LOCUS       NM_001270483            1111 bp    mRNA    linear   PRI 09-FEB-2025
DEFINITION  Homo sapiens thiosulfate sulfurtransferase (TST), transcript
            variant 2, mRNA.
ACCESSION   NM_001270483
VERSION     NM_001270483.1
KEYWORDS    RefSeq.
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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 1111)
  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 BQ231617.1, Z73420.1 and
            AW070418.1.
            
            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 (2) differs in the 5' UTR,
            compared to variant 1. 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 :: BQ231617.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-586               BQ231617.1         26-611
            587-588             Z73420.1           17228-17229         c
            589-659             BQ231617.1         615-685
            660-691             Z73420.1           10313-10344         c
            692-867             AW070418.1         246-421             c
            868-881             Z73420.1           10123-10136         c
            882-1111            AW070418.1         1-230               c
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     gene            1..1111
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="thiosulfate sulfurtransferase"
                     /db_xref="GeneID:7263"
                     /db_xref="HGNC:HGNC:12388"
                     /db_xref="MIM:180370"
     exon            1..22
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     exon            23..638
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     CDS             44..937
                     /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_001257412.1"
                     /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            639..1105
                     /gene="TST"
                     /gene_synonym="RDS"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1079..1084
                     /regulatory_class="polyA_signal_sequence"
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="hexamer: AATAAA"
     polyA_site      1099
                     /gene="TST"
                     /gene_synonym="RDS"
                     /note="major polyA site"
ORIGIN      
        1 tgtctcttcc tggggcctct gggtgacacg cagagctgaa gccatggttc atcaggtgct
       61 ctaccgggcg ctggtctcca ccaagtggct ggcggagtcc atcaggactg gcaagctggg
      121 gcccggcctg cgggtgctgg acgcgtcctg gtactcacca ggcacccgag aggcccgcaa
      181 ggagtacctc gagcgccacg tacccggcgc ctctttcttt gacatagaag agtgccggga
      241 cacggcgtcg ccctacgaga tgatgctgcc cagcgaggct ggcttcgccg agtatgtggg
      301 ccgcctgggc atcagcaacc acacgcacgt ggtggtgtat gatggtgaac acctgggcag
      361 cttctatgct ccccgggtct ggtggatgtt ccgtgtgttt ggccaccgca ccgtatcagt
      421 gctcaatggt ggcttccgga actggctgaa ggagggccac ccggtgacat ccgagccctc
      481 acgcccagaa ccggccgtct tcaaagccac actggaccgc tccctgctca agacctacga
      541 gcaggtgctg gagaaccttg aatctaagag gttccagctg gtggattcaa ggtctcaagg
      601 gcggttcctg ggcaccgagc cggagccgga tgcagtagga ctggactcgg gccatatccg
      661 tggtgccgtc aacatgcctt tcatggactt cctgactgag gatggcttcg agaagggccc
      721 agaagagctc cgtgctctgt tccagaccaa gaaggtggat ctctcgcagc ctctcattgc
      781 cacgtgccgc aagggagtca ccgcctgcca cgtggccttg gctgcctacc tctgcggcaa
      841 gcctgatgtg gccgtgtacg atggctcctg gtccgagtgg tttcgccggg cccccccaga
      901 gagccgtgtg tcccagggaa agtctgagaa ggcctgagcc gtgacctctt ctgcttactg
      961 taactgcggc cggtttagtg accccatgac ttacagccgg ttcttacctc ttaggtgaag
     1021 gagatgacat gtttttagaa ttgctgtgca aggctcaccc tctctctgtc aacactggaa
     1081 taaactttgc cttttctgag tagtgaaaaa a
//
