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Database: UniProt
Entry: LYPL1_PONAB
LinkDB: LYPL1_PONAB
Original site: LYPL1_PONAB 
ID   LYPL1_PONAB             Reviewed;         237 AA.
AC   Q5R8C2; Q5RB27;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Lysophospholipase-like protein 1 {ECO:0000250|UniProtKB:Q5VWZ2};
DE            EC=3.1.2.22 {ECO:0000250|UniProtKB:Q5VWZ2};
GN   Name=LYPLAL1 {ECO:0000250|UniProtKB:Q5VWZ2};
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Heart, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Palmitoyl thioesterase that catalyzes depalmitoylation of
CC       CGAS and KCNMA1. Acts as a regulator of innate immunity by mediating
CC       depalmitoylation of CGAS, thereby preventing CGAS homodimerization and
CC       cyclic GMP-AMP synthase activity. Does not exhibit phospholipase nor
CC       triacylglycerol lipase activity, able to hydrolyze only short chain
CC       substrates due to its shallow active site.
CC       {ECO:0000250|UniProtKB:Q5VWZ2}.
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:Q5VWZ2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC         Evidence={ECO:0000250|UniProtKB:Q5VWZ2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q5VWZ2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5R8C2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5R8C2-2; Sequence=VSP_017557;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
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DR   EMBL; CR858831; CAH91033.1; -; mRNA.
DR   EMBL; CR859831; CAH91988.1; -; mRNA.
DR   RefSeq; NP_001126154.1; NM_001132682.1. [Q5R8C2-1]
DR   RefSeq; NP_001128798.1; NM_001135326.1.
DR   RefSeq; XP_009235805.1; XM_009237530.1. [Q5R8C2-1]
DR   AlphaFoldDB; Q5R8C2; -.
DR   SMR; Q5R8C2; -.
DR   STRING; 9601.ENSPPYP00000000218; -.
DR   ESTHER; ponpy-lypl1; LYsophospholipase_carboxylesterase.
DR   Ensembl; ENSPPYT00000000233.2; ENSPPYP00000000218.2; ENSPPYG00000000212.3. [Q5R8C2-1]
DR   GeneID; 100173113; -.
DR   GeneID; 100189704; -.
DR   KEGG; pon:100189704; -.
DR   CTD; 127018; -.
DR   eggNOG; KOG2112; Eukaryota.
DR   GeneTree; ENSGT00940000159171; -.
DR   InParanoid; Q5R8C2; -.
DR   OMA; LEYPHIK; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0160049; P:negative regulation of cGAS/STING signaling pathway; ISS:UniProtKB.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   PANTHER; PTHR10655:SF71; LYSOPHOSPHOLIPASE-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT   CHAIN           2..237
FT                   /note="Lysophospholipase-like protein 1"
FT                   /id="PRO_0000227559"
FT   ACT_SITE        124
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:O75608"
FT   ACT_SITE        179
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT   VAR_SEQ         1..68
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_017557"
FT   CONFLICT        227
FT                   /note="T -> R (in Ref. 1; CAH91033)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   237 AA;  26299 MW;  041C69EC618BEE5B CRC64;
     MAAASASVLQ RCIVSPAGRH SASLIFLHGS GDSGQGLRMW IKQVLNQDLT FQHIKIIYPT
     APPRSYTPMK GGISNVWFDR FKITNDCPEH LESIDVMCQV LTDLIDEEVK SGIKKNRILI
     GGFSMGGSMA MHLAYRNHQD VAGVFALSSF LNKASAVYQA LQKSNGVLPE LFQCHGTADE
     LVLHSWAEET NSMLKSLGVT TKLHSFPDVY HELSKTELDI LKLWILTKLP GEMEKQK
//
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