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PPT2_RAT
ID   PPT2_RAT                Reviewed;         302 AA.
AC   O70489; O88500;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Lysosomal thioesterase PPT2;
DE            Short=PPT-2;
DE            EC=3.1.2.-;
DE   Flags: Precursor;
GN   Name=Ppt2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RA   Kuznetsov S.R., Jones T.L.Z.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70489-1; Sequence=Displayed;
CC       Name=2; Synonyms=Truncated;
CC         IsoId=O70489-2; Sequence=VSP_005189, VSP_005190;
CC   -!- SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.
CC       {ECO:0000305}.
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DR   EMBL; AF061971; AAC16003.1; -; mRNA.
DR   EMBL; AF067790; AAC19366.1; -; mRNA.
DR   EMBL; BX883044; CAE83963.1; -; Genomic_DNA.
DR   EMBL; BC062023; AAH62023.1; -; mRNA.
DR   RefSeq; NP_062240.1; NM_019367.2. [O70489-1]
DR   RefSeq; XP_006256079.2; XM_006256017.2. [O70489-1]
DR   RefSeq; XP_006256080.1; XM_006256018.3. [O70489-1]
DR   RefSeq; XP_006256081.1; XM_006256019.3. [O70489-1]
DR   RefSeq; XP_006256082.1; XM_006256020.3. [O70489-1]
DR   RefSeq; XP_006256084.1; XM_006256022.3. [O70489-1]
DR   RefSeq; XP_006256085.1; XM_006256023.3. [O70489-1]
DR   RefSeq; XP_008770984.1; XM_008772762.2. [O70489-1]
DR   RefSeq; XP_017457255.1; XM_017601766.1. [O70489-1]
DR   RefSeq; XP_017457256.1; XM_017601767.1. [O70489-1]
DR   AlphaFoldDB; O70489; -.
DR   SMR; O70489; -.
DR   STRING; 10116.ENSRNOP00000000497; -.
DR   ESTHER; ratno-PPT2; Palmitoyl-protein_thioesterase.
DR   GlyGen; O70489; 5 sites.
DR   jPOST; O70489; -.
DR   PaxDb; O70489; -.
DR   Ensembl; ENSRNOT00000080476; ENSRNOP00000074687; ENSRNOG00000000435. [O70489-1]
DR   GeneID; 54398; -.
DR   KEGG; rno:54398; -.
DR   UCSC; RGD:620375; rat. [O70489-1]
DR   CTD; 9374; -.
DR   RGD; 620375; Ppt2.
DR   eggNOG; KOG2541; Eukaryota.
DR   GeneTree; ENSGT00940000155779; -.
DR   HOGENOM; CLU_050129_1_0_1; -.
DR   InParanoid; O70489; -.
DR   OMA; AWHTRRD; -.
DR   OrthoDB; 836806at2759; -.
DR   PhylomeDB; O70489; -.
DR   TreeFam; TF323926; -.
DR   Reactome; R-RNO-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:O70489; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000435; Expressed in thymus and 18 other tissues.
DR   ExpressionAtlas; O70489; baseline and differential.
DR   Genevisible; O70489; RN.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0098599; F:palmitoyl hydrolase activity; ISO:RGD.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IEA:InterPro.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IBA:GO_Central.
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   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW   Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..302
FT                   /note="Lysosomal thioesterase PPT2"
FT                   /id="PRO_0000025556"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        165..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..296
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         155..158
FT                   /note="TSMR -> FCHG (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_005189"
FT   VAR_SEQ         159..302
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_005190"
SQ   SEQUENCE   302 AA;  34355 MW;  BD0812801E813A7D CRC64;
     MPGLWRQRLP SAWALLLLPF LPLLLPAAPA PHRGSYKPVI VVHGLFDSSY SFRHLLDYIN
     ETHPGTVVTV LDLFDGRESL RPLWEQVQGF REAVVPIMEK APEGVHLICY SQGGLVCRAL
     LSVMDEHNVD SFISLSSPQM GQYGDTDYLK WLFPTSMRSN LYRICYSPWG QEFSICNYWH
     DPHHDDLYLN ASSFLALING ERDHPNATAW RKNFLRVGRL VLIGGPDDGV ITPWQSSFFG
     FYDANETVLE MEEQPVYLRD SFGLKTLLAR GAIVRCPMAG VSHTTWHSNR TLYDACIEPW
     LS
 
 
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