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Protein

3-mercaptopyruvate sulfurtransferase

Gene

Mpst

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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.4 Publications

Miscellaneous

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

Catalytic activityi

3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin.2 Publications

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei188SubstrateBy similarity1
Active sitei248Cysteine persulfide intermediatePROSITE-ProRule annotation2 Publications1

GO - Molecular functioni

GO - Biological processi

  • hydrogen sulfide biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BRENDAi2.8.1.2 3474
ReactomeiR-MMU-1614558 Degradation of cysteine and homocysteine

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.22 Publications)
Short name:
MST
Gene namesi
Name:Mpst
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2179733 Mpst

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

Cell junction, Cytoplasm, Mitochondrion, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi188R → G: Abolishes hydrogen sulfide production. Slighly increased basal levels of bound persulfide. 1 Publication1
Mutagenesisi197R → G: Reduces hydrogen sulfide production by 50%. No change in basal levels of bound persulfide. 1 Publication1
Mutagenesisi248C → S: Loss of redox potential. Abolishes bound persulfide and hydrogen sulfide production. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001393992 – 2973-mercaptopyruvate sulfurtransferaseAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei35PhosphoserineBy similarity1
Modified residuei40N6-acetyllysine; alternateCombined sources1
Modified residuei40N6-succinyllysine; alternateCombined sources1
Modified residuei146N6-succinyllysineCombined sources1
Modified residuei164N6-succinyllysineCombined sources1
Disulfide bondi264Interchain (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
PhosphoSitePlusiQ99J99
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

BgeeiENSMUSG00000071711
CleanExiMM_MPST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ99J99, 3 interactors
MINTiQ99J99
STRINGi10090.ENSMUSP00000043061

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Helixi13 – 21Combined sources9
Beta strandi29 – 33Combined sources5
Helixi39 – 41Combined sources3
Helixi45 – 51Combined sources7
Helixi62 – 64Combined sources3
Beta strandi70 – 74Combined sources5
Helixi79 – 88Combined sources10
Beta strandi96 – 100Combined sources5
Helixi110 – 119Combined sources10
Beta strandi125 – 128Combined sources4
Helixi131 – 137Combined sources7
Helixi160 – 162Combined sources3
Helixi166 – 175Combined sources10
Beta strandi178 – 182Combined sources5
Helixi186 – 190Combined sources5
Helixi213 – 216Combined sources4
Helixi226 – 235Combined sources10
Beta strandi244 – 247Combined sources4
Beta strandi249 – 252Combined sources4
Helixi254 – 263Combined sources10
Beta strandi271 – 274Combined sources4
Helixi275 – 282Combined sources8
Helixi285 – 287Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WQJX-ray1.20A/B1-297[»]
5WQKX-ray1.70A/B5-297[»]
ProteinModelPortaliQ99J99
SMRiQ99J99
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 144Rhodanese 1PROSITE-ProRule annotationAdd BLAST120
Domaini174 – 288Rhodanese 2PROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni145 – 160HingeAdd 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

Redox-active center, Repeat

Phylogenomic databases

eggNOGiKOG1529 Eukaryota
COG2897 LUCA
GeneTreeiENSGT00510000046773
HOGENOMiHOG000157237
HOVERGENiHBG002345
InParanoidiQ99J99
KOiK01011
OMAiCGKPDVP
OrthoDBiEOG091G0X2Q
PhylomeDBiQ99J99
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.

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
DDSDQGLYSA 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):33,097
Last modified:March 28, 2018 - v4
Checksum:i9D316B9AD9344D0A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102D → G in EDL29674 (Ref. 3) 1
Sequence conflicti102D → G in AAH04079 (PubMed:15489334).1
Sequence conflicti102D → G in AAH94469 (PubMed:15489334).1
Sequence conflicti107L → P in AAH04079 (PubMed:15489334).1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK136571 mRNA Translation: BAE23053.1
AL583893 Genomic DNA No translation available.
AL590144 Genomic DNA No translation available.
CH466545 Genomic DNA Translation: EDL29674.1
BC004079 mRNA Translation: AAH04079.1
BC094469 mRNA Translation: AAH94469.1
CCDSiCCDS27615.1
RefSeqiNP_001155964.1, NM_001162492.1
NP_001155965.1, NM_001162493.1
NP_619611.3, NM_138670.3
XP_006521057.1, XM_006520994.3
XP_006521058.1, XM_006520995.2
XP_006521059.1, XM_006520996.3
UniGeneiMm.294215

Genome annotation databases

EnsembliENSMUST00000043865; ENSMUSP00000043061; ENSMUSG00000071711
ENSMUST00000167140; ENSMUSP00000130493; ENSMUSG00000071711
ENSMUST00000169133; ENSMUSP00000128075; ENSMUSG00000071711
GeneIDi246221
KEGGimmu:246221
UCSCiuc007wpe.2 mouse

Similar proteinsi

Entry informationi

Entry nameiTHTM_MOUSE
AccessioniPrimary (citable) accession number: Q99J99
Secondary accession number(s): Q3UW66, Q505N7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 28, 2018
Last modified: May 23, 2018
This is version 105 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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