THTR_RAT
ID THTR_RAT Reviewed; 297 AA.
AC P24329; Q5I0D4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese;
GN Name=Tst;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-297, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2018478; DOI=10.1042/bj2750227;
RA Weiland K.L., Dooley T.P.;
RT "Molecular cloning, sequencing and characterization of cDNA to rat liver
RT rhodanese, a thiosulphate sulphurtransferase.";
RL Biochem. J. 275:227-231(1991).
RN [3]
RP PROTEIN SEQUENCE OF 52-65; 123-132; 137-154; 177-183 AND 187-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP MUTAGENESIS OF ARG-249 AND LYS-250.
RC TISSUE=Liver;
RX PubMed=7608189; DOI=10.1074/jbc.270.27.16230;
RA Nagahara N., Okazaki T., Nishino T.;
RT "Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to
RT mitochondrial rhodanese. Striking similarity in active site amino acid
RT sequence and the increase in the mercaptopyruvate sulfurtransferase
RT activity of rhodanese by site-directed mutagenesis.";
RL J. Biol. Chem. 270:16230-16235(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP GLYCOSYLATION AT SER-35.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(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). Involved in the
CC formation of iron-sulfur complexes, cyanide detoxification or
CC modification of sulfur-containing enzymes. Other thiol compounds,
CC besides cyanide, can act as sulfur ion acceptors. Also has weak
CC mercaptopyruvate sulfurtransferase (MST) activity. {ECO:0000250,
CC ECO:0000269|PubMed:2018478}.
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 {ECO:0000269|PubMed:2018478}.
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; BC088449; AAH88449.1; -; mRNA.
DR EMBL; X56228; CAA39677.1; -; mRNA.
DR PIR; S15081; S15081.
DR RefSeq; NP_036940.1; NM_012808.1.
DR AlphaFoldDB; P24329; -.
DR SMR; P24329; -.
DR STRING; 10116.ENSRNOP00000039338; -.
DR CarbonylDB; P24329; -.
DR GlyGen; P24329; 1 site.
DR iPTMnet; P24329; -.
DR PhosphoSitePlus; P24329; -.
DR SwissPalm; P24329; -.
DR jPOST; P24329; -.
DR PaxDb; P24329; -.
DR PRIDE; P24329; -.
DR GeneID; 25274; -.
DR KEGG; rno:25274; -.
DR UCSC; RGD:3913; rat.
DR CTD; 7263; -.
DR RGD; 3913; Tst.
DR VEuPathDB; HostDB:ENSRNOG00000000186; -.
DR eggNOG; KOG1529; Eukaryota.
DR HOGENOM; CLU_031618_3_1_1; -.
DR InParanoid; P24329; -.
DR OMA; LLDVRWQ; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; P24329; -.
DR TreeFam; TF315133; -.
DR BRENDA; 2.8.1.1; 5301.
DR Reactome; R-RNO-1614558; Degradation of cysteine and homocysteine.
DR SABIO-RK; P24329; -.
DR PRO; PR:P24329; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000000186; Expressed in liver and 19 other tissues.
DR Genevisible; P24329; RN.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0016783; F:sulfurtransferase activity; TAS:Reactome.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:RGD.
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; Direct protein sequencing; Glycoprotein; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transferase.
FT CHAIN 1..297
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139397"
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:0000250|UniProtKB:Q16762"
FT MOD_RES 14
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00586"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 136
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 136
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 163
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 175
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 224
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 236
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52196"
FT CARBOHYD 35
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT MUTAGEN 249
FT /note="R->G: Unaltered rhodanese activity; increased MST
FT activity."
FT /evidence="ECO:0000269|PubMed:7608189"
FT MUTAGEN 250
FT /note="K->S: Decreased rhodanese activity; unaltered MST
FT activity."
FT /evidence="ECO:0000269|PubMed:7608189"
SQ SEQUENCE 297 AA; 33407 MW; AACD5FA8E8A762D6 CRC64;
MVHQVLYRAL VSTKWLAESI RSGKVGPSLR VLDASWYSPG TRQARKEYQE RHVPGASFFD
IEECRDTTSP YEMMLPSEAH FGDYVGNLGI SNDTHVVVYD GDDLGSFYAP RVWWMFRVFG
HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLNRS LLKTYEQVLE NLQSKRFQLV
DSRAQGRYLG TQPEPDAVGL DSGHIRGSVN VPFMNFLTED GFEKSPEELR AIFQDKKVDL
SQPLIATCRK GVTACHIALA AYLCGKPDVA VYDGSWSEWF RRAPPETRVS QGKSGKA
