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Protein

3-mercaptopyruvate sulfurtransferase

Gene

Mpst

Organism
Rattus norvegicus (Rat)
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.2 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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei188 – 1881SubstrateBy similarity
Active sitei248 – 2481Cysteine persulfide intermediatePROSITE-ProRule annotation1 Publication

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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12473.
BRENDAi2.8.1.2. 5301.
SABIO-RKP97532.

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.2)
Short name:
MST
Gene namesi
Name:Mpst
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi620065. Mpst.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • mitochondrion Source: UniProtKB
  • 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
Mutagenesisi65 – 651C → S: No effect on redox potential. 1 Publication
Mutagenesisi155 – 1551C → S: No effect on redox potential. 1 Publication
Mutagenesisi188 – 1881R → G: Large decrease in MST activity; some decrease in rhodanese activity. 1 Publication
Mutagenesisi197 – 1971R → G: Decreased MST activity; increased rhodanese activity. 1 Publication
Mutagenesisi248 – 2481C → S: Loss of both enzyme activities. Greatly reduced redox potential. 2 Publications
Mutagenesisi249 – 2491G → R: Decreased MST activity; increased rhodanese activity.
Mutagenesisi250 – 2501S → A: Slight decrease in MST activity. 1 Publication
Mutagenesisi250 – 2501S → K: Slight decrease in MST activity; increased rhodanese activity. 1 Publication
Mutagenesisi255 – 2551C → S: Little change in redox potential. 1 Publication
Mutagenesisi264 – 2641C → S: Greatly reduced redox potential. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 2972963-mercaptopyruvate sulfurtransferasePRO_0000139400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei40 – 401N6-acetyllysine; alternateBy similarity
Modified residuei40 – 401N6-succinyllysine; alternateBy similarity
Modified residuei146 – 1461N6-succinyllysineBy similarity
Disulfide bondi155 – 155Interchain (with C-155 or C-264); redox-activeBy similarity
Modified residuei164 – 1641N6-succinyllysineBy similarity
Disulfide bondi264 – 264Interchain (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-2DPAGE0004:P97532.

PTM databases

iPTMnetiP97532.
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

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. Positions 4-294.
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.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP97532.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG72ZCGB.
PhylomeDBiP97532.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP97532.
SMRiP97532. Positions 4-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000201.

PTM databases

iPTMnetiP97532.
SwissPalmiP97532.

2D gel databases

World-2DPAGE0004:P97532.

Proteomic databases

PaxDbiP97532.
PRIDEiP97532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4357.
RGDi620065. Mpst.

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP97532.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG72ZCGB.
PhylomeDBiP97532.
TreeFamiTF315133.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12473.
BRENDAi2.8.1.2. 5301.
SABIO-RKP97532.

Miscellaneous databases

NextBioi622723.
PROiP97532.

Gene expression databases

GenevisibleiP97532. 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. "Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. cDNA cloning, overexpression, and site-directed mutagenesis."
    Nagahara N., Nishino T.
    J. Biol. Chem. 271:27395-27401(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 9-77 AND 147-285, ACTIVE SITE, MUTAGENESIS OF ARG-188; ARG-197; CYS-248 AND SER-250.
    Strain: Wistar.
    Tissue: Liver.
  2. "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: Ovary.
  3. "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: PROTEIN SEQUENCE OF 9-77 AND 147-285, CHARACTERIZATION.
    Strain: Wistar.
    Tissue: Liver.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 53-64 AND 119-164, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  5. "Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis."
    Nagahara N., Ito T., Kitamura H., Nishino T.
    Histochem. Cell Biol. 110:243-250(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis."
    Nagahara N., Katayama A.
    J. Biol. Chem. 280:34569-34576(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-65; CYS-155; CYS-248; CYS-255 AND CYS-264.
  7. "Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation."
    Nagahara N., Yoshii T., Abe Y., Matsumura T.
    J. Biol. Chem. 282:1561-1569(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBUNIT.
  8. "Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide."
    Shibuya N., Mikami Y., Kimura Y., Nagahara N., Kimura H.
    J. Biochem. 146:623-626(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiTHTM_RAT
AccessioniPrimary (citable) accession number: P97532
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 116 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.By similarity

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.