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Protein

Thiosulfate sulfurtransferase

Gene

Tst

Organism
Rattus norvegicus (Rat)
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). 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)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-RKP24329.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3913. Tst.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi249 – 2491R → G: Unaltered rhodanese activity; increased MST activity. 1 Publication
Mutagenesisi250 – 2501K → S: Decreased rhodanese activity; unaltered MST activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 297296Thiosulfate sulfurtransferasePRO_0000139397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141N6-acetyllysine; alternateBy similarity
Modified residuei14 – 141N6-succinyllysine; alternateBy similarity
Modified residuei35 – 351Phosphoserine; alternateBy similarity
Glycosylationi35 – 351O-linked (GlcNAc); alternate1 Publication
Modified residuei38 – 381PhosphoserineCombined sources
Modified residuei136 – 1361N6-acetyllysine; alternateBy similarity
Modified residuei136 – 1361N6-succinyllysine; alternateBy similarity
Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
Modified residuei163 – 1631N6-succinyllysine; alternateBy similarity
Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity
Modified residuei224 – 2241N6-acetyllysine; alternateBy similarity
Modified residuei224 – 2241N6-succinyllysine; alternateBy similarity
Modified residuei236 – 2361N6-acetyllysineBy similarity
Modified residuei237 – 2371N6-acetyllysine; alternateBy similarity
Modified residuei237 – 2371N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP24329.
PRIDEiP24329.

PTM databases

iPTMnetiP24329.
PhosphoSiteiP24329.

Expressioni

Tissue specificityi

Expressed in numerous tissues.1 Publication

Gene expression databases

GenevisibleiP24329. RN.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039338.

Structurei

3D structure databases

ProteinModelPortaliP24329.
SMRiP24329. 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.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP24329.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiP24329.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP24329.
SMRiP24329. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039338.

PTM databases

iPTMnetiP24329.
PhosphoSiteiP24329.

Proteomic databases

PaxDbiP24329.
PRIDEiP24329.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7263.
RGDi3913. Tst.

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP24329.
KOiK01011.
OMAiSRAQGRY.
OrthoDBiEOG72ZCGB.
PhylomeDBiP24329.
TreeFamiTF315133.

Enzyme and pathway databases

SABIO-RKP24329.

Miscellaneous databases

NextBioi605969.
PROiP24329.

Gene expression databases

GenevisibleiP24329. RN.

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. "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].
    Tissue: Kidney.
  2. "Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase."
    Weiland K.L., Dooley T.P.
    Biochem. J. 275:227-231(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-297, FUNCTION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 52-65; 123-132; 137-154; 177-183 AND 187-206, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  4. "Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis."
    Nagahara N., Okazaki T., Nishino T.
    J. Biol. Chem. 270:16230-16235(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-249 AND LYS-250.
    Tissue: Liver.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
    Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
    PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-35.

Entry informationi

Entry nameiTHTR_RAT
AccessioniPrimary (citable) accession number: P24329
Secondary accession number(s): Q5I0D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: January 20, 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.