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Protein

3-mercaptopyruvate sulfurtransferase

Gene

MPST

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

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.

Sites

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

GO - Molecular functioni

  • 3-mercaptopyruvate sulfurtransferase activity Source: UniProtKB-EC
  • thiosulfate sulfurtransferase activity Source: ProtInc

GO - Biological processi

  • cyanate catabolic process Source: ProtInc
  • hydrogen sulfide biosynthetic process Source: UniProtKB
  • kidney development Source: Ensembl
  • liver development Source: Ensembl
  • response to toxic substance Source: ProtInc
  • spinal cord development Source: Ensembl
  • transsulfuration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:HS05177-MONOMER.
ZFISH:HS05177-MONOMER.
BRENDAi2.8.1.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
3-mercaptopyruvate sulfurtransferase (EC:2.8.1.2)
Short name:
MST
Gene namesi
Name:MPST
Synonyms:TST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:7223. MPST.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • neuron projection Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Mitochondrion, Synapse, Synaptosome

Pathology & Biotechi

Involvement in diseasei

Aberrant MPST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases have associated mental retardation (PubMed:4973015 and PubMed:6945862).

Organism-specific databases

DisGeNETi4357.
MIMi249650. phenotype.
OpenTargetsiENSG00000128309.
PharmGKBiPA30928.

Polymorphism and mutation databases

BioMutaiMPST.
DMDMi6226903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001393982 – 2973-mercaptopyruvate sulfurtransferaseAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei3PhosphoserineCombined sources1
Modified residuei35PhosphoserineCombined sources1
Modified residuei40N6-acetyllysine; alternateBy similarity1
Modified residuei40N6-succinyllysine; alternateBy similarity1
Modified residuei146N6-succinyllysineBy similarity1
Modified residuei164N6-succinyllysineBy similarity1
Disulfide bondi264Interchain (with C-264); redox-activeBy similarity
Isoform 2 (identifier: P25325-2)
Modified residuei15PhosphoserineCombined sources1
Modified residuei23PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP25325.
PaxDbiP25325.
PeptideAtlasiP25325.
PRIDEiP25325.

2D gel databases

OGPiP25325.
REPRODUCTION-2DPAGEIPI00165360.

PTM databases

iPTMnetiP25325.
PhosphoSitePlusiP25325.
SwissPalmiP25325.

Expressioni

Gene expression databases

BgeeiENSG00000128309.
CleanExiHS_MPST.
ExpressionAtlasiP25325. baseline and differential.
GenevisibleiP25325. HS.

Organism-specific databases

HPAiHPA001240.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110497. 15 interactors.
DIPiDIP-613N.
IntActiP25325. 2 interactors.
STRINGi9606.ENSP00000380318.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 21Combined sources9
Beta strandi29 – 33Combined sources5
Helixi39 – 41Combined sources3
Helixi45 – 51Combined sources7
Turni62 – 64Combined sources3
Beta strandi71 – 74Combined sources4
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 – 189Combined sources4
Helixi213 – 216Combined sources4
Beta strandi219 – 221Combined sources3
Helixi226 – 235Combined sources10
Beta strandi244 – 247Combined sources4
Beta strandi249 – 252Combined sources4
Helixi255 – 263Combined sources9
Beta strandi271 – 274Combined sources4
Helixi275 – 283Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OLHX-ray2.50A11-289[»]
4JGTX-ray2.16A/B/C11-289[»]
ProteinModelPortaliP25325.
SMRiP25325.
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

Sequence similaritiesi

Contains 2 rhodanese domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP25325.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG091G0X2Q.
PhylomeDBiP25325.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25325-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE
60 70 80 90 100
ERHIPGAAFF DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY
110 120 130 140 150
DASDQGLYSA PRVWWMFRAF GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA
160 170 180 190 200
PAEFRAQLDP AFIKTYEDIK ENLESRRFQV VDSRATGRFR GTEPEPRDGI
210 220 230 240 250
EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL SKPLVATCGS
260 270 280 290
GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH
Length:297
Mass (Da):33,178
Last modified:January 23, 2007 - v3
Checksum:i2313CC15A47A42EA
GO
Isoform 2 (identifier: P25325-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAEPGSRESETRARSPSVAAM

Show »
Length:317
Mass (Da):35,250
Checksum:iCDDCDD4B3AAC2869
GO

Sequence cautioni

The sequence AAH16737 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAG30409 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti46 – 48RRE → TQ in CAA42060 (PubMed:1953758).Curated3
Sequence conflicti205I → T in BAG51564 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0550271M → MAEPGSRESETRARSPSVAA M in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59434 mRNA. Translation: CAA42060.1.
BT019636 mRNA. Translation: AAV38442.1.
AK055733 mRNA. Translation: BAG51564.1.
CR541712 mRNA. Translation: CAG46513.1.
Z73420 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW60133.1.
CH471095 Genomic DNA. Translation: EAW60134.1.
CH471095 Genomic DNA. Translation: EAW60135.1.
BC003508 mRNA. Translation: AAH03508.1.
BC016737 mRNA. Translation: AAH16737.1. Different initiation.
BC018717 mRNA. Translation: AAH18717.1.
CR456523 mRNA. Translation: CAG30409.1. Different initiation.
CCDSiCCDS13939.1. [P25325-1]
CCDS46703.1. [P25325-2]
PIRiJH0461. ROHU.
RefSeqiNP_001013454.1. NM_001013436.2. [P25325-1]
NP_001123989.1. NM_001130517.2. [P25325-1]
NP_066949.2. NM_021126.5. [P25325-2]
XP_005261667.1. XM_005261610.3. [P25325-1]
UniGeneiHs.248267.

