ID   PPT2B_XENLA             Reviewed;         288 AA.
AC   Q6GNY7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Lysosomal thioesterase PPT2-B;
DE            Short=PPT-2-B;
DE            EC=3.1.2.-;
DE   Flags: Precursor;
GN   Name=ppt2-b;
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=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC073363; AAH73363.1; -; mRNA.
DR   RefSeq; NP_001085801.1; NM_001092332.1.
DR   AlphaFoldDB; Q6GNY7; -.
DR   SMR; Q6GNY7; -.
DR   ESTHER; xenla-q6gny7; Palmitoyl-protein_thioesterase.
DR   PRIDE; Q6GNY7; -.
DR   GeneID; 444228; -.
DR   KEGG; xla:444228; -.
DR   CTD; 444228; -.
DR   Xenbase; XB-GENE-6255702; ppt2l.L.
DR   OMA; HGISAEC; -.
DR   OrthoDB; 836806at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 444228; Expressed in spleen 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..288
FT                   /note="Lysosomal thioesterase PPT2-B"
FT                   /id="PRO_0000247508"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        151..162
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  33195 MW;  44DE073730259394 CRC64;
     MRGYLLLLPL LLCLVDNSVS YKPVILVHGL LSSSKSFDKL IQFIKKAHPG TDIYPVDMFN
     HLKSLNPMWK QVYEIRKYIS PIIKNAGLKG VHLICYSQGG LICRGLLETM PEHNVDTFIA
     LSSPLMGQYG MTLYVQKALP LVNISALQEV CYRKFFKEIS ICGYWRDPHR YEKYLEYSAF
     LPKLNNELLD SNSTERKRNF LRLRKLVLIG GPDDEVIAPW QSSHFGFYNE KEEVVNMKDQ
     MVYQKDTFGL QSLDGRGAIT IYSVPGVLHA SWPNNQTVFK NYIEKWLT