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Protein

Thiosulfate sulfurtransferase

Gene

Tst

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

Functioni

Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification.By similarity

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871SubstrateBy similarity
Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation
Binding sitei250 – 2501SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

SABIO-RKP52196.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.1)
Alternative name(s):
Rhodanese
Gene namesi
Name:Tst
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:98852. Tst.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 297296Thiosulfate sulfurtransferasePRO_0000139396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysine; alternateCombined sources
Modified residuei14 – 141N6-succinyllysine; alternateCombined sources
Modified residuei35 – 351Phosphoserine; alternateBy similarity
Glycosylationi35 – 351O-linked (GlcNAc); alternateBy similarity
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei136 – 1361N6-acetyllysine; alternateCombined sources
Modified residuei136 – 1361N6-succinyllysine; alternateCombined sources
Modified residuei163 – 1631N6-acetyllysine; alternateCombined sources
Modified residuei163 – 1631N6-succinyllysine; alternateBy similarity
Modified residuei175 – 1751N6-acetyllysine; alternateCombined sources
Modified residuei175 – 1751N6-succinyllysine; alternateCombined sources
Modified residuei219 – 2191N6-acetyllysine; alternateCombined sources
Modified residuei219 – 2191N6-succinyllysine; alternateCombined sources
Modified residuei224 – 2241N6-acetyllysine; alternateCombined sources
Modified residuei224 – 2241N6-succinyllysine; alternateCombined sources
Modified residuei236 – 2361N6-acetyllysineCombined sources
Modified residuei237 – 2371N6-acetyllysine; alternateCombined sources
Modified residuei237 – 2371N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP52196.
PaxDbiP52196.
PRIDEiP52196.

2D gel databases

REPRODUCTION-2DPAGEP52196.
SWISS-2DPAGEP52196.

PTM databases

iPTMnetiP52196.
PhosphoSiteiP52196.
SwissPalmiP52196.

Expressioni

Tissue specificityi

Expressed in numerous tissues.

Gene expression databases

BgeeiP52196.
CleanExiMM_TST.
ExpressionAtlasiP52196. baseline and differential.
GenevisibleiP52196. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP52196. 2 interactions.
MINTiMINT-1860310.
STRINGi10090.ENSMUSP00000055743.

Structurei

3D structure databases

ProteinModelPortaliP52196.
SMRiP52196. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 143119Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini173 – 288116Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 15916HingeAdd
BLAST

Domaini

Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).By similarity

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP52196.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiP52196.
TreeFamiTF315133.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P52196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHQVLYRAL VSTKWLAESI RSGRLGPSLR VLDASWYSPG TRQARKEYQE
60 70 80 90 100
RHVPGASFFD IEECRDTTSP YEMMLPSEAH FGDYVGNLGI SNDTHVVVYD
110 120 130 140 150
GDDLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP
160 170 180 190 200
AVFKATLNLS LLKTYEQVLE NLQSKRFQLV DSRAQGRYLG TQPEPDIVGL
210 220 230 240 250
DSGHIRGSVN MPFMDFLTKD GFEKSPEELR AIFQDKKVDL SQPLIATCRK
260 270 280 290
GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPETRVS QGKSGKA
Length:297
Mass (Da):33,466
Last modified:January 23, 2007 - v3
Checksum:iB88AA16C61086F51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35741 mRNA. Translation: AAC52342.1.
BC005644 mRNA. Translation: AAH05644.1.
CCDSiCCDS27614.1.
PIRiJC4398.
RefSeqiNP_033463.1. NM_009437.4.
UniGeneiMm.15312.

Genome annotation databases

EnsembliENSMUST00000058659; ENSMUSP00000055743; ENSMUSG00000044986.
GeneIDi22117.
KEGGimmu:22117.
UCSCiuc007wpd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35741 mRNA. Translation: AAC52342.1.
BC005644 mRNA. Translation: AAH05644.1.
CCDSiCCDS27614.1.
PIRiJC4398.
RefSeqiNP_033463.1. NM_009437.4.
UniGeneiMm.15312.

3D structure databases

ProteinModelPortaliP52196.
SMRiP52196. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52196. 2 interactions.
MINTiMINT-1860310.
STRINGi10090.ENSMUSP00000055743.

PTM databases

iPTMnetiP52196.
PhosphoSiteiP52196.
SwissPalmiP52196.

2D gel databases

REPRODUCTION-2DPAGEP52196.
SWISS-2DPAGEP52196.

Proteomic databases

EPDiP52196.
PaxDbiP52196.
PRIDEiP52196.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058659; ENSMUSP00000055743; ENSMUSG00000044986.
GeneIDi22117.
KEGGimmu:22117.
UCSCiuc007wpd.1. mouse.

Organism-specific databases

CTDi7263.
MGIiMGI:98852. Tst.

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP52196.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiP52196.
TreeFamiTF315133.

Enzyme and pathway databases

SABIO-RKP52196.

Miscellaneous databases

ChiTaRSiTst. mouse.
NextBioi301977.
PROiP52196.
SOURCEiSearch...

Gene expression databases

BgeeiP52196.
CleanExiMM_TST.
ExpressionAtlasiP52196. baseline and differential.
GenevisibleiP52196. MM.

Family and domain databases

Gene3Di3.40.250.10. 2 hits.
InterProiIPR001763. Rhodanese-like_dom.
IPR001307. Thiosulphate_STrfase_CS.
[Graphical view]
PfamiPF00581. Rhodanese. 2 hits.
[Graphical view]
SMARTiSM00450. RHOD. 2 hits.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 2 hits.
PROSITEiPS00380. RHODANESE_1. 1 hit.
PS00683. RHODANESE_2. 1 hit.
PS50206. RHODANESE_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse rhodanese gene (Tst): cDNA cloning, sequencing, and recombinant protein expression."
    Dooley T.P., Nair S.K., Garcia R.E., Courtney B.C.
    Biochem. Biophys. Res. Commun. 216:1101-1109(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Liver.
  2. "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].
    Strain: NMRI.
    Tissue: Mammary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-136; LYS-175; LYS-219; LYS-224 AND LYS-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-136; LYS-163; LYS-175; LYS-219; LYS-224; LYS-236 AND LYS-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTHTR_MOUSE
AccessioniPrimary (citable) accession number: P52196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.