ID   PPT2A_XENLA             Reviewed;         296 AA.
AC   Q6PCJ9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Lysosomal thioesterase PPT2-A;
DE            Short=PPT-2-A;
DE            EC=3.1.2.-;
DE   Flags: Precursor;
GN   Name=ppt2-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes thioester-linked fatty acyl groups from various
CC       substrates including S-palmitoyl-CoA. Has the highest S-thioesterase
CC       activity for the acyl groups palmitic and myristic acid followed by
CC       other short- and long-chain acyl substrates. However, because of
CC       structural constraints, may be unable to remove palmitate from peptides
CC       or proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC       {ECO:0000305}.
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DR   EMBL; BC059297; AAH59297.1; -; mRNA.
DR   RefSeq; NP_001079999.1; NM_001086530.1.
DR   RefSeq; XP_018084103.1; XM_018228614.1.
DR   AlphaFoldDB; Q6PCJ9; -.
DR   SMR; Q6PCJ9; -.
DR   ESTHER; xenla-q6pcj9; Palmitoyl-protein_thioesterase.
DR   MaxQB; Q6PCJ9; -.
DR   DNASU; 379689; -.
DR   GeneID; 379689; -.
DR   KEGG; xla:379689; -.
DR   CTD; 379689; -.
DR   Xenbase; XB-GENE-865230; ppt2.L.
DR   OMA; AWHTRRD; -.
DR   OrthoDB; 836806at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 379689; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR030295; PPT2.
DR   PANTHER; PTHR11247:SF27; PTHR11247:SF27; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Reference proteome;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..296
FT                   /note="Lysosomal thioesterase PPT2-A"
FT                   /id="PRO_0000247507"
FT   ACT_SITE        105
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        159..170
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  34096 MW;  9EB7EB750AF0ED66 CRC64;
     MTASRPKALQ TFCLLLPLLV WMVDRSLCYK PVIVVHGLFD SSANFKNLLQ YINESHPGTN
     VTVLDLFDNK ESLQPLWKQV QGFKEAIYPI MQNAGRDGVH LLCYSQGGLI CRGLLQTMPD
     HNVDTFISLS SPQMGQYGDT DYLRYLFPTY VKSNLYRLCY TQMGQTFSIC NFWNDPHHHG
     IYVNVSDFLA PLNSERPEPN ATDWKKNFLR LRKMVLIGGP DDGVITPWES SHFGFYDENE
     TVLEMKYQMV YQDDTFGLRS MDYRGAITVY GVPGVVHTMW HSNQTVFKNC IEKWLT