LOCUS       NM_003312               1125 bp    mRNA    linear   PRI 09-FEB-2025
DEFINITION  Homo sapiens thiosulfate sulfurtransferase (TST), transcript
            variant 1, mRNA.
ACCESSION   NM_003312
VERSION     NM_003312.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1125)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (bases 1 to 1125)
  AUTHORS   Kruithof,P.D., Lunev,S., Aguilar Lozano,S.P., de Assis Batista,F.,
            Al-Dahmani,Z.M., Joles,J.A., Dolga,A.M., Groves,M.R. and van
            Goor,H.
  TITLE     Unraveling the role of thiosulfate sulfurtransferase in metabolic
            diseases
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1866 (6), 165716 (2020)
   PUBMED   32061776
  REMARK    GeneRIF: Unraveling the role of thiosulfate sulfurtransferase in
            metabolic diseases.
            Review article
REFERENCE   3  (bases 1 to 1125)
  AUTHORS   Morton,N.M., Beltram,J., Carter,R.N., Michailidou,Z., Gorjanc,G.,
            McFadden,C., Barrios-Llerena,M.E., Rodriguez-Cuenca,S.,
            Gibbins,M.T., Aird,R.E., Moreno-Navarrete,J.M., Munger,S.C.,
            Svenson,K.L., Gastaldello,A., Ramage,L., Naredo,G., Zeyda,M.,
            Wang,Z.V., Howie,A.F., Saari,A., Sipila,P., Stulnig,T.M.,
            Gudnason,V., Kenyon,C.J., Seckl,J.R., Walker,B.R., Webster,S.P.,
            Dunbar,D.R., Churchill,G.A., Vidal-Puig,A., Fernandez-Real,J.M.,
            Emilsson,V. and Horvat,S.
  TITLE     Genetic identification of thiosulfate sulfurtransferase as an
            adipocyte-expressed antidiabetic target in mice selected for
            leanness
  JOURNAL   Nat Med 22 (7), 771-779 (2016)
   PUBMED   27270587
  REMARK    GeneRIF: TST mRNA expression in adipose tissue correlated
            positively with insulin sensitivity in adipose tissue and
            negatively with fat mass.
            Erratum:[Nat Med. 2018 Apr 10;24(4):525. doi: 10.1038/nm0418-525e..
            PMID: 29634685]
REFERENCE   4  (bases 1 to 1125)
  AUTHORS   Libiad,M., Sriraman,A. and Banerjee,R.
  TITLE     Polymorphic Variants of Human Rhodanese Exhibit Differences in
            Thermal Stability and Sulfur Transfer Kinetics
  JOURNAL   J Biol Chem 290 (39), 23579-23588 (2015)
   PUBMED   26269602
  REMARK    GeneRIF: show that polymorphic variations that are distant from the
            active site differentially modulate the sulfurtransferase activity
            of human rhodanese to cyanide versus sulfite
REFERENCE   5  (bases 1 to 1125)
  AUTHORS   Smirnov,A., Comte,C., Mager-Heckel,A.M., Addis,V.,
            Krasheninnikov,I.A., Martin,R.P., Entelis,N. and Tarassov,I.
  TITLE     Mitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA
            import into human mitochondria
  JOURNAL   J Biol Chem 285 (40), 30792-30803 (2010)
   PUBMED   20663881
  REMARK    GeneRIF: silencing of the rhodanese gene caused not only a
            proportional decrease of 5 S rRNA import but also a general
            inhibition of mitochondrial translation, indicating the functional
            importance of the imported 5 S rRNA inside the organelle.
REFERENCE   6  (bases 1 to 1125)
  AUTHORS   Aita,N., Ishii,K., Akamatsu,Y., Ogasawara,Y. and Tanabe,S.
  TITLE     Cloning and expression of human liver rhodanese cDNA
  JOURNAL   Biochem Biophys Res Commun 231 (1), 56-60 (1997)
   PUBMED   9070219
REFERENCE   7  (bases 1 to 1125)
  AUTHORS   Polo,C.F., Vazquez,E.S., Caballero,F., Gerez,E. and Battle,A.M.
  TITLE     Heme biosynthesis pathway regulation in a model of
            hepatocarcinogenesis pre-initiation
  JOURNAL   Comp Biochem Physiol B 103 (1), 251-256 (1992)
   PUBMED   1451437
REFERENCE   8  (bases 1 to 1125)
  AUTHORS   Pallini,R., Cannella,C. and Di Natale,P.
  TITLE     Synthesis of rhodanese in Hep 3B cells
  JOURNAL   Mol Cell Biochem 93 (1), 61-67 (1990)
   PUBMED   1691817
REFERENCE   9  (bases 1 to 1125)
  AUTHORS   Tanka,D. and Gatai,K.
