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Peptidyl-tRNA hydrolase ICT1, mitochondrial (EC 3.1.1.29) (39S ribosomal protein L58, mitochondrial) (MRP-L58) (Digestion substraction 1) (DS-1) (Immature colon carcinoma transcript 1 protein) (Mitochondrial large ribosomal subunit protein mL62)

 ICT1_HUMAN              Reviewed;         206 AA.
Q14197; B2RAD1; Q53HM7; Q53Y11;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 149.
RecName: Full=Peptidyl-tRNA hydrolase ICT1, mitochondrial;
EC=3.1.1.29;
AltName: Full=39S ribosomal protein L58, mitochondrial {ECO:0000312|HGNC:HGNC:5359};
Short=MRP-L58;
AltName: Full=Digestion substraction 1;
Short=DS-1;
AltName: Full=Immature colon carcinoma transcript 1 protein;
AltName: Full=Mitochondrial large ribosomal subunit protein mL62 {ECO:0000303|PubMed:27023846};
Flags: Precursor;
Name=MRPL58 {ECO:0000312|HGNC:HGNC:5359}; Synonyms=DS1, ICT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=8575443; DOI=10.1111/j.1432-1033.1995.843_a.x;
van Belzen N., Diesveld M.P.G., van der Made A.C.J., Nozawa Y.,
Dinjens W.N.M., Vlietstra R., Trapman J., Bosman F.T.;
"Identification of mRNAs that show modulated expression during colon
carcinoma cell differentiation.";
Eur. J. Biochem. 234:843-848(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL 39S RIBOSOMAL SUBUNIT,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-88 AND GLY-89.
PubMed=20186120; DOI=10.1038/emboj.2010.14;
Richter R., Rorbach J., Pajak A., Smith P.M., Wessels H.J.,
Huynen M.A., Smeitink J.A., Lightowlers R.N.,
Chrzanowska-Lightowlers Z.M.;
"A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into
the human mitochondrial ribosome.";
EMBO J. 29:1116-1125(2010).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=23908630; DOI=10.3389/fphys.2013.00183;
Koc E.C., Cimen H., Kumcuoglu B., Abu N., Akpinar G., Haque M.E.,
Spremulli L.L., Koc H.;
"Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as
new members of the mammalian mitochondrial ribosome.";
Front. Physiol. 4:183-183(2013).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
NOMENCLATURE.
PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343;
Greber B.J., Ban N.;
"Structure and function of the mitochondrial ribosome.";
Annu. Rev. Biochem. 85:103-132(2016).
[12] {ECO:0000244|PDB:3J7Y}
STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=25278503; DOI=10.1126/science.1258026;
Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C.,
Murshudov G., Scheres S.H., Ramakrishnan V.;
"Structure of the large ribosomal subunit from human mitochondria.";
Science 346:718-722(2014).
[13] {ECO:0000244|PDB:3J9M}
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=25838379; DOI=10.1126/science.aaa1193;
Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
"Ribosome. The structure of the human mitochondrial ribosome.";
Science 348:95-98(2015).
-!- FUNCTION: Essential peptidyl-tRNA hydrolase component of the
mitochondrial large ribosomal subunit. Acts as a codon-independent
translation release factor that has lost all stop codon
specificity and directs the termination of translation in
mitochondrion, possibly in case of abortive elongation. May be
involved in the hydrolysis of peptidyl-tRNAs that have been
prematurely terminated and thus in the recycling of stalled
mitochondrial ribosomes. {ECO:0000269|PubMed:20186120}.
-!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
substituted amino acid + tRNA.
-!- SUBUNIT: Component of the mitochondrial large ribosomal subunit
(mt-LSU). Mature mammalian 55S mitochondrial ribosomes consist of
a small (28S) and a large (39S) subunit. The 28S small subunit
contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different
proteins. The 39S large subunit contains a 16S rRNA (16S mt-rRNA),
a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)), which
plays an integral structural role, and 52 different proteins.
{ECO:0000269|PubMed:20186120, ECO:0000269|PubMed:23908630,
ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20186120,
ECO:0000269|PubMed:23908630, ECO:0000269|PubMed:25278503,
ECO:0000269|PubMed:25838379}.
-!- TISSUE SPECIFICITY: Down-regulated during the in vitro
differentiation of HT29-D4 colon carcinoma cells.
{ECO:0000269|PubMed:8575443}.
-!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release
factor family. Mitochondrion-specific ribosomal protein mL62
subfamily. {ECO:0000305}.
-!- CAUTION: In contrast to other members of the family, lacks the
regions that come into close contact with the mRNA in the
ribosomal A-site and determine the STOP codon specificity,
explaining the loss of codon specificity for translation release
factor activity. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X81788; CAA57387.1; -; mRNA.
EMBL; BT007111; AAP35775.1; -; mRNA.
EMBL; AK222553; BAD96273.1; -; mRNA.
EMBL; AK314138; BAG36828.1; -; mRNA.
EMBL; CH471099; EAW89227.1; -; Genomic_DNA.
EMBL; BC015335; AAH15335.1; -; mRNA.
