PTH2_BOVIN
ID PTH2_BOVIN Reviewed; 179 AA.
AC Q3ZBL5; Q05KI4; Q5BIN3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Peptidyl-tRNA hydrolase 2, mitochondrial;
DE Short=PTH 2;
DE EC=3.1.1.29;
DE AltName: Full=Bcl-2 inhibitor of transcription;
DE Flags: Precursor;
GN Name=PTRH2; Synonyms=BIT1;
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 [MRNA].
RC TISSUE=Placenta;
RA Ushizawa K., Takahashi T., Hosoe M., Hashizume K.;
RT "Expression of Bcl-2 family in bovine placenta.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC EC=3.1.1.29;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000250|UniProtKB:Q9Y3E5}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000305}.
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DR EMBL; AB238942; BAF35578.1; -; mRNA.
DR EMBL; BT021191; AAX31373.1; -; mRNA.
DR EMBL; BC103230; AAI03231.1; -; mRNA.
DR RefSeq; NP_001029691.1; NM_001034519.1.
DR RefSeq; XP_005219951.1; XM_005219894.3.
DR AlphaFoldDB; Q3ZBL5; -.
DR SMR; Q3ZBL5; -.
DR STRING; 9913.ENSBTAP00000022212; -.
DR PaxDb; Q3ZBL5; -.
DR PeptideAtlas; Q3ZBL5; -.
DR PRIDE; Q3ZBL5; -.
DR Ensembl; ENSBTAT00000022212; ENSBTAP00000022212; ENSBTAG00000016710.
DR GeneID; 516595; -.
DR KEGG; bta:516595; -.
DR CTD; 51651; -.
DR VEuPathDB; HostDB:ENSBTAG00000016710; -.
DR VGNC; VGNC:33562; PTRH2.
DR eggNOG; KOG3282; Eukaryota.
DR GeneTree; ENSGT00390000015991; -.
DR HOGENOM; CLU_073661_1_1_1; -.
DR InParanoid; Q3ZBL5; -.
DR OMA; GHAAVEC; -.
DR OrthoDB; 1564104at2759; -.
DR TreeFam; TF324583; -.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000016710; Expressed in semen and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
DR GO; GO:2000811; P:negative regulation of anoikis; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:2000210; P:positive regulation of anoikis; IBA:GO_Central.
DR CDD; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; -; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR002833; PTH2.
DR PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Isopeptide bond; Mitochondrion; Reference proteome;
KW Transit peptide; Ubl conjugation.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 63..179
FT /note="Peptidyl-tRNA hydrolase 2, mitochondrial"
FT /id="PRO_0000240443"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CONFLICT 20
FT /note="A -> V (in Ref. 2; AAX31373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 19291 MW; 8FC2E82B73B7BC02 CRC64;
MISRSLVMEY LTNPGALSLA AGVACGVCLG WGLRMRFGML PKSSVRETNP DTETEASILG
ESGEYKMILV VRNDLKMGKG KVAAQCSHAA VSAYKQIQRR NPELLKEWEY CGQPKVVVKA
PDEETLVELL THAKVLGLTV SLIQDAGRTQ IAPGSRTVLG IGPGPADLID KVTGHLKLY