  TITLE     Histochemical detection of thiosulphate sulphurtransferase
            (rhodanese) activity
  JOURNAL   Histochemistry 77 (2), 285-288 (1983)
   PUBMED   6573305
REFERENCE   10 (bases 1 to 1125)
  AUTHORS   Pecci,L., Pensa,B., Costa,M., Cignini,P.L. and Cannella,C.
  TITLE     Reaction of rhodanese with dithiothreitol
  JOURNAL   Biochim Biophys Acta 445 (1), 104-111 (1976)
   PUBMED   986188
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI869664.1 and BC010148.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NM_003312.5.
            
            Summary: This is one of two neighboring genes encoding similar
            proteins that each contain two rhodanese domains. The encoded
            protein is localized to the mitochondria and catalyzes the
            conversion of thiosulfate and cyanide to thiocyanate and sulfite.
            In addition, the protein interacts with 5S ribosomal RNA and
            facilitates its import into the mitochondria. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000862.1, AK223521.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000249042.8/
                                                  ENSP00000249042.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-17                AI869664.1         86-102
            18-1125             BC010148.2         1-1108
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     gene            1..1125
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="thiosulfate sulfurtransferase"
                     /db_xref="GeneID:7263"
                     /db_xref="HGNC:HGNC:12388"
                     /db_xref="MIM:180370"
     exon            1..48
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     exon            49..664
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     CDS             70..963
                     /gene="TST"
                     /gene_synonym="RDS"
                     /EC_number="2.8.1.1"
                     /note="thiosulfate sulfurtransferase (rhodanese);
                     epididymis secretory sperm binding protein"
                     /codon_start=1
                     /product="thiosulfate sulfurtransferase"
                     /protein_id="NP_003303.2"
                     /db_xref="CCDS:CCDS13938.1"
                     /db_xref="GeneID:7263"
                     /db_xref="HGNC:HGNC:12388"
                     /db_xref="MIM:180370"
                     /translation="MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREA
                     RKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGE
                     HLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRS
                     LLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLT
                     EDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSW
                     SEWFRRAPPESRVSQGKSEKA"
     exon            665..1125
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1105..1110
                     /regulatory_class="polyA_signal_sequence"
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="hexamer: AATAAA"
     polyA_site      1125
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="major polyA site"
ORIGIN      
        1 aacttctcca gccggccggg gcgagcgcca gcgcggcgtc cggggcgagt gacacgcaga
       61 gctgaagcca tggttcatca ggtgctctac cgggcgctgg tctccaccaa gtggctggcg
      121 gagtccatca ggactggcaa gctggggccc ggcctgcggg tgctggacgc gtcctggtac
      181 tcaccaggca cccgagaggc ccgcaaggag tacctcgagc gccacgtacc cggcgcctct
      241 ttctttgaca tagaagagtg ccgggacacg gcgtcgccct acgagatgat gctgcccagc
      301 gaggctggct tcgccgagta tgtgggccgc ctgggcatca gcaaccacac gcacgtggtg
      361 gtgtatgatg gtgaacacct gggcagcttc tatgctcccc gggtctggtg gatgttccgt
      421 gtgtttggcc accgcaccgt atcagtgctc aatggtggct tccggaactg gctgaaggag
      481 ggccacccgg tgacatccga gccctcacgc ccagaaccgg ccgtcttcaa agccacactg
      541 gaccgctccc tgctcaagac ctacgagcag gtgctggaga accttgaatc taagaggttc
      601 cagctggtgg attcaaggtc tcaagggcgg ttcctgggca ccgagccgga gccggatgca
      661 gtaggactgg actcgggcca tatccgtggt gccgtcaaca tgcctttcat ggacttcctg
      721 actgaggatg gcttcgagaa gggcccagaa gagctccgtg ctctgttcca gaccaagaag
      781 gtggatctct cgcagcctct cattgccacg tgccgcaagg gagtcaccgc ctgccacgtg
      841 gccttggctg cctacctctg cggcaagcct gatgtggccg tgtacgatgg ctcctggtcc
      901 gagtggtttc gccgggcccc cccagagagc cgtgtgtccc agggaaagtc tgagaaggcc
      961 tgagccgtga cctcttctgc ttactgtaac tgcggccggt ttagtgaccc catgacttac
     1021 agccggttct tacctcttag gtgaaggaga tgacatgttt ttagaattgc tgtgcaaggc
     1081 tcaccctctc tctgtcaaca ctggaataaa ctttgccttt tctga
//
