LYPA2_MOUSE
ID LYPA2_MOUSE Reviewed; 231 AA.
AC Q9WTL7; Q3TJD6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Acyl-protein thioesterase 2;
DE Short=APT-2;
DE EC=3.1.2.- {ECO:0000250|UniProtKB:O95372};
DE AltName: Full=Lysophospholipase 2;
DE AltName: Full=Lysophospholipase II;
DE Short=LPL-II;
DE Short=LysoPLA II;
DE Short=mLyso II;
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:O95372};
GN Name=Lypla2;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=10064901; DOI=10.1016/s1388-1981(99)00007-4;
RA Toyoda T., Sugimoto H., Yamashita S.;
RT "Sequence, expression in Escherichia coli, and characterization of
RT lysophospholipase II.";
RL Biochim. Biophys. Acta 1437:182-193(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, Placenta, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 PROTEIN SEQUENCE OF 154-164, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=25301951; DOI=10.1074/jbc.m114.582353;
RA Manna J.D., Wepy J.A., Hsu K.L., Chang J.W., Cravatt B.F., Marnett L.J.;
RT "Identification of the major prostaglandin glycerol ester hydrolase in
RT human cancer cells.";
RL J. Biol. Chem. 289:33741-33753(2014).
CC -!- FUNCTION: Acts as a acyl-protein thioesterase hydrolyzing fatty acids
CC from S-acylated cysteine residues in proteins such as trimeric G alpha
CC proteins, GAP43, ZDHHC6 or HRAS (By similarity). Deacylates GAP43 (By
CC similarity). Mediates depalmitoylation of ZDHHC6 (By similarity). Has
CC lysophospholipase activity (PubMed:10064901). Hydrolyzes prostaglandin
CC glycerol esters (PG-Gs) (PubMed:25301951). Hydrolyzes PG-Gs in the
CC following order prostaglandin D2-glycerol ester (PGD2-G) >
CC prostaglandin E2 glycerol ester (PGE2-G) > prostaglandin F2-alpha-
CC glycerol ester (PGF2-alpha-G) (By similarity). Hydrolyzes 1-
CC arachidonoylglycerol but not 2-arachidonoylglycerol or
CC arachidonoylethanolamide (By similarity).
CC {ECO:0000250|UniProtKB:O95372, ECO:0000269|PubMed:10064901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) +
CC prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230,
CC ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O95372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297;
CC Evidence={ECO:0000250|UniProtKB:O95372};
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:O95372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:O95372};
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:O95372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) +
CC hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64765, ChEBI:CHEBI:75020;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553;
CC Evidence={ECO:0000250|UniProtKB:O95372};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95372}.
CC -!- TISSUE SPECIFICITY: Ubiquitous; detected at low levels.
CC {ECO:0000269|PubMed:10064901}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; AB009653; BAA76751.1; -; mRNA.
DR EMBL; AK003689; BAB22940.1; -; mRNA.
DR EMBL; AK075590; BAC35841.1; -; mRNA.
DR EMBL; AK089112; BAC40757.1; -; mRNA.
DR EMBL; AK167478; BAE39559.1; -; mRNA.
DR EMBL; BC068120; AAH68120.1; -; mRNA.
DR CCDS; CCDS18797.1; -.
DR RefSeq; NP_036072.1; NM_011942.1.
DR AlphaFoldDB; Q9WTL7; -.
DR SMR; Q9WTL7; -.
DR BioGRID; 204948; 1.
DR STRING; 10090.ENSMUSP00000064204; -.
DR BindingDB; Q9WTL7; -.
DR ChEMBL; CHEMBL3259480; -.
DR ESTHER; mouse-lypla2; LYsophospholipase_carboxylesterase.
DR iPTMnet; Q9WTL7; -.
DR PhosphoSitePlus; Q9WTL7; -.
DR SwissPalm; Q9WTL7; -.
DR REPRODUCTION-2DPAGE; IPI00123518; -.
DR REPRODUCTION-2DPAGE; Q9WTL7; -.
DR EPD; Q9WTL7; -.
DR jPOST; Q9WTL7; -.
DR MaxQB; Q9WTL7; -.
DR PaxDb; Q9WTL7; -.
DR PeptideAtlas; Q9WTL7; -.
DR PRIDE; Q9WTL7; -.
DR ProteomicsDB; 252689; -.
DR Antibodypedia; 30196; 176 antibodies from 25 providers.
DR DNASU; 26394; -.
DR Ensembl; ENSMUST00000067567; ENSMUSP00000064204; ENSMUSG00000028670.
DR Ensembl; ENSMUST00000105852; ENSMUSP00000101478; ENSMUSG00000028670.
DR GeneID; 26394; -.
DR KEGG; mmu:26394; -.
DR UCSC; uc008vhm.2; mouse.
DR CTD; 11313; -.
DR MGI; MGI:1347000; Lypla2.
DR VEuPathDB; HostDB:ENSMUSG00000028670; -.
DR eggNOG; KOG2112; Eukaryota.
DR GeneTree; ENSGT00940000156197; -.
DR HOGENOM; CLU_049413_3_5_1; -.
DR InParanoid; Q9WTL7; -.
DR OMA; WYDILAM; -.
DR OrthoDB; 1373549at2759; -.
DR PhylomeDB; Q9WTL7; -.
DR TreeFam; TF314619; -.
DR BRENDA; 3.1.1.5; 3474.
DR Reactome; R-MMU-373760; L1CAM interactions.
DR BioGRID-ORCS; 26394; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lypla2; mouse.
DR PRO; PR:Q9WTL7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WTL7; protein.
DR Bgee; ENSMUSG00000028670; Expressed in embryonic brain and 241 other tissues.
DR Genevisible; Q9WTL7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1905344; P:prostaglandin catabolic process; IDA:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Lipoprotein; Palmitate; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..231
FT /note="Acyl-protein thioesterase 2"
FT /id="PRO_0000102272"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O95372"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYL8"
FT LIPID 2
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O95372"
SQ SEQUENCE 231 AA; 24794 MW; E18797A17570AA97 CRC64;
MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP
RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG
FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRNFPQAAN GSAKDLAILQ CHGELDPMVP
VRFGALTAEK LRTVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V
