ID   PPT2_BOVIN              Reviewed;         305 AA.
AC   Q1JQA0; Q58CW8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Lysosomal thioesterase PPT2;
DE            Short=PPT-2;
DE            EC=3.1.2.-;
DE   Flags: Precursor;
GN   Name=PPT2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) 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, is unable to remove palmitate from peptides or
CC       proteins (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX46676.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BT021829; AAX46676.1; ALT_FRAME; mRNA.
DR   EMBL; BC116122; AAI16123.1; -; mRNA.
DR   RefSeq; NP_001030395.2; NM_001035318.2.
DR   RefSeq; XP_005223714.1; XM_005223657.1.
DR   AlphaFoldDB; Q1JQA0; -.
DR   SMR; Q1JQA0; -.
DR   STRING; 9913.ENSBTAP00000005815; -.
DR   ESTHER; bovin-ppt2; Palmitoyl-protein_thioesterase.
DR   PaxDb; Q1JQA0; -.
DR   PRIDE; Q1JQA0; -.
DR   Ensembl; ENSBTAT00000005815; ENSBTAP00000005815; ENSBTAG00000004436.
DR   Ensembl; ENSBTAT00000074549; ENSBTAP00000070571; ENSBTAG00000004436.
DR   GeneID; 516797; -.
DR   KEGG; bta:516797; -.
DR   CTD; 9374; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004436; -.
DR   VGNC; VGNC:57311; PPT2.
DR   eggNOG; KOG2541; Eukaryota.
DR   GeneTree; ENSGT00940000155779; -.
DR   HOGENOM; CLU_050129_1_0_1; -.
DR   InParanoid; Q1JQA0; -.
DR   OMA; AWHTRRD; -.
DR   OrthoDB; 836806at2759; -.
DR   TreeFam; TF323926; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000004436; Expressed in granulosa cell and 104 other tissues.
DR   ExpressionAtlas; Q1JQA0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IPR002472; Palm_thioest.
DR   InterPro; IPR030295; PPT2.
DR   PANTHER; PTHR11247:SF27; PTHR11247:SF27; 1.
DR   PRINTS; PR00414; PPTHIESTRASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Reference proteome;
KW   Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..305
FT                   /note="Lysosomal thioesterase PPT2"
FT                   /id="PRO_0000247506"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        112..120
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..179
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..299
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34627 MW;  53BA780D38DDD748 CRC64;
     MLGLPERRLP SAEFLLLLPF LLLLLLLLPA APAPHRAAYK PVIVVHGLFD SSYSFRHLLE
     YINETHPGTA VTVLDLFDGR ESLRPLWEQV QGFREAVAPI MAKALQGVHL ICYSQGGLVC
     RALLSVMDEH NVDSFISLSS PQMGQYGDTN YLKWLFPTSM RSNLYRICYS PWGQEFSICN
     YWHDPHHDDL YLNASSFLAL INGERDHPNA TAWRKNFLRL GRLVLIGGPD DGVITPWQSS
     FFGFYDANET VLEMEKQLVY LRDSFGLKTL LARGAIVRCP MAGISHTAWH SNRTLYETCI
     EPWLS