LYPA1_PONAB
ID LYPA1_PONAB Reviewed; 230 AA.
AC Q5RBR7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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) (By similarity). Has much
CC higher thioesterase activity than lysophospholipase activity (By
CC similarity). Contributes to the production of lysophosphatidic acid
CC (LPA) during blood coagulation by recognizing and cleaving plasma
CC phospholipids to generate lysophospholipids which in turn act as
CC substrates for ENPP2 to produce LPA (By similarity).
CC {ECO:0000250|UniProtKB:O75608, ECO:0000250|UniProtKB:P70470}.
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:0000250|UniProtKB:O75608}. 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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
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DR EMBL; CR858568; CAH90793.1; -; mRNA.
DR RefSeq; NP_001125450.1; NM_001131978.1.
DR AlphaFoldDB; Q5RBR7; -.
DR SMR; Q5RBR7; -.
DR STRING; 9601.ENSPPYP00000020848; -.
DR ESTHER; ponpy-lypa1; LYsophospholipase_carboxylesterase.
DR MEROPS; S09.941; -.
DR GeneID; 100172358; -.
DR KEGG; pon:100172358; -.
DR CTD; 10434; -.
DR eggNOG; KOG2112; Eukaryota.
DR InParanoid; Q5RBR7; -.
DR OrthoDB; 1373549at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Fatty acid metabolism; Hydrolase; Lipid metabolism; Membrane; Nucleus;
KW Reference proteome.
FT CHAIN 1..230
FT /note="Acyl-protein thioesterase 1"
FT /id="PRO_0000238675"
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; 24702 MW; E7DC3F90C8AD9997 CRC64;
MCGNNMSTPL PAIVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIRSSHIK YICPHAPVRP
VTLNMNMAMP SWFDIIGLSP DSQEDESGIK QAAENIKALI DQEVKNGIPS NRIILGGFSQ
GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFPQGPIGGA NRDISILQCH GDCDPLVPLM
FGSLTVEKLK TLVNPANVTF KTYEGMMHSS CQQEMMDVKQ FIDKLLPPID
