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Protein

Thiosulfate sulfurtransferase

Gene

Tst

Organism
Rattus norvegicus (Rat)
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). Involved in the formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity.By similarity1 Publication

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

SABIO-RKiP24329

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase (EC:2.8.1.1)
Alternative name(s):
Rhodanese
Gene namesi
Name:Tst
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3913 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi249R → G: Unaltered rhodanese activity; increased MST activity. 1 Publication1
Mutagenesisi250K → S: Decreased rhodanese activity; unaltered MST activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001393971 – 297Thiosulfate sulfurtransferaseAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14N6-acetyllysine; alternateBy similarity1
Modified residuei14N6-succinyllysine; alternateBy similarity1
Glycosylationi35O-linked (GlcNAc) serine1 Publication1
Modified residuei38PhosphoserineCombined sources1
Modified residuei136N6-acetyllysine; alternateBy similarity1
Modified residuei136N6-succinyllysine; alternateBy similarity1
Modified residuei163N6-acetyllysineBy similarity1
Modified residuei175N6-acetyllysine; alternateBy similarity1
Modified residuei175N6-succinyllysine; alternateBy similarity1
Modified residuei224N6-acetyllysine; alternateBy similarity1
Modified residuei224N6-succinyllysine; alternateBy similarity1
Modified residuei236N6-acetyllysineBy similarity1
Modified residuei237N6-acetyllysine; alternateBy similarity1
Modified residuei237N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP24329
PRIDEiP24329

PTM databases

CarbonylDBiP24329
iPTMnetiP24329
PhosphoSitePlusiP24329

Expressioni

Tissue specificityi

Expressed in numerous tissues.1 Publication

Gene expression databases

BgeeiENSRNOG00000000186
GenevisibleiP24329 RN

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039338

Structurei

3D structure databases

ProteinModelPortaliP24329
SMRiP24329
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
InParanoidiP24329
KOiK01011
OMAiGDNSNWF
OrthoDBiEOG091G0X2Q
PhylomeDBiP24329
TreeFamiTF315133

Family and domain databases

Gene3Di3.40.250.102 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.

P24329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHQVLYRAL VSTKWLAESI RSGKVGPSLR 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
AVFKATLNRS LLKTYEQVLE NLQSKRFQLV DSRAQGRYLG TQPEPDAVGL
210 220 230 240 250
DSGHIRGSVN VPFMNFLTED GFEKSPEELR AIFQDKKVDL SQPLIATCRK
260 270 280 290
GVTACHIALA AYLCGKPDVA VYDGSWSEWF RRAPPETRVS QGKSGKA
Length:297
Mass (Da):33,407
Last modified:January 23, 2007 - v3
Checksum:iAACD5FA8E8A762D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088449 mRNA Translation: AAH88449.1
X56228 mRNA Translation: CAA39677.1
PIRiS15081
RefSeqiNP_036940.1, NM_012808.1
UniGeneiRn.6360

Genome annotation databases

EnsembliENSRNOT00000050511; ENSRNOP00000039338; ENSRNOG00000000186
GeneIDi25274
KEGGirno:25274
UCSCiRGD:3913 rat

Similar proteinsi

Entry informationi

Entry nameiTHTR_RAT
AccessioniPrimary (citable) accession number: P24329
Secondary accession number(s): Q5I0D4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 142 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, Direct protein sequencing, Reference proteome