ICT1_HUMAN
ID ICT1_HUMAN Reviewed; 206 AA.
AC Q14197; B2RAD1; Q53HM7; Q53Y11;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Peptidyl-tRNA hydrolase ICT1, mitochondrial {ECO:0000305};
DE EC=3.1.1.29 {ECO:0000269|PubMed:20186120};
DE AltName: Full=39S ribosomal protein L58, mitochondrial {ECO:0000312|HGNC:HGNC:5359};
DE Short=MRP-L58;
DE AltName: Full=Digestion substraction 1;
DE Short=DS-1;
DE AltName: Full=Immature colon carcinoma transcript 1 protein;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL62 {ECO:0000303|PubMed:27023846};
DE Flags: Precursor;
GN Name=MRPL58 {ECO:0000312|HGNC:HGNC:5359}; Synonyms=DS1, ICT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8575443; DOI=10.1111/j.1432-1033.1995.843_a.x;
RA van Belzen N., Diesveld M.P.G., van der Made A.C.J., Nozawa Y.,
RA Dinjens W.N.M., Vlietstra R., Trapman J., Bosman F.T.;
RT "Identification of mRNAs that show modulated expression during colon
RT carcinoma cell differentiation.";
RL Eur. J. Biochem. 234:843-848(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [7]
RP FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL 39S RIBOSOMAL SUBUNIT,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-88 AND GLY-89, AND CATALYTIC
RP ACTIVITY.
RX PubMed=20186120; DOI=10.1038/emboj.2010.14;
RA Richter R., Rorbach J., Pajak A., Smith P.M., Wessels H.J., Huynen M.A.,
RA Smeitink J.A., Lightowlers R.N., Chrzanowska-Lightowlers Z.M.;
RT "A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the
RT human mitochondrial ribosome.";
RL EMBO J. 29:1116-1125(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23908630; DOI=10.3389/fphys.2013.00183;
RA Koc E.C., Cimen H., Kumcuoglu B., Abu N., Akpinar G., Haque M.E.,
RA Spremulli L.L., Koc H.;
RT "Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as new
RT members of the mammalian mitochondrial ribosome.";
RL Front. Physiol. 4:183-183(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP NOMENCLATURE.
RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343;
RA Greber B.J., Ban N.;
RT "Structure and function of the mitochondrial ribosome.";
RL Annu. Rev. Biochem. 85:103-132(2016).
RN [12] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
RN [13] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
RN [14] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- FUNCTION: Essential peptidyl-tRNA hydrolase component of the
CC mitochondrial large ribosomal subunit. Acts as a codon-independent
CC translation release factor that has lost all stop codon specificity and
CC directs the termination of translation in mitochondrion, possibly in
CC case of abortive elongation. May be involved in the hydrolysis of
CC peptidyl-tRNAs that have been prematurely terminated and thus in the
CC recycling of stalled mitochondrial ribosomes.
CC {ECO:0000269|PubMed:20186120}.
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; Evidence={ECO:0000269|PubMed:20186120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54449;
CC Evidence={ECO:0000305|PubMed:20186120};
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503,
CC PubMed:20186120). Mature mammalian 55S mitochondrial ribosomes consist
CC of a small (28S) and a large (39S) subunit. The 28S small subunit
CC contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins.
CC The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of
CC mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an
CC integral structural role, and 52 different proteins.
CC {ECO:0000269|PubMed:20186120, ECO:0000269|PubMed:23908630,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20186120,
CC ECO:0000269|PubMed:23908630, ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- TISSUE SPECIFICITY: Down-regulated during the in vitro differentiation
CC of HT29-D4 colon carcinoma cells. {ECO:0000269|PubMed:8575443}.
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; X81788; CAA57387.1; -; mRNA.
DR EMBL; BT007111; AAP35775.1; -; mRNA.
DR EMBL; AK222553; BAD96273.1; -; mRNA.
DR EMBL; AK314138; BAG36828.1; -; mRNA.
DR EMBL; CH471099; EAW89227.1; -; Genomic_DNA.
DR EMBL; BC015335; AAH15335.1; -; mRNA.
DR CCDS; CCDS11711.1; -.
DR PIR; S63540; S63540.
