Tst thiosulfate sulfurtransferase, mitochondrial [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tstprovided by MGI
Official Full Name: thiosulfate sulfurtransferase, mitochondrialprovided by MGI
Primary source: MGI:MGI:98852
See related: Ensembl:ENSMUSG00000044986 AllianceGenome:MGI:98852
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: rhodanese
Summary: Predicted to enable 3-mercaptopyruvate sulfurtransferase activity; 5S rRNA binding activity; and thiosulfate sulfurtransferase activity. Predicted to be involved in epithelial cell differentiation and rRNA import into mitochondrion. Located in mitochondrial inner membrane. Is expressed in several structures, including alimentary system; genitourinary system; nervous system; respiratory system; and sensory organ. Orthologous to human TST (thiosulfate sulfurtransferase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in liver adult (RPKM 153.9), adrenal adult (RPKM 109.2) and 17 other tissues See more
Orthologs: human all
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Genomic context

Location:: 15 E1; 15 37.47 cM

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	15	NC_000081.7 (78283756..78290065, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	15	NC_000081.6 (78399556..78405865, complement)

Chromosome 15 - NC_000081.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tst gene mediates protection against palmitate-induced inflammation in 3T3-L1 adipocytes.
Title: Tst gene mediates protection against palmitate-induced inflammation in 3T3-L1 adipocytes.
Results identified two regulatory variants between fat and lean mice: one overlaps an evolutionary constrained Tst intronic element and the other resides in the seed region of a predicted 3'UTR miRNA binding site.
Title: Construction of an integrative regulatory element and variation map of the murine Tst locus.
Elevated adipose Tst expression correlated with indices of metabolic health across diverse mouse strains. Transgenic overexpression of Tst in adipocytes protected mice from diet-induced obesity and insulin-resistant diabetes. Tst-deficient mice showed markedly exacerbated diabetes.
Title: Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness.
increased sensitivity to cyanide, generally reported in old mice, may be due in part to a decrease in the activity of brain rhodanese
Title: Age-related changes in the activity of cerebral rhodanese in mice during the first four months of life.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1)
Targeted (2)

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables 3-mercaptopyruvate sulfurtransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables 5S rRNA binding	ISO Inferred from Sequence Orthology more info
enables 5S rRNA binding	ISS Inferred from Sequence or Structural Similarity more info
enables thiosulfate sulfurtransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables thiosulfate sulfurtransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in epithelial cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in epithelial cell differentiation	ISO Inferred from Sequence Orthology more info
involved_in rRNA import into mitochondrion	ISO Inferred from Sequence Orthology more info
involved_in rRNA import into mitochondrion	ISS Inferred from Sequence or Structural Similarity more info
involved_in rRNA transport	ISO Inferred from Sequence Orthology more info
involved_in rRNA transport	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in mitochondrial inner membrane	HDA more info	PubMed
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: thiosulfate sulfurtransferase

NP_033463.1

EC 2.8.1.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_009437.5 → NP_033463.1 thiosulfate sulfurtransferase

See identical proteins and their annotated locations for NP_033463.1

Status: VALIDATED

Source sequence(s)

AL583893

Consensus CDS

CCDS27614.1

UniProtKB/Swiss-Prot

P52196

UniProtKB/TrEMBL

Q545S0

Related

ENSMUSP00000055743.8, ENSMUST00000058659.9

Conserved Domains (3) summary

COG2897
Location:10 → 279

SseA; 3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism]

cd01445
Location:11 → 136

TST_Repeats; Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only the second repeat contains the catalytically active Cys residue. The role of the 1st repeat is uncertain, but believed to be involved in protein interaction. ...

cd01449
Location:163 → 281

TST_Repeat_2; Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.