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}.
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; 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