LYPA1_RAT
ID LYPA1_RAT Reviewed; 230 AA.
AC P70470;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Acyl-protein thioesterase 1;
DE Short=APT-1;
DE EC=3.1.2.-;
DE AltName: Full=Lysophospholipase 1;
DE AltName: Full=Lysophospholipase I;
DE Short=LPL-I;
DE Short=LysoPLA I;
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:O75608};
GN Name=Lypla1; Synonyms=Apt1;
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], PROTEIN SEQUENCE OF 20-30 AND 192-196,
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8631810; DOI=10.1074/jbc.271.13.7705;
RA Sugimoto H., Hayashi H., Yamashita S.;
RT "Purification, cDNA cloning, and regulation of lysophospholipase from rat
RT liver.";
RL J. Biol. Chem. 271:7705-7711(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=9644627; DOI=10.1681/asn.v971178;
RA Portilla D., Crew M.D., Grant D., Serrero G., Bates L.M., Dai G.,
RA Sasner M., Cheng J., Buonanno A.;
RT "cDNA cloning and expression of a novel family of enzymes with calcium-
RT independent phospholipase A2 and lysophospholipase activities.";
RL J. Am. Soc. Nephrol. 9:1178-1186(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 98-112 AND 191-201, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9624183; DOI=10.1074/jbc.273.25.15830;
RA Duncan J.A., Gilman A.G.;
RT "A cytoplasmic acyl-protein thioesterase that removes palmitate from G
RT protein alpha subunits and p21(RAS).";
RL J. Biol. Chem. 273:15830-15837(1998).
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 or HRAS (PubMed:9624183). Has depalmitoylating activity toward
CC KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By
CC similarity). Acts as a lysophospholipase hydrolyzing various
CC lysophospholipids including lysophosphatidylcholine (lyso-PC),
CC lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-
CC PI) and lysophosphatidylserine (lyso-PS) (PubMed:8631810,
CC PubMed:9644627). Has much higher thioesterase activity than
CC lysophospholipase activity (By similarity). Contributes to the
CC production of lysophosphatidic acid (LPA) during blood coagulation by
CC recognizing and cleaving plasma phospholipids to generate
CC lysophospholipids which in turn act as substrates for ENPP2 to produce
CC LPA (By similarity). {ECO:0000250|UniProtKB:O75608,
CC ECO:0000269|PubMed:8631810, ECO:0000269|PubMed:9624183,
CC ECO:0000269|PubMed:9644627}.
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:O75608};
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:O75608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:O75608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O
CC = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:41720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57875, ChEBI:CHEBI:78421;
CC Evidence={ECO:0000250|UniProtKB:O75608};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721;
CC Evidence={ECO:0000250|UniProtKB:O75608};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75608}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9624183}. Cell
CC membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane
CC {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic
CC localization with a weak expression in the cell membrane, nuclear
CC membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected at low levels in all tissues
CC tested. {ECO:0000269|PubMed:8631810, ECO:0000269|PubMed:9644627}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; D63885; BAA09935.1; -; mRNA.
DR EMBL; U97146; AAC63430.1; -; mRNA.
DR EMBL; BC085750; AAH85750.1; -; mRNA.
DR RefSeq; NP_037138.1; NM_013006.1.
DR AlphaFoldDB; P70470; -.
DR SMR; P70470; -.
DR BioGRID; 247546; 1.
DR IntAct; P70470; 1.
DR STRING; 10116.ENSRNOP00000011312; -.
DR BindingDB; P70470; -.
DR ChEMBL; CHEMBL2280; -.
DR ESTHER; ratno-lypla1a; LYsophospholipase_carboxylesterase.
DR iPTMnet; P70470; -.
DR PhosphoSitePlus; P70470; -.
DR SwissPalm; P70470; -.
DR jPOST; P70470; -.
DR PaxDb; P70470; -.
DR PRIDE; P70470; -.
DR Ensembl; ENSRNOT00000117962; ENSRNOP00000083839; ENSRNOG00000008320.
DR GeneID; 25514; -.
DR KEGG; rno:25514; -.
DR UCSC; RGD:3025; rat.
DR CTD; 10434; -.
DR RGD; 3025; Lypla1.
DR eggNOG; KOG2112; Eukaryota.
DR GeneTree; ENSGT00940000154185; -.
DR HOGENOM; CLU_049413_3_5_1; -.
DR InParanoid; P70470; -.
DR OMA; QPIGGIM; -.
DR OrthoDB; 1373549at2759; -.
DR PhylomeDB; P70470; -.
DR TreeFam; TF314619; -.
DR Reactome; R-RNO-203615; eNOS activation.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:P70470; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008320; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; P70470; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; ISO:RGD.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:RGD.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; ISO:RGD.
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 Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Membrane; Nucleus; Reference proteome.
FT CHAIN 1..230
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000102270"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MOD_RES 224
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97823"
SQ SEQUENCE 230 AA; 24709 MW; AAFE8C4702EAAD74 CRC64;
MCGNNMSAPM PAVVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIKSSHIK YICPHAPVMP
VTLNMSMMMP SWFDIIGLSP DSQEDESGIK QAAETVKALI DQEVKNGIPS NRIILGGFSQ
GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFSQGPINSA NRDISVLQCH GDCDPLVPLM
FGSLTVERLK GLVNPANVTF KVYEGMMHSS CQQEMMDVKY FIDKLLPPID