Genome annotation databases

EnsembliENST00000341116; ENSP00000342333; ENSG00000128309. [P25325-1]
ENST00000397225; ENSP00000380402; ENSG00000128309. [P25325-1]
ENST00000401419; ENSP00000384812; ENSG00000128309. [P25325-1]
ENST00000404802; ENSP00000383950; ENSG00000128309. [P25325-1]
ENST00000429360; ENSP00000411719; ENSG00000128309. [P25325-2]
GeneIDi4357.
KEGGihsa:4357.
UCSCiuc003aql.5. human. [P25325-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59434 mRNA. Translation: CAA42060.1.
BT019636 mRNA. Translation: AAV38442.1.
AK055733 mRNA. Translation: BAG51564.1.
CR541712 mRNA. Translation: CAG46513.1.
Z73420 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW60133.1.
CH471095 Genomic DNA. Translation: EAW60134.1.
CH471095 Genomic DNA. Translation: EAW60135.1.
BC003508 mRNA. Translation: AAH03508.1.
BC016737 mRNA. Translation: AAH16737.1. Different initiation.
BC018717 mRNA. Translation: AAH18717.1.
CR456523 mRNA. Translation: CAG30409.1. Different initiation.
CCDSiCCDS13939.1. [P25325-1]
CCDS46703.1. [P25325-2]
PIRiJH0461. ROHU.
RefSeqiNP_001013454.1. NM_001013436.2. [P25325-1]
NP_001123989.1. NM_001130517.2. [P25325-1]
NP_066949.2. NM_021126.5. [P25325-2]
XP_005261667.1. XM_005261610.3. [P25325-1]
UniGeneiHs.248267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OLHX-ray2.50A11-289[»]
4JGTX-ray2.16A/B/C11-289[»]
ProteinModelPortaliP25325.
SMRiP25325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110497. 15 interactors.
DIPiDIP-613N.
IntActiP25325. 2 interactors.
STRINGi9606.ENSP00000380318.

PTM databases

iPTMnetiP25325.
PhosphoSitePlusiP25325.
SwissPalmiP25325.

Polymorphism and mutation databases

BioMutaiMPST.
DMDMi6226903.

2D gel databases

OGPiP25325.
REPRODUCTION-2DPAGEIPI00165360.

Proteomic databases

EPDiP25325.
PaxDbiP25325.
PeptideAtlasiP25325.
PRIDEiP25325.

Protocols and materials databases

DNASUi4357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341116; ENSP00000342333; ENSG00000128309. [P25325-1]
ENST00000397225; ENSP00000380402; ENSG00000128309. [P25325-1]
ENST00000401419; ENSP00000384812; ENSG00000128309. [P25325-1]
ENST00000404802; ENSP00000383950; ENSG00000128309. [P25325-1]
ENST00000429360; ENSP00000411719; ENSG00000128309. [P25325-2]
GeneIDi4357.
KEGGihsa:4357.
UCSCiuc003aql.5. human. [P25325-1]

Organism-specific databases

CTDi4357.
DisGeNETi4357.
GeneCardsiMPST.
HGNCiHGNC:7223. MPST.
HPAiHPA001240.
MIMi249650. phenotype.
602496. gene.
neXtProtiNX_P25325.
OpenTargetsiENSG00000128309.
PharmGKBiPA30928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1529. Eukaryota.
COG2897. LUCA.
GeneTreeiENSGT00510000046773.
HOGENOMiHOG000157237.
HOVERGENiHBG002345.
InParanoidiP25325.
KOiK01011.
OMAiSWGEWGS.
OrthoDBiEOG091G0X2Q.
PhylomeDBiP25325.
TreeFamiTF315133.

Enzyme and pathway databases

BioCyciMetaCyc:HS05177-MONOMER.
ZFISH:HS05177-MONOMER.
BRENDAi2.8.1.2. 2681.

Miscellaneous databases

ChiTaRSiMPST. human.
GeneWikiiMPST.
GenomeRNAii4357.
PROiP25325.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000128309.
CleanExiHS_MPST.
ExpressionAtlasiP25325. baseline and differential.
GenevisibleiP25325. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P25325
Secondary accession number(s): A8MZ34
, B3KP52, J3KPV7, O75750, Q6FHN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Caution

Was originally thought to be rhodanese.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.