THTR_MOUSE
ID THTR_MOUSE Reviewed; 297 AA.
AC P52196;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese;
GN Name=Tst;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7488186; DOI=10.1006/bbrc.1995.2734;
RA Dooley T.P., Nair S.K., Garcia R.E., Courtney B.C.;
RT "Mouse rhodanese gene (Tst): cDNA cloning, sequencing, and recombinant
RT protein expression.";
RL Biochem. Biophys. Res. Commun. 216:1101-1109(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-136; LYS-175; LYS-219;
RP LYS-224 AND LYS-237, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-136; LYS-163; LYS-175;
RP LYS-219; LYS-224; LYS-236 AND LYS-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Together with MRPL18, acts as a mitochondrial import factor
CC for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form
CC is able to bind to the 5S rRNA (By similarity). Formation of iron-
CC sulfur complexes and cyanide detoxification. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues.
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}.
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DR EMBL; U35741; AAC52342.1; -; mRNA.
DR EMBL; BC005644; AAH05644.1; -; mRNA.
DR CCDS; CCDS27614.1; -.
DR PIR; JC4398; JC4398.
DR RefSeq; NP_033463.1; NM_009437.4.
DR AlphaFoldDB; P52196; -.
DR SMR; P52196; -.
DR STRING; 10090.ENSMUSP00000055743; -.
DR GlyGen; P52196; 1 site.
DR iPTMnet; P52196; -.
DR PhosphoSitePlus; P52196; -.
DR SwissPalm; P52196; -.
DR REPRODUCTION-2DPAGE; P52196; -.
DR SWISS-2DPAGE; P52196; -.
DR jPOST; P52196; -.
DR PaxDb; P52196; -.
DR PeptideAtlas; P52196; -.
DR PRIDE; P52196; -.
DR ProteomicsDB; 258876; -.
DR Antibodypedia; 302; 170 antibodies from 28 providers.
DR DNASU; 22117; -.
DR Ensembl; ENSMUST00000058659; ENSMUSP00000055743; ENSMUSG00000044986.
DR GeneID; 22117; -.
DR KEGG; mmu:22117; -.
DR UCSC; uc007wpd.1; mouse.
DR CTD; 7263; -.
DR MGI; MGI:98852; Tst.
DR VEuPathDB; HostDB:ENSMUSG00000044986; -.
DR eggNOG; KOG1529; Eukaryota.
DR GeneTree; ENSGT00510000046773; -.
DR HOGENOM; CLU_031618_3_1_1; -.
DR InParanoid; P52196; -.
DR OMA; LLDVRWQ; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; P52196; -.
DR TreeFam; TF315133; -.
DR Reactome; R-MMU-1614558; Degradation of cysteine and homocysteine.
DR SABIO-RK; P52196; -.
DR BioGRID-ORCS; 22117; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tst; mouse.
DR PRO; PR:P52196; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P52196; protein.
DR Bgee; ENSMUSG00000044986; Expressed in olfactory epithelium and 220 other tissues.
DR ExpressionAtlas; P52196; baseline and differential.
DR Genevisible; P52196; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR GO; GO:0035928; P:rRNA import into mitochondrion; ISS:UniProtKB.
DR GO; GO:0051029; P:rRNA transport; ISS:UniProtKB.
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 Acetylation; Glycoprotein; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transferase.
FT CHAIN 1..297
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139396"
FT DOMAIN 25..143
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 173..288
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 144..159
FT /note="Hinge"
FT ACT_SITE 248
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 14
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24329"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 219
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 219
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 236
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CARBOHYD 35
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33466 MW; B88AA16C61086F51 CRC64;
MVHQVLYRAL VSTKWLAESI RSGRLGPSLR VLDASWYSPG TRQARKEYQE RHVPGASFFD
IEECRDTTSP YEMMLPSEAH FGDYVGNLGI SNDTHVVVYD GDDLGSFYAP RVWWMFRVFG
HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLNLS LLKTYEQVLE NLQSKRFQLV
DSRAQGRYLG TQPEPDIVGL DSGHIRGSVN MPFMDFLTKD GFEKSPEELR AIFQDKKVDL
SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPETRVS QGKSGKA
