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Protein

3-mercaptopyruvate sulfurtransferase

Gene

Mpst

Organism
Rattus norvegicus (Rat)
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.By similarity

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei188SubstrateBy similarity1
Active sitei248Cysteine persulfide intermediatePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • 3-mercaptopyruvate sulfurtransferase activity Source: UniProtKB-EC
  • identical protein binding Source: RGD
  • thiosulfate sulfurtransferase activity Source: RGD

GO - Biological processi

  • hydrogen sulfide biosynthetic process Source: UniProtKB
  • kidney development Source: RGD
  • liver development Source: RGD
  • spinal cord development Source: RGD
  • transsulfuration Source: RGD

Keywordsi

Molecular functionTransferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12473
BRENDAi2.8.1.2 5301
ReactomeiR-RNO-1614558 Degradation of cysteine and homocysteine
SABIO-RKiP97532

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.22 Publications)
Short name:
MST
Gene namesi
Name:Mpst
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi620065 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
Mutagenesisi65C → S: No effect on redox potential. 1 Publication1
Mutagenesisi155C → S: No effect on redox potential. 1 Publication1
Mutagenesisi188R → G: Large decrease in MST activity; some decrease in rhodanese activity. 1 Publication1
Mutagenesisi197R → G: Decreased MST activity; increased rhodanese activity. 1 Publication1
Mutagenesisi248C → S: Loss of both enzyme activities. Greatly reduced redox potential. 2 Publications1
Mutagenesisi249G → R: Decreased MST activity; increased rhodanese activity. 1
Mutagenesisi250S → A: Slight decrease in MST activity. 1 Publication1
Mutagenesisi250S → K: Slight decrease in MST activity; increased rhodanese activity. 1 Publication1
Mutagenesisi255C → S: Little change in redox potential. 1 Publication1
Mutagenesisi264C → S: Greatly reduced redox potential. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001394002 – 2973-mercaptopyruvate sulfurtransferaseAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei35PhosphoserineBy similarity1
Modified residuei40N6-acetyllysine; alternateBy similarity1
Modified residuei40N6-succinyllysine; alternateBy similarity1
Modified residuei146N6-succinyllysineBy similarity1
Disulfide bondi155Interchain (with C-155 or C-264); redox-activeBy similarity
Modified residuei164N6-succinyllysineBy similarity1
Disulfide bondi264Interchain (with C-155 or C-264); redox-activeBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP97532
PRIDEiP97532

2D gel databases

World-2DPAGEi0004:P97532

PTM databases

iPTMnetiP97532
PhosphoSitePlusiP97532
SwissPalmiP97532

Expressioni

Tissue specificityi

Expressed in liver, heart, kidney and brain. Localizes to tubular epithelium in the kidney, pericentral hepatocytes in the liver, cardiac cells in the heart and neuroglial cells in the brain. Also expressed in vascular endothelium of the thoracic aorta. Weak expression in lung and thymus.2 Publications

Gene expression databases

BgeeiENSRNOG00000000185
GenevisibleiP97532 RN

Interactioni

Subunit structurei

Monomer (active form). Homodimer; disulfide-linked (inactive form).1 Publication

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000201

Structurei

3D structure databases

ProteinModelPortaliP97532
SMRiP97532
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
InParanoidiP97532
KOiK01011
OMAiCGKPDVP
OrthoDBiEOG091G0X2Q
PhylomeDBiP97532
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.

P97532-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPQLFRAL VSAQWVAEAL KSPRASQPLK LLDASWYLPK LGRDARREFE
60 70 80 90 100
ERHIPGAAFF DIDRCSDHTS PYDHMLPSAT HFADYAGSLG VSAATHVVIY
110 120 130 140 150
DGSDQGLYSA PRVWWMFRAF GHHSVSLLDG GFRYWLSQNL PISSGKSPSE
160 170 180 190 200
PAEFCAQLDP SFIKTHEDIL ENLDARRFQV VDARAAGRFQ GTQPEPRDGI
210 220 230 240 250
EPGHIPGSVN IPFTEFLTSE GLEKSPEEIQ RLFQEKKVDL SKPLVATCGS
260 270 280 290
GVTACHVVLG AFLCGKPDVP VYDGSWVEWY MRAQPEHVIS QGRGKTL
Length:297
Mass (Da):32,940
Last modified:January 23, 2007 - v3
Checksum:i314E2B8EAFDEFB77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50564 mRNA Translation: BAA09127.1
BC086575 mRNA Translation: AAH86575.1
PIRiA57483
RefSeqiNP_620198.1, NM_138843.1
UniGeneiRn.32263

Genome annotation databases

EnsembliENSRNOT00000000201; ENSRNOP00000000201; ENSRNOG00000000185
GeneIDi192172
KEGGirno:192172
UCSCiRGD:620065 rat

Similar proteinsi

Entry informationi

Entry nameiTHTM_RAT
AccessioniPrimary (citable) accession number: P97532
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 129 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

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