ID PTH2_MOUSE Reviewed; 181 AA.
AC Q8R2Y8; Q8BI01; Q8BI31;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 151.
DE RecName: Full=Peptidyl-tRNA hydrolase 2, mitochondrial;
DE Short=PTH 2;
DE EC=3.1.1.29;
GN Name=Ptrh2; Synonyms=Pth2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 outer membrane
CC {ECO:0000250|UniProtKB:Q9Y3E5}; Single-pass membrane protein
CC {ECO:0000255}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26006.1; Type=Erroneous initiation; Evidence={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; AK028555; BAC26006.1; ALT_INIT; mRNA.
DR EMBL; AK031620; BAC27482.1; -; mRNA.
DR EMBL; AK038888; BAC30159.1; -; mRNA.
DR EMBL; BC026947; AAH26947.1; -; mRNA.
DR CCDS; CCDS48876.1; -.
DR RefSeq; NP_001092280.1; NM_001098810.2.
DR RefSeq; NP_778169.1; NM_175004.2.
DR AlphaFoldDB; Q8R2Y8; -.
DR SMR; Q8R2Y8; -.
DR BioGRID; 229838; 3.
DR STRING; 10090.ENSMUSP00000103656; -.
DR iPTMnet; Q8R2Y8; -.
DR PhosphoSitePlus; Q8R2Y8; -.
DR SwissPalm; Q8R2Y8; -.
DR EPD; Q8R2Y8; -.
DR jPOST; Q8R2Y8; -.
DR MaxQB; Q8R2Y8; -.
DR PaxDb; 10090-ENSMUSP00000103657; -.
DR PeptideAtlas; Q8R2Y8; -.
DR ProteomicsDB; 291620; -.
DR Pumba; Q8R2Y8; -.
DR Antibodypedia; 2479; 405 antibodies from 37 providers.
DR DNASU; 217057; -.
DR Ensembl; ENSMUST00000108021.2; ENSMUSP00000103656.2; ENSMUSG00000072582.10.
DR Ensembl; ENSMUST00000108022.8; ENSMUSP00000103657.2; ENSMUSG00000072582.10.
DR GeneID; 217057; -.
DR KEGG; mmu:217057; -.
DR UCSC; uc007ksy.1; mouse.
DR AGR; MGI:2444848; -.
DR CTD; 51651; -.
DR MGI; MGI:2444848; Ptrh2.
DR VEuPathDB; HostDB:ENSMUSG00000072582; -.
DR eggNOG; KOG3282; Eukaryota.
DR GeneTree; ENSGT00390000015991; -.
DR HOGENOM; CLU_073661_1_1_1; -.
DR InParanoid; Q8R2Y8; -.
DR OMA; GHAAVEC; -.
DR OrthoDB; 169876at2759; -.
DR PhylomeDB; Q8R2Y8; -.
DR TreeFam; TF324583; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 217057; 4 hits in 79 CRISPR screens.
DR PRO; PR:Q8R2Y8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R2Y8; Protein.
DR Bgee; ENSMUSG00000072582; Expressed in floor plate of midbrain and 255 other cell types or tissues.
DR Genevisible; Q8R2Y8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; ISO:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
DR CDD; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; Bit1; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR002833; PTH2.
DR NCBIfam; TIGR00283; arch_pth2; 1.
DR PANTHER; PTHR12649; PEPTIDYL-TRNA HYDROLASE 2; 1.
DR PANTHER; PTHR12649:SF11; PEPTIDYL-TRNA HYDROLASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; Peptidyl-tRNA hydrolase II; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..181
FT /note="Peptidyl-tRNA hydrolase 2, mitochondrial"
FT /id="PRO_0000029863"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E5"
FT CONFLICT 171
FT /note="I -> T (in Ref. 1; BAC30159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 19527 MW; C341176DE560C2B8 CRC64;
MLSKFLTMEY LVHPGTLSLA AGVACGMCLG WGLRSHLGMF PQNSTSEANR DTETGTEASI
LGESGEYKMI LVVRTDLKMG KGKVAAQCSH AAVSAYKQTQ RRSPQVLKEW EYCGQPKVVV
KAPDEDTLIQ LLTHAKTLGL TVSLIQDAGR TQIEPGSRTV LGIGPGPVEL IDEVTGHLKL
Y
//
