ICT1_MOUSE
ID ICT1_MOUSE Reviewed; 206 AA.
AC Q8R035; A2A6T2; A2A6T3; Q3TUL0; Q9CTK1; Q9D1R3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peptidyl-tRNA hydrolase ICT1, mitochondrial;
DE EC=3.1.1.29;
DE AltName: Full=39S ribosomal protein L58, mitochondrial {ECO:0000312|MGI:MGI:1915822};
DE Short=MRP-L58;
DE AltName: Full=Immature colon carcinoma transcript 1 protein homolog;
DE Flags: Precursor;
GN Name=Mrpl58 {ECO:0000312|MGI:MGI:1915822}; Synonyms=Ict1;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 37-206 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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).
RN [6]
RP STRUCTURE BY NMR OF 63-162, AND FUNCTION.
RX PubMed=20869366; DOI=10.1016/j.jmb.2010.09.033;
RA Handa Y., Hikawa Y., Tochio N., Kogure H., Inoue M., Koshiba S.,
RA Guntert P., Inoue Y., Kigawa T., Yokoyama S., Nameki N.;
RT "Solution structure of the catalytic domain of the mitochondrial protein
RT ICT1 that is essential for cell vitality.";
RL J. Mol. Biol. 404:260-273(2010).
CC -!- FUNCTION: Essential peptidyl-tRNA hydrolase component of the
CC mitochondrial large ribosomal subunit (PubMed:20869366). Acts as a
CC codon-independent translation release factor that has lost all stop
CC codon specificity and directs the termination of translation in
CC mitochondrion, possibly in case of abortive elongation. May be involved
CC in the hydrolysis of peptidyl-tRNAs that have been prematurely
CC terminated and thus in the recycling of stalled mitochondrial ribosomes
CC (By similarity). {ECO:0000250|UniProtKB:Q14197,
CC ECO:0000269|PubMed:20869366}.
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: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins.
CC {ECO:0000250|UniProtKB:Q14197}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q14197}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R035-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R035-2; Sequence=VSP_014374;
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. Mitochondrion-specific ribosomal protein mL62 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the regions
CC that come into close contact with the mRNA in the ribosomal A-site and
CC determine the STOP codon specificity, explaining the loss of codon
CC specificity for translation release factor activity. {ECO:0000305}.
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DR EMBL; AK003192; BAB22632.1; -; mRNA.
DR EMBL; AK003286; BAB22691.1; -; mRNA.
DR EMBL; AK160697; BAE35961.1; -; mRNA.
DR EMBL; AL603828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34481.1; -; Genomic_DNA.
DR EMBL; CH466558; EDL34486.1; -; Genomic_DNA.
DR EMBL; BC028523; AAH28523.1; -; mRNA.
DR CCDS; CCDS25632.1; -. [Q8R035-2]
DR CCDS; CCDS83928.1; -. [Q8R035-1]
DR RefSeq; NP_001334574.1; NM_001347645.1. [Q8R035-1]
DR RefSeq; NP_081005.1; NM_026729.1. [Q8R035-2]
DR PDB; 1J26; NMR; -; A=63-161.
DR PDBsum; 1J26; -.
DR AlphaFoldDB; Q8R035; -.
DR BMRB; Q8R035; -.
DR SMR; Q8R035; -.
DR BioGRID; 212934; 87.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000116746; -.
DR iPTMnet; Q8R035; -.
DR PhosphoSitePlus; Q8R035; -.
DR EPD; Q8R035; -.
DR jPOST; Q8R035; -.
DR MaxQB; Q8R035; -.
DR PeptideAtlas; Q8R035; -.
DR PRIDE; Q8R035; -.
DR ProteomicsDB; 267187; -. [Q8R035-1]
DR ProteomicsDB; 267188; -. [Q8R035-2]
DR Antibodypedia; 1066; 334 antibodies from 30 providers.
DR DNASU; 68572; -.
DR Ensembl; ENSMUST00000103036; ENSMUSP00000099325; ENSMUSG00000018858. [Q8R035-2]
DR Ensembl; ENSMUST00000153983; ENSMUSP00000116746; ENSMUSG00000018858. [Q8R035-1]
DR GeneID; 68572; -.
DR KEGG; mmu:68572; -.
DR UCSC; uc007mhj.1; mouse. [Q8R035-1]
DR UCSC; uc007mhl.1; mouse. [Q8R035-2]
DR CTD; 3396; -.
DR MGI; MGI:1915822; Mrpl58.
DR VEuPathDB; HostDB:ENSMUSG00000018858; -.
DR eggNOG; KOG3429; Eukaryota.
DR GeneTree; ENSGT00390000013268; -.
DR HOGENOM; CLU_089470_6_1_1; -.
DR InParanoid; Q8R035; -.
DR OMA; IIRSQEA; -.
DR OrthoDB; 1611415at2759; -.
DR PhylomeDB; Q8R035; -.
DR TreeFam; TF315161; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 68572; 4 hits in 60 CRISPR screens.
DR EvolutionaryTrace; Q8R035; -.
DR PRO; PR:Q8R035; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R035; protein.
DR Bgee; ENSMUSG00000018858; Expressed in thymus and 263 other tissues.
DR ExpressionAtlas; Q8R035; baseline and differential.
DR Genevisible; Q8R035; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0070126; P:mitochondrial translational termination; ISS:UniProtKB.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR Pfam; PF00472; RF-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Mitochondrion;
KW Protein biosynthesis; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..206
FT /note="Peptidyl-tRNA hydrolase ICT1, mitochondrial"
FT /id="PRO_0000030340"
FT VAR_SEQ 34..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014374"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1J26"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1J26"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1J26"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1J26"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1J26"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1J26"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:1J26"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:1J26"
FT HELIX 143..161
FT /evidence="ECO:0007829|PDB:1J26"
SQ SEQUENCE 206 AA; 23477 MW; 1B898BE6A559E1F0 CRC64;
MATAWGLRWG LSRTGTLLLA PPARCARRAL HRQVDGTTFQ SIYSLDKLYP ESKGADTAWK
VPEHAKQASS YIPLDRLSIS YCRSSGPGGQ NVNKVNSKAE VRFHLASADW IEEPVRQKIA
LTHKNKINKA GELVLTSESS RYQFRNLAEC LQKIRDMIAE ASQVPKEPSK EDARLQRLRI
EKMNRERLRQ KRLNSALKTS RRMTMD
