197.1; -; mRNA. DR EMBL; BC098655; AAH98655.1; -; mRNA. DR IPI; IPI00207299; -. DR RefSeq; NP_653351.1; -. DR UniGene; Rn.29979; -. DR HSSP; P09959; 1SW6. DR PhosphoSite; O88202; -. DR PRIDE; O88202; -. DR Ensembl; ENSRNOG00000012843; Rattus norvegicus. DR GeneID; 246266; -. DR KEGG; rno:246266; -. DR RGD; 708388; LOC246266. DR HOVERGEN; O88202; -. DR BRENDA; 3.1.1.47; 248. DR BRENDA; 3.1.1.5; 248. DR BRENDA; 3.5.1.1; 248. DR NextBio; 623626; -. DR ArrayExpress; O88202; -. DR GermOnline; ENSRNOG00000012843; Rattus norvegicus. DR GO; GO:0005625; C:soluble fraction; IDA:RGD. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine ester...; IMP:RGD. DR GO; GO:0004067; F:asparaginase activity; IDA:UniProtKB. DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB. 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 InterPro; IPR002110; ANK. DR InterPro; IPR006033; AsnASEI. DR InterPro; IPR006034; Asp/Glutamnse. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. 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; Direct protein sequencing; Hydrolase; Lipid degradation; KW Phosphoprotein; Repeat. FT CHAIN 1 564 60 kDa lysophospholipase. FT /FTId=PRO_0000171092. 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 (By similarity). FT CONFLICT 280 280 I -> L (in Ref. 2; AAH98655). 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 //