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Database: UniProt
Entry: F6SPC5_MACMU
LinkDB: F6SPC5_MACMU
Original site: F6SPC5_MACMU 
ID   F6SPC5_MACMU            Unreviewed;       208 AA.
AC   F6SPC5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 53.
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:ENSMMUP00000032103.3,
GN   ECO:0000313|VGNC:VGNC:84014};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000032103.3, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000032103.3}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000032103.3};
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   RefSeq; XP_015000850.1; XM_015145364.1.
DR   AlphaFoldDB; F6SPC5; -.
DR   SMR; F6SPC5; -.
DR   Ensembl; ENSMMUT00000039024.3; ENSMMUP00000032103.3; ENSMMUG00000013157.4.
DR   GeneID; 693700; -.
DR   CTD; 10434; -.
DR   VEuPathDB; HostDB:ENSMMUG00000013157; -.
DR   VGNC; VGNC:84014; LYPLA1.
DR   GeneTree; ENSGT00940000154185; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000006718; Chromosome 8.
DR   Bgee; ENSMMUG00000013157; Expressed in ileum and 22 other cell types or tissues.
DR   ExpressionAtlas; F6SPC5; baseline.
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:UP000006718}.
FT   DOMAIN          34..203
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   208 AA;  22282 MW;  D10A5EE1AD8754C4 CRC64;
     MCGNNMSTPL PAIVPAARKA TAAVIFLHGL GDTGPVRPVT LNMNMAMPSW FDIIGLSPDS
     QEDESGIKQA AENIKALIDQ EVKNGIPSNR IILGGFSQGG ALSLYTALTT QQKLAGVTAL
     SCWLPLRASF PQGPVGGANR DISILQCHGD CDPLVPLMFG SLTVEKLKTL VNPVNVTFKT
     YEGMMHSSCQ QEMMDVKQFI DKLLPPID
//
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