LPP60_HUMAN
ID LPP60_HUMAN Reviewed; 573 AA.
AC Q86U10; B9EGQ2; Q8IV80;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=60 kDa lysophospholipase;
DE Short=LysoLP;
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; Synonyms=C14orf76;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-344.
RC TISSUE=Ovary, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-64.
RC TISSUE=Fetal liver;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-573 (ISOFORM 3).
RC TISSUE=Kidney;
RG The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- INTERACTION:
CC Q86U10; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-19946665, EBI-12155483;
CC Q86U10; P40199: CEACAM6; NbExp=3; IntAct=EBI-19946665, EBI-4314501;
CC Q86U10; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-19946665, EBI-9679045;
CC Q86U10; P57764: GSDMD; NbExp=3; IntAct=EBI-19946665, EBI-2798865;
CC Q86U10; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-19946665, EBI-5662487;
CC Q86U10; Q14D33: RTP5; NbExp=3; IntAct=EBI-19946665, EBI-10217913;
CC Q86U10; Q92529: SHC3; NbExp=3; IntAct=EBI-19946665, EBI-79084;
CC Q86U10; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-19946665, EBI-8644516;
CC Q86U10; Q12893: TMEM115; NbExp=3; IntAct=EBI-19946665, EBI-8633987;
CC Q86U10; O75604: USP2; NbExp=3; IntAct=EBI-19946665, EBI-743272;
CC Q86U10; Q9BRG1: VPS25; NbExp=5; IntAct=EBI-19946665, EBI-741945;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86U10-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q86U10-3; Sequence=VSP_040740;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase 1
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD62331.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AL136001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81858.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81859.1; -; Genomic_DNA.
DR EMBL; BC035836; AAH35836.1; -; mRNA.
DR EMBL; BC136637; AAI36638.1; -; mRNA.
DR EMBL; BX247999; CAD62331.1; ALT_SEQ; mRNA.
DR EMBL; AI373537; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS45170.2; -. [Q86U10-1]
DR RefSeq; NP_001073933.2; NM_001080464.2. [Q86U10-1]
DR RefSeq; XP_005267647.1; XM_005267590.4. [Q86U10-3]
DR AlphaFoldDB; Q86U10; -.
DR SMR; Q86U10; -.
DR BioGRID; 131909; 13.
DR IntAct; Q86U10; 11.
DR STRING; 9606.ENSP00000450040; -.
DR DrugBank; DB00721; Procaine.
DR PhosphoSitePlus; Q86U10; -.
DR BioMuta; ASPG; -.
DR DMDM; 317373428; -.
DR MassIVE; Q86U10; -.
DR PaxDb; Q86U10; -.
DR PeptideAtlas; Q86U10; -.
DR PRIDE; Q86U10; -.
DR ProteomicsDB; 69756; -. [Q86U10-1]
DR ProteomicsDB; 69757; -. [Q86U10-3]
DR Antibodypedia; 59083; 60 antibodies from 14 providers.
DR DNASU; 374569; -.
DR Ensembl; ENST00000551177.6; ENSP00000450040.1; ENSG00000166183.16. [Q86U10-1]
DR GeneID; 374569; -.
DR KEGG; hsa:374569; -.
DR MANE-Select; ENST00000551177.6; ENSP00000450040.1; NM_001080464.3; NP_001073933.2.
DR UCSC; uc001yoq.3; human. [Q86U10-1]
DR CTD; 374569; -.
DR DisGeNET; 374569; -.
DR GeneCards; ASPG; -.
DR HGNC; HGNC:20123; ASPG.
DR HPA; ENSG00000166183; Tissue enhanced (heart muscle, liver).
DR MIM; 618472; gene.
DR neXtProt; NX_Q86U10; -.
DR OpenTargets; ENSG00000166183; -.
DR VEuPathDB; HostDB:ENSG00000166183; -.
DR eggNOG; KOG0503; Eukaryota.
DR GeneTree; ENSGT00390000001610; -.
DR HOGENOM; CLU_019134_3_0_1; -.
DR InParanoid; Q86U10; -.
DR OMA; NCVCYLI; -.
DR OrthoDB; 886725at2759; -.
DR PhylomeDB; Q86U10; -.
DR TreeFam; TF315247; -.
DR BioCyc; MetaCyc:HS15413-MON; -.
DR PathwayCommons; Q86U10; -.
DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
DR SignaLink; Q86U10; -.
DR SIGNOR; Q86U10; -.
DR BioGRID-ORCS; 374569; 10 hits in 1057 CRISPR screens.
DR GenomeRNAi; 374569; -.
DR Pharos; Q86U10; Tbio.
DR PRO; PR:Q86U10; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86U10; protein.
DR Bgee; ENSG00000166183; Expressed in right lobe of liver and 98 other tissues.
DR ExpressionAtlas; Q86U10; baseline and differential.
DR Genevisible; Q86U10; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0009066; P:aspartate family amino acid metabolic process; TAS:Reactome.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; Alternative splicing; ANK repeat; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..573
FT /note="60 kDa lysophospholipase"
FT /id="PRO_0000324163"
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 399..429
FT /note="ANK 2"
FT REPEAT 433..462
FT /note="ANK 3"
FT REPEAT 466..495
FT /note="ANK 4"
FT REPEAT 533..562
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 VAR_SEQ 568
FT /note="E -> EPSCFQE (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040740"
FT VARIANT 95
FT /note="C -> R (in dbSNP:rs1770984)"
FT /id="VAR_059131"
FT VARIANT 96
FT /note="L -> V (in dbSNP:rs1744284)"
FT /id="VAR_059132"
FT VARIANT 344
FT /note="S -> R (in dbSNP:rs8012505)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_059133"
SQ SEQUENCE 573 AA; 60883 MW; 62DBC583FF9C3AD7 CRC64;
MARAVGPERR LLAVYTGGTI GMRSELGVLV PGTGLAAILR TLPMFHDEEH ARARGLSEDT
LVLPPASRNQ RILYTVLECQ PLFDSSDMTI AEWVCLAQTI KRHYEQYHGF VVIHGTDTMA
FAASMLSFML ENLQKTVILT GAQVPIHALW SDGRENLLGA LLMAGQYVIP EVCLFFQNQL
FRGNRATKVD ARRFAAFCSP NLLPLATVGA DITINRELVR KVDGKAGLVV HSSMEQDVGL
LRLYPGIPAA LVRAFLQPPL KGVVMETFGS GNGPTKPDLL QELRVATERG LVIVNCTHCL
QGAVTTDYAA GMAMAGAGVI SGFDMTSEAA LAKLSYVLGQ PGLSLDVRKE LLTKDLRGEM
TPPSVEERRP SLQGNTLGGG VSWLLSLSGS QEADALRNAL VPSLACAAAH AGDVEALQAL
VELGSDLGLV DFNGQTPLHA AARGGHTEAV TMLLQRGVDV NTRDTDGFSP LLLAVRGRHP
GVIGLLREAG ASLSTQELEE AGTELCRLAY RADLEGLQVW WQAGADLGQP GYDGHSALHV
AEAAGNLAVV AFLQSLEGAV GAQAPCPEVL PGV