DR RefSeq; NP_001290194.1; NM_001303265.1.
DR RefSeq; NP_001536.1; NM_001545.2.
DR PDB; 3J7Y; EM; 3.40 A; p=1-206.
DR PDB; 3J9M; EM; 3.50 A; p=1-206.
DR PDB; 5OOL; EM; 3.06 A; p=1-206.
DR PDB; 5OOM; EM; 3.03 A; p=1-206.
DR PDB; 6I9R; EM; 3.90 A; p=1-206.
DR PDB; 6NU2; EM; 3.90 A; p=38-193.
DR PDB; 6NU3; EM; 4.40 A; p=1-206.
DR PDB; 6VLZ; EM; 2.97 A; p=1-206.
DR PDB; 6VMI; EM; 2.96 A; p=1-206.
DR PDB; 6ZM5; EM; 2.89 A; p=1-206.
DR PDB; 6ZM6; EM; 2.59 A; p=1-206.
DR PDB; 6ZS9; EM; 4.00 A; p=1-206.
DR PDB; 6ZSA; EM; 4.00 A; p=1-206.
DR PDB; 6ZSB; EM; 4.50 A; p=1-206.
DR PDB; 6ZSC; EM; 3.50 A; p=1-206.
DR PDB; 6ZSD; EM; 3.70 A; p=1-206.
DR PDB; 6ZSE; EM; 5.00 A; p=1-206.
DR PDB; 6ZSG; EM; 4.00 A; p=1-206.
DR PDB; 7A5F; EM; 4.40 A; p3=1-206.
DR PDB; 7A5G; EM; 4.33 A; p3=1-206.
DR PDB; 7A5H; EM; 3.30 A; p=1-206.
DR PDB; 7A5I; EM; 3.70 A; p3=1-206.
DR PDB; 7A5J; EM; 3.10 A; p=1-206.
DR PDB; 7A5K; EM; 3.70 A; p3=1-206.
DR PDB; 7L08; EM; 3.49 A; p=1-206.
DR PDB; 7L20; EM; 3.15 A; p=1-206.
DR PDB; 7NQL; EM; 3.40 A; BL=30-206.
DR PDB; 7O9K; EM; 3.10 A; p=1-206.
DR PDB; 7O9M; EM; 2.50 A; p=1-205.
DR PDB; 7ODR; EM; 2.90 A; p=1-206.
DR PDB; 7ODS; EM; 3.10 A; p=1-206.
DR PDB; 7ODT; EM; 3.10 A; p=1-206.
DR PDB; 7OF0; EM; 2.20 A; p=1-206.
DR PDB; 7OF2; EM; 2.70 A; p=1-206.
DR PDB; 7OF3; EM; 2.70 A; p=1-206.
DR PDB; 7OF4; EM; 2.70 A; p=1-206.
DR PDB; 7OF5; EM; 2.90 A; p=1-206.
DR PDB; 7OF6; EM; 2.60 A; p=1-206.
DR PDB; 7OF7; EM; 2.50 A; p=1-206.
DR PDB; 7OG4; EM; 3.80 A; p=1-206.
DR PDB; 7OI6; EM; 5.70 A; p=1-206.
DR PDB; 7OI7; EM; 3.50 A; p=1-206.
DR PDB; 7OI8; EM; 3.50 A; p=1-206.
DR PDB; 7OI9; EM; 3.30 A; p=1-206.
DR PDB; 7OIA; EM; 3.20 A; p=1-206.
DR PDB; 7OIB; EM; 3.30 A; p=1-206.
DR PDB; 7OIC; EM; 3.10 A; p=1-206.
DR PDB; 7OID; EM; 3.70 A; p=1-206.
DR PDB; 7OIE; EM; 3.50 A; p=1-206.
DR PDB; 7PD3; EM; 3.40 A; p=1-206.
DR PDB; 7QH6; EM; 3.08 A; p=1-206.
DR PDBsum; 3J7Y; -.
DR PDBsum; 3J9M; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7NQL; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; Q14197; -.
DR SMR; Q14197; -.
DR BioGRID; 109622; 420.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR IntAct; Q14197; 232.
DR MINT; Q14197; -.
DR STRING; 9606.ENSP00000301585; -.
