THTM_HUMAN
ID THTM_HUMAN Reviewed; 297 AA.
AC P25325; A8MZ34; B3KP52; J3KPV7; O75750; Q6FHN9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2 {ECO:0000250|UniProtKB:P97532};
GN Name=MPST; Synonyms=TST2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1953758; DOI=10.1016/s0006-291x(05)81148-9;
RA Pallini R., Guazzi G.C., Cannella C., Cacace M.G.;
RT "Cloning and sequence analysis of the human liver rhodanese: comparison
RT with the bovine and chicken enzymes.";
RL Biochem. Biophys. Res. Commun. 180:887-893(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Muscle, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [9]
RP PROTEIN SEQUENCE OF 89-112 AND 119-133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4973015; DOI=10.1001/archpedi.1969.02100030068007;
RA Ampola M.G., Efron M.L., Bixby E.M., Meshorer E.;
RT "Mental deficiency and a new aminoaciduria.";
RL Am. J. Dis. Child. 117:66-70(1969).
RN [11]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4690911; DOI=10.1016/0009-8981(73)90480-4;
RA Niederwiesler A., Giliberti P., Baerlocher K.;
RT "beta-Mercaptolactate cysteine disulfiduria in two normal sisters.
RT Isolation and characterization of beta-mercaptolactate cysteine
RT disulfide.";
RL Clin. Chim. Acta 43:405-416(1973).
RN [12]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=6945862; DOI=10.1016/0006-2944(81)90035-1;
RA Hannestad U., Martensson J., Sjodahl R., Sorbo B.;
RT "3-mercaptolactate cysteine disulfiduria: biochemical studies on affected
RT and unaffected members of a family.";
RL Biochem. Med. 26:106-114(1981).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-35, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-15 AND SER-23 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 11-289.
RG Structural genomics consortium (SGC);
RT "Human 3-mercaptopyruvate sulfurtransferase.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol
CC compounds. Also has weak rhodanese activity. Detoxifies cyanide and is
CC required for thiosulfate biosynthesis. Acts as an antioxidant. In
CC combination with cysteine aminotransferase (CAT), contributes to the
CC catabolism of cysteine and is an important producer of hydrogen sulfide
CC in the brain, retina and vascular endothelial cells. Hydrogen sulfide
CC H(2)S is an important synaptic modulator, signaling molecule, smooth
CC muscle contractor and neuroprotectant. Its production by the 3MST/CAT
CC pathway is regulated by calcium ions. {ECO:0000250|UniProtKB:P97532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol =
CC [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate;
CC Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2;
CC Evidence={ECO:0000250|UniProtKB:P97532};
CC -!- ACTIVITY REGULATION: By oxidative stress, and thioredoxin. Under
CC oxidative stress conditions, the catalytic cysteine site is converted
CC to a sulfenate which inhibits the MPST enzyme activity. Reduced
CC thioredoxin cleaves an intersubunit disulfide bond to turn on the redox
CC switch and reactivate the enzyme. {ECO:0000250|UniProtKB:P97532}.
CC -!- SUBUNIT: Monomer (active form). Homodimer; disulfide-linked (inactive
CC form). {ECO:0000250|UniProtKB:P97532}.
CC -!- INTERACTION:
CC P25325; O96006: ZBED1; NbExp=3; IntAct=EBI-2515082, EBI-740037;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97532}.
CC Mitochondrion {ECO:0000250|UniProtKB:P97532}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q99J99}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25325-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25325-2; Sequence=VSP_055027;
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Note=Aberrant MPST activity is found in a few cases of
CC mercaptolactate-cysteine disulfiduria (MCDU) characterized by the
CC appearance of large quantaties of the sulfur-containing amino acid,
CC beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4973015,
CC PubMed:4690911 and PubMed:6945862). Some cases have associated
CC intellectual disability (PubMed:4973015 and PubMed:6945862).
CC -!- MISCELLANEOUS: Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are
CC required to release hydrogen sulfide from the persulfide intermediate.
CC {ECO:0000250|UniProtKB:Q99J99}.
CC -!- CAUTION: Was originally thought to be rhodanese.
CC {ECO:0000305|PubMed:1953758}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16737.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG30409.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X59434; CAA42060.1; -; mRNA.
DR EMBL; BT019636; AAV38442.1; -; mRNA.
DR EMBL; AK055733; BAG51564.1; -; mRNA.
DR EMBL; CR541712; CAG46513.1; -; mRNA.
DR EMBL; Z73420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60133.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60134.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW60135.1; -; Genomic_DNA.
DR EMBL; BC003508; AAH03508.1; -; mRNA.
DR EMBL; BC016737; AAH16737.1; ALT_INIT; mRNA.
DR EMBL; BC018717; AAH18717.1; -; mRNA.
DR EMBL; CR456523; CAG30409.1; ALT_INIT; mRNA.
DR CCDS; CCDS13939.1; -. [P25325-1]
DR CCDS; CCDS46703.1; -. [P25325-2]
DR PIR; JH0461; ROHU.
DR RefSeq; NP_001013454.1; NM_001013436.2. [P25325-1]
DR RefSeq; NP_001123989.1; NM_001130517.2. [P25325-1]
DR RefSeq; NP_066949.2; NM_021126.5. [P25325-2]
DR RefSeq; XP_005261667.1; XM_005261610.3.
