Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thiosulfate sulfurtransferase

Gene

Tst

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei187SubstrateBy similarity1
Active sitei248Cysteine persulfide intermediatePROSITE-ProRule annotation1
Binding sitei250SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRNA-binding, Transferase

Enzyme and pathway databases

ReactomeiR-MMU-1614558 Degradation of cysteine and homocysteine
SABIO-RKiP52196

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:98852 Tst

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001393961 – 297Thiosulfate sulfurtransferaseAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-acetyllysine; alternateCombined sources1
Modified residuei14N6-succinyllysine; alternateCombined sources1
Glycosylationi35O-linked (GlcNAc) serineBy similarity1
Modified residuei38PhosphoserineBy similarity1
Modified residuei136N6-acetyllysine; alternateCombined sources1
Modified residuei136N6-succinyllysine; alternateCombined sources1
Modified residuei163N6-acetyllysineCombined sources1
Modified residuei175N6-acetyllysine; alternateCombined sources1
Modified residuei175N6-succinyllysine; alternateCombined sources1
Modified residuei219N6-acetyllysine; alternateCombined sources1
Modified residuei219N6-succinyllysine; alternateCombined sources1
Modified residuei224N6-acetyllysine; alternateCombined sources1
Modified residuei224N6-succinyllysine; alternateCombined sources1
Modified residuei236N6-acetyllysineCombined sources1
Modified residuei237N6-acetyllysine; alternateCombined sources1
Modified residuei237N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP52196
PeptideAtlasiP52196
PRIDEiP52196

2D gel databases

REPRODUCTION-2DPAGEiP52196
SWISS-2DPAGEiP52196

PTM databases

iPTMnetiP52196
PhosphoSitePlusiP52196
SwissPalmiP52196

Expressioni

Tissue specificityi

Expressed in numerous tissues.

Gene expression databases

BgeeiENSMUSG00000044986
CleanExiMM_TST
ExpressionAtlasiP52196 baseline and differential
GenevisibleiP52196 MM

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiP52196, 2 interactors
MINTiP52196
STRINGi10090.ENSMUSP00000055743

Structurei

3D structure databases

ProteinModelPortaliP52196
SMRiP52196
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 143Rhodanese 1PROSITE-ProRule annotationAdd BLAST119
Domaini173 – 288Rhodanese 2PROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 159HingeAdd BLAST16

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1529 Eukaryota
COG2897 LUCA
GeneTreeiENSGT00510000046773
HOGENOMiHOG000157237
HOVERGENiHBG002345
InParanoidiP52196
KOiK01011
OMAiGDNSNWF
OrthoDBiEOG091G0X2Q
PhylomeDBiP52196
TreeFamiTF315133

Family and domain databases

Gene3Di3.40.250.10, 2 hits
InterProiView protein in InterPro
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf
IPR001307 Thiosulphate_STrfase_CS
PfamiView protein in Pfam
PF00581 Rhodanese, 2 hits
SMARTiView protein in SMART
SM00450 RHOD, 2 hits
SUPFAMiSSF52821 SSF52821, 2 hits
PROSITEiView protein in PROSITE
PS00380 RHODANESE_1, 1 hit
PS00683 RHODANESE_2, 1 hit
PS50206 RHODANESE_3, 2 hits

Sequencei

Sequence statusi: Complete.

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

Similar proteinsi

Entry informationi

Entry nameiTHTR_MOUSE
AccessioniPrimary (citable) accession number: P52196
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 141 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health