CCDS; CCDS11711.1; -.
PIR; S63540; S63540.
RefSeq; NP_001290194.1; NM_001303265.1.
RefSeq; NP_001536.1; NM_001545.2.
UniGene; Hs.407955; -.
PDB; 3J7Y; EM; 3.40 A; p=1-206.
PDB; 3J9M; EM; 3.50 A; p=1-206.
PDB; 5OOL; EM; 3.06 A; p=1-206.
PDB; 5OOM; EM; 3.03 A; p=1-206.
PDBsum; 3J7Y; -.
PDBsum; 3J9M; -.
PDBsum; 5OOL; -.
PDBsum; 5OOM; -.
ProteinModelPortal; Q14197; -.
SMR; Q14197; -.
BioGrid; 109622; 247.
IntAct; Q14197; 220.
MINT; MINT-3029229; -.
STRING; 9606.ENSP00000301585; -.
iPTMnet; Q14197; -.
PhosphoSitePlus; Q14197; -.
BioMuta; ICT1; -.
EPD; Q14197; -.
MaxQB; Q14197; -.
PaxDb; Q14197; -.
PeptideAtlas; Q14197; -.
PRIDE; Q14197; -.
TopDownProteomics; Q14197; -.
DNASU; 3396; -.
Ensembl; ENST00000301585; ENSP00000301585; ENSG00000167862.
GeneID; 3396; -.
KEGG; hsa:3396; -.
UCSC; uc002jmm.4; human.
CTD; 3396; -.
EuPathDB; HostDB:ENSG00000167862.9; -.
GeneCards; MRPL58; -.
HGNC; HGNC:5359; MRPL58.
HPA; HPA003634; -.
MIM; 603000; gene.
neXtProt; NX_Q14197; -.
OpenTargets; ENSG00000167862; -.
PharmGKB; PA29607; -.
eggNOG; KOG3429; Eukaryota.
eggNOG; COG1186; LUCA.
GeneTree; ENSGT00390000013268; -.
HOGENOM; HOG000231063; -.
HOVERGEN; HBG006115; -.
InParanoid; Q14197; -.
KO; K15033; -.
OMA; KIYPNAR; -.
OrthoDB; EOG091G0SBR; -.
PhylomeDB; Q14197; -.
TreeFam; TF315161; -.
BRENDA; 3.1.1.29; 2681.
Reactome; R-HSA-5368286; Mitochondrial translation initiation.
Reactome; R-HSA-5389840; Mitochondrial translation elongation.
Reactome; R-HSA-5419276; Mitochondrial translation termination.
GenomeRNAi; 3396; -.
PRO; PR:Q14197; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000167862; -.
CleanEx; HS_ICT1; -.
ExpressionAtlas; Q14197; baseline and differential.
Genevisible; Q14197; HS.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:UniProtKB.
GO; GO:0016150; F:translation release factor activity, codon nonspecific; IDA:UniProtKB.
GO; GO:0070125; P:mitochondrial translational elongation; TAS:Reactome.
GO; GO:0070126; P:mitochondrial translational termination; IDA:UniProtKB.
GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
InterPro; IPR000352; Pep_chain_release_fac_I_II.
Pfam; PF00472; RF-1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Mitochondrion;
Polymorphism; Protein biosynthesis; Reference proteome;
Ribonucleoprotein; Ribosomal protein; Transit peptide.
TRANSIT 1 29 Mitochondrion. {ECO:0000255}.
CHAIN 30 206 Peptidyl-tRNA hydrolase ICT1,
mitochondrial.
/FTId=PRO_0000030339.
VARIANT 8 8 R -> P (in dbSNP:rs3744206).
/FTId=VAR_020045.
VARIANT 77 77 L -> F (in dbSNP:rs10512599).
/FTId=VAR_024604.
VARIANT 122 122 T -> M (in dbSNP:rs34496172).
/FTId=VAR_061767.
MUTAGEN 88 88 G->A: Strongly impairs peptide release
activity. {ECO:0000269|PubMed:20186120}.
MUTAGEN 89 89 G->S: Strongly impairs peptide release
activity. {ECO:0000269|PubMed:20186120}.
CONFLICT 94 94 K -> R (in Ref. 4; BAD96273).
{ECO:0000305}.
HELIX 45 48 {ECO:0000244|PDB:5OOM}.
HELIX 55 58 {ECO:0000244|PDB:5OOM}.
TURN 74 76 {ECO:0000244|PDB:5OOM}.
STRAND 77 81 {ECO:0000244|PDB:5OOM}.
STRAND 99 107 {ECO:0000244|PDB:5OOM}.
HELIX 113 122 {ECO:0000244|PDB:5OOM}.
TURN 123 125 {ECO:0000244|PDB:5OOM}.
STRAND 131 137 {ECO:0000244|PDB:5OOM}.
STRAND 140 142 {ECO:0000244|PDB:3J7Y}.
HELIX 143 162 {ECO:0000244|PDB:5OOM}.
HELIX 175 188 {ECO:0000244|PDB:5OOM}.
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


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