DR PDB; 3OLH; X-ray; 2.50 A; A=11-289.
DR PDB; 4JGT; X-ray; 2.16 A; A/B/C=11-289.
DR PDBsum; 3OLH; -.
DR PDBsum; 4JGT; -.
DR AlphaFoldDB; P25325; -.
DR SMR; P25325; -.
DR BioGRID; 110497; 58.
DR DIP; DIP-613N; -.
DR IntAct; P25325; 7.
DR MINT; P25325; -.
DR STRING; 9606.ENSP00000380402; -.
DR GuidetoPHARMACOLOGY; 1446; -.
DR GlyGen; P25325; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P25325; -.
DR PhosphoSitePlus; P25325; -.
DR SwissPalm; P25325; -.
DR BioMuta; MPST; -.
DR DMDM; 6226903; -.
DR OGP; P25325; -.
DR REPRODUCTION-2DPAGE; IPI00165360; -.
DR EPD; P25325; -.
DR jPOST; P25325; -.
DR MassIVE; P25325; -.
DR MaxQB; P25325; -.
DR PaxDb; P25325; -.
DR PeptideAtlas; P25325; -.
DR PRIDE; P25325; -.
DR ProteomicsDB; 54268; -. [P25325-1]
DR Antibodypedia; 223; 155 antibodies from 24 providers.
DR DNASU; 4357; -.
DR Ensembl; ENST00000341116.7; ENSP00000342333.3; ENSG00000128309.17. [P25325-1]
DR Ensembl; ENST00000397225.2; ENSP00000380402.2; ENSG00000128309.17. [P25325-1]
DR Ensembl; ENST00000401419.7; ENSP00000384812.3; ENSG00000128309.17. [P25325-1]
DR Ensembl; ENST00000404802.7; ENSP00000383950.3; ENSG00000128309.17. [P25325-1]
DR Ensembl; ENST00000429360.6; ENSP00000411719.3; ENSG00000128309.17. [P25325-2]
DR GeneID; 4357; -.
DR KEGG; hsa:4357; -.
DR MANE-Select; ENST00000429360.6; ENSP00000411719.3; NM_021126.8; NP_066949.2. [P25325-2]
DR UCSC; uc003aql.5; human. [P25325-1]
DR CTD; 4357; -.
DR DisGeNET; 4357; -.
DR GeneCards; MPST; -.
DR HGNC; HGNC:7223; MPST.
DR HPA; ENSG00000128309; Tissue enhanced (liver).
DR MIM; 249650; phenotype.
DR MIM; 602496; gene.
DR neXtProt; NX_P25325; -.
DR OpenTargets; ENSG00000128309; -.
DR PharmGKB; PA30928; -.
DR VEuPathDB; HostDB:ENSG00000128309; -.
DR eggNOG; KOG1529; Eukaryota.
DR GeneTree; ENSGT00510000046773; -.
DR HOGENOM; CLU_031618_3_1_1; -.
DR InParanoid; P25325; -.
DR OMA; QRPGHVP; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; P25325; -.
DR TreeFam; TF315133; -.
DR BioCyc; MetaCyc:HS05177-MON; -.
DR BRENDA; 2.8.1.2; 2681.
DR PathwayCommons; P25325; -.
DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR SignaLink; P25325; -.
DR BioGRID-ORCS; 4357; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; MPST; human.
DR GeneWiki; MPST; -.
DR GenomeRNAi; 4357; -.
DR Pharos; P25325; Tchem.
DR PRO; PR:P25325; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P25325; protein.
DR Bgee; ENSG00000128309; Expressed in mucosa of transverse colon and 197 other tissues.
DR ExpressionAtlas; P25325; baseline and differential.
DR Genevisible; P25325; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0009440; P:cyanate catabolic process; TAS:ProtInc.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; PTHR11364; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Mitochondrion; Phosphoprotein;
KW Redox-active center; Reference proteome; Repeat; Synapse; Synaptosome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..297
FT /note="3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139398"
FT DOMAIN 25..144
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 174..288
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 145..160
FT /note="Hinge"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99J99"
FT MOD_RES 40
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99J99"
FT MOD_RES 146
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J99"
FT MOD_RES 164
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99J99"
FT DISULFID 264
FT /note="Interchain (with C-264); redox-active"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MAEPGSRESETRARSPSVAAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055027"
FT CONFLICT 46..48
FT /note="RRE -> TQ (in Ref. 1; CAA42060)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="I -> T (in Ref. 3; BAG51564)"
FT /evidence="ECO:0000305"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:4JGT"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3OLH"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3OLH"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:4JGT"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4JGT"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:4JGT"
FT MOD_RES P25325-2:15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES P25325-2:23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 297 AA; 33178 MW; 2313CC15A47A42EA CRC64;
MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE ERHIPGAAFF
DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY DASDQGLYSA PRVWWMFRAF
GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA PAEFRAQLDP AFIKTYEDIK ENLESRRFQV
VDSRATGRFR GTEPEPRDGI EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL
SKPLVATCGS GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH
