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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
 
 
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