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Protein

3-mercaptopyruvate sulfurtransferase

Gene

Mpst

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

Functioni

Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H2S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.3 Publications

Catalytic activityi

3-mercaptopyruvate + cyanide = pyruvate + thiocyanate.

Enzyme regulationi

By oxidative stress, and thioredoxin. Under oxidative stress conditions, the catalytic cysteine site is converted to a sulfenate which inhibits the MPST enzyme activity. Reduced thioredoxin cleaves an intersubunit disulfide bond to turn on the redox switch and reactivate the enzyme. Inhibited by different oxidants, hydrogen peroxide and tetrathionate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881SubstrateBy similarity
Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • 3-mercaptopyruvate sulfurtransferase activity Source: MGI
  • thiosulfate sulfurtransferase activity Source: InterPro

GO - Biological processi

  • hydrogen sulfide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.1.2. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.2)
Short name:
MST
Gene namesi
Name:Mpst
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2179733. Mpst.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
  • neuron projection Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Mitochondrion, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881R → G: Abolishes hydrogen sulfide production. Slighly increased basal levels of bound persulfide. 1 Publication
Mutagenesisi197 – 1971R → G: Reduces hydrogen sulfide production by 50%. No change in basal levels of bound persulfide. 1 Publication
Mutagenesisi248 – 2481C → S: Loss of redox potential. Abolishes bound persulfide and hydrogen sulfide production. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 2972963-mercaptopyruvate sulfurtransferasePRO_0000139399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei40 – 401N6-acetyllysine; alternateCombined sources
Modified residuei40 – 401N6-succinyllysine; alternateCombined sources
Modified residuei146 – 1461N6-succinyllysineCombined sources
Modified residuei164 – 1641N6-succinyllysineCombined sources
Disulfide bondi264 – 264Interchain (with C-264); redox-activeBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ99J99.
MaxQBiQ99J99.
PaxDbiQ99J99.
PRIDEiQ99J99.

2D gel databases

REPRODUCTION-2DPAGEIPI00114957.
Q99J99.

PTM databases

iPTMnetiQ99J99.
PhosphoSiteiQ99J99.
SwissPalmiQ99J99.

Expressioni

Tissue specificityi

Expressed in the brain and retina. In the retina, localized to the inner and outer plexiform layer, the inner and outer nuclear layer and the outer segments of photoreceptors. In the brain, localized to neurons of mitral cell layers, glomerular, and external plexiform layers in the olfactory bulb. Also found in Purkinje cell stomata and proximal dendrites. In the spinal cord, localized to large neurons. In the cerebral cortex, localized to pyramidial neurons in layers II/III and V, and in layers I-VI of neocortical areas. In the hippocampus, found in CA1 and CA3 pyramidal cells.3 Publications

Developmental stagei

In the developing brain, maintained expression from E16 to postnatal day 14. Levels decrease between postnatal day 28 and postnatal day 52 and increase again with further aging up to 156 days old.1 Publication

Gene expression databases

CleanExiMM_MPST.

Interactioni

Subunit structurei

Monomer; active form. Homodimer; disulfide-linked, inactive form.By similarity

Protein-protein interaction databases

IntActiQ99J99. 3 interactions.
MINTiMINT-1860650.
STRINGi10090.ENSMUSP00000043061.

Structurei

3D structure databases

ProteinModelPortaliQ99J99.
SMRiQ99J99. Positions 11-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 144120Rhodanese 1PROSITE-ProRule annotationAdd
BLAST
Domaini174 – 288115Rhodanese 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 16016HingeAdd
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

Redox-active center, Repeat

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ99J99.
PhylomeDBiQ99J99.

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.

Q99J99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPQLFRAL VSAQWVAEAL KAPRSSQPLK LLDASWYLPK LGRDARREFE
60 70 80 90 100
ERHIPGAAFF DIDRCSDHTS PYDHMLPNAT HFADYAGSLG VSAATHVVIY
110 120 130 140 150
DGSDQGPYSA PRVWWMFRAF GHHSVSLLDG GFRHWLNQNL PISSGKSHSE
160 170 180 190 200
PAEFSAQLDP SFIKTHEDIL ENLDARRFQV VDARAAGRFQ GTQPEPRDGI
210 220 230 240 250
EPGHIPGSVN IPFTEFLTNE GLEKSPEEIK RLFKEKKVDL SKPLVATCGS
260 270 280 290
GVTACHVVLG AFLCGKSDVP VYDGSWVEWY MRAQPEHIIS EGRGKTQ
Length:297
Mass (Da):33,023
Last modified:January 23, 2007 - v3
Checksum:i87590F6884F51D98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC004079 mRNA. Translation: AAH04079.1.
CCDSiCCDS27615.1.
UniGeneiMm.294215.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC004079 mRNA. Translation: AAH04079.1.
CCDSiCCDS27615.1.
UniGeneiMm.294215.

3D structure databases

ProteinModelPortaliQ99J99.
SMRiQ99J99. Positions 11-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99J99. 3 interactions.
MINTiMINT-1860650.
STRINGi10090.ENSMUSP00000043061.

PTM databases

iPTMnetiQ99J99.
PhosphoSiteiQ99J99.
SwissPalmiQ99J99.

2D gel databases

REPRODUCTION-2DPAGEIPI00114957.
Q99J99.

Proteomic databases

EPDiQ99J99.
MaxQBiQ99J99.
PaxDbiQ99J99.
PRIDEiQ99J99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:2179733. Mpst.

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiQ99J99.
PhylomeDBiQ99J99.

Enzyme and pathway databases

BRENDAi2.8.1.2. 3474.

Miscellaneous databases

PROiQ99J99.
SOURCEiSearch...

Gene expression databases

CleanExiMM_MPST.

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...

Entry informationi

Entry nameiTHTM_MOUSE
AccessioniPrimary (citable) accession number: Q99J99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are required to release hydrogen sulfide from the persulfide intermediate.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.