LYPA1_RABIT
ID LYPA1_RABIT Reviewed; 230 AA.
AC O77821;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Acyl-protein thioesterase 1;
DE Short=APT-1;
DE EC=3.1.2.-;
DE AltName: Full=Calcium-independent phospholipase A2;
DE Short=CaIPLA2;
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 98-103; 150-161 AND
RP 191-201.
RC TISSUE=Kidney;
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).
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; U97148; AAC63432.1; -; mRNA.
DR RefSeq; NP_001103287.1; NM_001109817.1.
DR AlphaFoldDB; O77821; -.
DR SMR; O77821; -.
DR STRING; 9986.ENSOCUP00000005836; -.
DR ESTHER; rabit-lypla1; LYsophospholipase_carboxylesterase.
DR GeneID; 100125992; -.
DR KEGG; ocu:100125993; -.
DR CTD; 10434; -.
DR eggNOG; KOG2112; Eukaryota.
DR InParanoid; O77821; -.
DR OrthoDB; 1373549at2759; -.
DR Proteomes; UP000001811; 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 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_0000102269"
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; 24688 MW; 89AF2017AEFC9FAC CRC64;
MCGNNMSAPM PAVVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIKSPHIK YICPHAPVMP
VTLNMNMAMP SWFDIVGLSP DSQEDESGIK QAAETVKALI DQEVKNGIPS NRIILGGFSQ
GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFSQGPINSA NRDISVLQCH GDCDPLVPLM
FGSLTVERLK ALINPANVTF KIYEGMMHSS CQQEMMDVKH FIDKLLPPID