DR GlyGen; Q14197; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14197; -.
DR PhosphoSitePlus; Q14197; -.
DR BioMuta; MRPL58; -.
DR EPD; Q14197; -.
DR jPOST; Q14197; -.
DR MassIVE; Q14197; -.
DR MaxQB; Q14197; -.
DR PaxDb; Q14197; -.
DR PeptideAtlas; Q14197; -.
DR PRIDE; Q14197; -.
DR ProteomicsDB; 59919; -.
DR TopDownProteomics; Q14197; -.
DR Antibodypedia; 1066; 334 antibodies from 30 providers.
DR DNASU; 3396; -.
DR Ensembl; ENST00000301585.10; ENSP00000301585.5; ENSG00000167862.10.
DR GeneID; 3396; -.
DR KEGG; hsa:3396; -.
DR MANE-Select; ENST00000301585.10; ENSP00000301585.5; NM_001545.3; NP_001536.1.
DR UCSC; uc002jmm.4; human.
DR CTD; 3396; -.
DR DisGeNET; 3396; -.
DR GeneCards; MRPL58; -.
DR HGNC; HGNC:5359; MRPL58.
DR HPA; ENSG00000167862; Low tissue specificity.
DR MIM; 603000; gene.
DR neXtProt; NX_Q14197; -.
DR OpenTargets; ENSG00000167862; -.
DR PharmGKB; PA29607; -.
DR VEuPathDB; HostDB:ENSG00000167862; -.
DR eggNOG; KOG3429; Eukaryota.
DR GeneTree; ENSGT00390000013268; -.
DR HOGENOM; CLU_089470_6_1_1; -.
DR InParanoid; Q14197; -.
DR OMA; IIRSQEA; -.
DR OrthoDB; 1611415at2759; -.
DR PhylomeDB; Q14197; -.
DR TreeFam; TF315161; -.
DR BRENDA; 3.1.1.29; 2681.
DR PathwayCommons; Q14197; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; Q14197; -.
DR SIGNOR; Q14197; -.
DR BioGRID-ORCS; 3396; 142 hits in 1089 CRISPR screens.
DR ChiTaRS; MRPL58; human.
DR GenomeRNAi; 3396; -.
DR Pharos; Q14197; Tbio.
DR PRO; PR:Q14197; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14197; protein.
DR Bgee; ENSG00000167862; Expressed in triceps brachii and 202 other tissues.
DR ExpressionAtlas; Q14197; baseline and differential.
DR Genevisible; Q14197; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016150; F:translation release factor activity, codon nonspecific; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0070126; P:mitochondrial translational termination; IDA:UniProtKB.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR Pfam; PF00472; RF-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Mitochondrion; Protein biosynthesis;
KW Reference proteome; Ribonucleoprotein; 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_0000030339"
FT VARIANT 8
FT /note="R -> P (in dbSNP:rs3744206)"
FT /id="VAR_020045"
FT VARIANT 77
FT /note="L -> F (in dbSNP:rs10512599)"
FT /id="VAR_024604"
FT VARIANT 122
FT /note="T -> M (in dbSNP:rs34496172)"
FT /id="VAR_061767"
FT MUTAGEN 88
FT /note="G->A: Strongly impairs peptide release activity."
FT /evidence="ECO:0000269|PubMed:20186120"
FT MUTAGEN 89
FT /note="G->S: Strongly impairs peptide release activity."
FT /evidence="ECO:0000269|PubMed:20186120"
FT CONFLICT 94
FT /note="K -> R (in Ref. 4; BAD96273)"
FT /evidence="ECO:0000305"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 143..162
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 206 AA; 23630 MW; 663BF52443D41540 CRC64;
MAATRCLRWG LSRAGVWLLP PPARCPRRAL HKQKDGTEFK SIYSLDKLYP ESQGSDTAWR
VPNGAKQADS DIPLDRLTIS YCRSSGPGGQ NVNKVNSKAE VRFHLATAEW IAEPVRQKIA
ITHKNKINRL GELILTSESS RYQFRNLADC LQKIRDMITE ASQTPKEPTK EDVKLHRIRI
ENMNRERLRQ KRIHSAVKTS RRVDMD
