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Protein

Peptidyl-tRNA hydrolase ICT1, mitochondrial

Gene

Ict1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity1 Publication

Catalytic activityi

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-tRNA hydrolase ICT1, mitochondrial (EC:3.1.1.29)
Alternative name(s):
39S ribosomal protein L58, mitochondrial
Short name:
MRP-L58
Immature colon carcinoma transcript 1 protein homolog
Gene namesi
Name:Ict1
Synonyms:Mrpl58
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1915822. Ict1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 206177Peptidyl-tRNA hydrolase ICT1, mitochondrialPRO_0000030340Add
BLAST

Proteomic databases

EPDiQ8R035.
MaxQBiQ8R035.
PRIDEiQ8R035.

PTM databases

iPTMnetiQ8R035.
PhosphoSiteiQ8R035.

Expressioni

Gene expression databases

BgeeiQ8R035.
CleanExiMM_ICT1.
ExpressionAtlasiQ8R035. baseline and differential.
GenevisibleiQ8R035. MM.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins.By similarity

Protein-protein interaction databases

BioGridi212934. 1 interaction.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni74 – 763Combined sources
Beta strandi77 – 826Combined sources
Beta strandi87 – 904Combined sources
Beta strandi98 – 1047Combined sources
Helixi105 – 1073Combined sources
Helixi113 – 12210Combined sources
Turni123 – 1264Combined sources
Beta strandi129 – 1379Combined sources
Helixi143 – 16119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J26NMR-A63-161[»]
ProteinModelPortaliQ8R035.
SMRiQ8R035. Positions 39-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R035.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000013268.
HOGENOMiHOG000231063.
HOVERGENiHBG006115.
InParanoidiQ8R035.
KOiK15033.
OMAiTRSQQMN.
OrthoDBiEOG72G18Z.
PhylomeDBiQ8R035.
TreeFamiTF315161.

Family and domain databases

InterProiIPR000352. Pep_chain_release_fac_I_II.
[Graphical view]
PfamiPF00472. RF-1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R035-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATAWGLRWG LSRTGTLLLA PPARCARRAL HRQVDGTTFQ SIYSLDKLYP
60 70 80 90 100
ESKGADTAWK VPEHAKQASS YIPLDRLSIS YCRSSGPGGQ NVNKVNSKAE
110 120 130 140 150
VRFHLASADW IEEPVRQKIA LTHKNKINKA GELVLTSESS RYQFRNLAEC
160 170 180 190 200
LQKIRDMIAE ASQVPKEPSK EDARLQRLRI EKMNRERLRQ KRLNSALKTS

RRMTMD
Length:206
Mass (Da):23,477
Last modified:June 1, 2002 - v1
Checksum:i1B898BE6A559E1F0
GO
Isoform 2 (identifier: Q8R035-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-62: Missing.

Note: No experimental confirmation available.
Show »
Length:177
Mass (Da):20,277
Checksum:iD23C97F02213C13D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei34 – 6229Missing in isoform 2. 1 PublicationVSP_014374Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003192 mRNA. Translation: BAB22632.1.
AK003286 mRNA. Translation: BAB22691.1.
AK160697 mRNA. Translation: BAE35961.1.
AL603828, AL627096 Genomic DNA. Translation: CAM13810.1.
AL627096, AL603828 Genomic DNA. Translation: CAM22619.1.
AL603828, AL627096 Genomic DNA. Translation: CAM13811.1.
AL627096, AL603828 Genomic DNA. Translation: CAM22618.1.
CH466558 Genomic DNA. Translation: EDL34481.1.
CH466558 Genomic DNA. Translation: EDL34486.1.
BC028523 mRNA. Translation: AAH28523.1.
CCDSiCCDS25632.1. [Q8R035-2]
RefSeqiNP_081005.1. NM_026729.1. [Q8R035-2]
XP_006534127.1. XM_006534064.1. [Q8R035-1]
UniGeneiMm.271062.

Genome annotation databases

EnsembliENSMUST00000103036; ENSMUSP00000099325; ENSMUSG00000018858. [Q8R035-2]
ENSMUST00000153983; ENSMUSP00000116746; ENSMUSG00000018858. [Q8R035-1]
GeneIDi68572.
KEGGimmu:68572.
UCSCiuc007mhj.1. mouse. [Q8R035-1]
uc007mhl.1. mouse. [Q8R035-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003192 mRNA. Translation: BAB22632.1.
AK003286 mRNA. Translation: BAB22691.1.
AK160697 mRNA. Translation: BAE35961.1.
AL603828, AL627096 Genomic DNA. Translation: CAM13810.1.
AL627096, AL603828 Genomic DNA. Translation: CAM22619.1.
AL603828, AL627096 Genomic DNA. Translation: CAM13811.1.
AL627096, AL603828 Genomic DNA. Translation: CAM22618.1.
CH466558 Genomic DNA. Translation: EDL34481.1.
CH466558 Genomic DNA. Translation: EDL34486.1.
BC028523 mRNA. Translation: AAH28523.1.
CCDSiCCDS25632.1. [Q8R035-2]
RefSeqiNP_081005.1. NM_026729.1. [Q8R035-2]
XP_006534127.1. XM_006534064.1. [Q8R035-1]
UniGeneiMm.271062.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J26NMR-A63-161[»]
ProteinModelPortaliQ8R035.
SMRiQ8R035. Positions 39-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212934. 1 interaction.

PTM databases

iPTMnetiQ8R035.
PhosphoSiteiQ8R035.

Proteomic databases

EPDiQ8R035.
MaxQBiQ8R035.
PRIDEiQ8R035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103036; ENSMUSP00000099325; ENSMUSG00000018858. [Q8R035-2]
ENSMUST00000153983; ENSMUSP00000116746; ENSMUSG00000018858. [Q8R035-1]
GeneIDi68572.
KEGGimmu:68572.
UCSCiuc007mhj.1. mouse. [Q8R035-1]
uc007mhl.1. mouse. [Q8R035-2]

Organism-specific databases

CTDi3396.
MGIiMGI:1915822. Ict1.

Phylogenomic databases

GeneTreeiENSGT00390000013268.
HOGENOMiHOG000231063.
HOVERGENiHBG006115.
InParanoidiQ8R035.
KOiK15033.
OMAiTRSQQMN.
OrthoDBiEOG72G18Z.
PhylomeDBiQ8R035.
TreeFamiTF315161.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

EvolutionaryTraceiQ8R035.
PROiQ8R035.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R035.
CleanExiMM_ICT1.
ExpressionAtlasiQ8R035. baseline and differential.
GenevisibleiQ8R035. MM.

Family and domain databases

InterProiIPR000352. Pep_chain_release_fac_I_II.
[Graphical view]
PfamiPF00472. RF-1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-206 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo and Head.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Lung.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen and Testis.
  6. "Solution structure of the catalytic domain of the mitochondrial protein ICT1 that is essential for cell vitality."
    Handa Y., Hikawa Y., Tochio N., Kogure H., Inoue M., Koshiba S., Guntert P., Inoue Y., Kigawa T., Yokoyama S., Nameki N.
    J. Mol. Biol. 404:260-273(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 63-162, FUNCTION.

Entry informationi

Entry nameiICT1_MOUSE
AccessioniPrimary (citable) accession number: Q8R035
Secondary accession number(s): A2A6T2
, A2A6T3, Q3TUL0, Q9CTK1, Q9D1R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.