LYPA2_RAT
ID LYPA2_RAT Reviewed; 231 AA.
AC Q9QYL8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 AltName: Full=Palmitoyl-protein hydrolase {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:O95372};
GN Name=Lypla2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sugimoto H.;
RT "Rat lysophospholipase II.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP PROTEIN SEQUENCE OF 165-190, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). Hydrolyzes prostaglandin
CC glycerol esters (PG-Gs) in the following order prostaglandin D2-
CC glycerol ester (PGD2-G) > prostaglandin E2 glycerol ester (PGE2-G) >
CC prostaglandin F2-alpha-glycerol ester (PGF2-alpha-G) (By similarity).
CC Hydrolyzes 1-arachidonoylglycerol but not 2-arachidonoylglycerol or
CC arachidonoylethanolamide (By similarity).
CC {ECO:0000250|UniProtKB:O95372, ECO:0000250|UniProtKB:Q9WTL7}.
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; AB021645; BAA87911.1; -; mRNA.
DR EMBL; BC070503; AAH70503.1; -; mRNA.
DR RefSeq; NP_112632.1; NM_031342.1.
DR AlphaFoldDB; Q9QYL8; -.
DR SMR; Q9QYL8; -.
DR STRING; 10116.ENSRNOP00000014415; -.
DR ChEMBL; CHEMBL3784905; -.
DR ESTHER; ratno-lypla2; LYsophospholipase_carboxylesterase.
DR iPTMnet; Q9QYL8; -.
DR PhosphoSitePlus; Q9QYL8; -.
DR SwissPalm; Q9QYL8; -.
DR jPOST; Q9QYL8; -.
DR PaxDb; Q9QYL8; -.
DR PRIDE; Q9QYL8; -.
DR Ensembl; ENSRNOT00000014415; ENSRNOP00000014415; ENSRNOG00000010067.
DR GeneID; 83510; -.
DR KEGG; rno:83510; -.
DR UCSC; RGD:620210; rat.
DR CTD; 11313; -.
DR RGD; 620210; Lypla2.
DR eggNOG; KOG2112; Eukaryota.
DR GeneTree; ENSGT00940000156197; -.
DR HOGENOM; CLU_049413_3_5_1; -.
DR InParanoid; Q9QYL8; -.
DR OMA; WYDILAM; -.
DR OrthoDB; 1373549at2759; -.
DR PhylomeDB; Q9QYL8; -.
DR TreeFam; TF314619; -.
DR Reactome; R-RNO-373760; L1CAM interactions.
DR PRO; PR:Q9QYL8; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000010067; Expressed in thymus and 20 other tissues.
DR Genevisible; Q9QYL8; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005795; C:Golgi stack; ISO:RGD.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; ISS: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_0000102273"
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:0007744|PubMed:22673903"
FT LIPID 2
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O95372"
SQ SEQUENCE 231 AA; 24807 MW; 49A710C5A997C7C1 CRC64;
MCGNNMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP
RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG
FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRNFPQAAN GSAKDLAILQ CHGELDPMVP
VRFGALTAEK LRTVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V
