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Database: UniProt
Entry: A0A287CV85_ICTTR
LinkDB: A0A287CV85_ICTTR
Original site: A0A287CV85_ICTTR 
ID   A0A287CV85_ICTTR        Unreviewed;       172 AA.
AC   A0A287CV85;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Acyl-protein thioesterase 1 {ECO:0000256|ARBA:ARBA00014923};
DE            EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
DE   AltName: Full=Lysophospholipase 1 {ECO:0000256|ARBA:ARBA00042324};
DE   AltName: Full=Lysophospholipase I {ECO:0000256|ARBA:ARBA00042319};
DE   AltName: Full=Palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00031195};
GN   Name=LYPLA1 {ECO:0000313|Ensembl:ENSSTOP00000025186.1};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000025186.1, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000025186.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000256|ARBA:ARBA00000597};
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:0000256|ARBA:ARBA00036969};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721;
CC         Evidence={ECO:0000256|ARBA:ARBA00036969};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Nucleus membrane
CC       {ECO:0000256|ARBA:ARBA00004126}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000256|ARBA:ARBA00006499}.
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DR   EMBL; AGTP01027356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A287CV85; -.
DR   Ensembl; ENSSTOT00000043038.1; ENSSTOP00000025186.1; ENSSTOG00000015303.3.
DR   GeneTree; ENSGT00940000154185; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   PANTHER; PTHR10655:SF22; ACYL-PROTEIN THIOESTERASE 1; 1.
DR   PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN          1..167
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   172 AA;  18777 MW;  C1FD5F20CC2D449F CRC64;
     MPVTLNMKMA MPSWFDIIGL SPDAQEDEPG IKQAAENVKA LIDQEVKNGI PSNRIILGGF
     SQGGALSLYT ALTTQQKLAG VTALSCWLPL RASFPQSPIS GPNREISILQ CHGDCDPLVP
     LMFGSLTVEK LKTLVNPANV TFKIYEGMMH CSCQQEMMDV KQFIDKLLPP VD
//
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