LOCUS       NM_017210               1862 bp    mRNA    linear   ROD 07-FEB-2025
DEFINITION  Rattus norvegicus iodothyronine deiodinase 3 (Dio3), mRNA.
ACCESSION   NM_017210
VERSION     NM_017210.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (bases 1 to 1862)
  AUTHORS   Wang,G., Duan,J., Cao,K., Gao,T., Jiang,A., Xu,Y., Zhu,Z. and Yu,W.
  TITLE     [Inhibition of type 3 deiodinase expression can improve
            mitochondrial function in skeletal muscle of sepsis by
            up-regulating peroxisome proliferator-activated receptor-gamma
            coactivator-1alpha]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 36 (8), 841-847 (2024)
   PUBMED   39238408
  REMARK    GeneRIF: [Inhibition of type 3 deiodinase expression can improve
            mitochondrial function in skeletal muscle of sepsis by
            up-regulating peroxisome proliferator-activated receptor-gamma
            coactivator-1alpha].
REFERENCE   2  (bases 1 to 1862)
  AUTHORS   Di Munno,C., Busiello,R.A., Calonne,J., Salzano,A.M.,
            Miles-Chan,J., Scaloni,A., Ceccarelli,M., de Lange,P., Lombardi,A.,
            Senese,R., Cioffi,F., Visser,T.J., Peeters,R.P., Dulloo,A.G. and
            Silvestri,E.
  TITLE     Adaptive Thermogenesis Driving Catch-Up Fat Is Associated With
            Increased Muscle Type 3 and Decreased Hepatic Type 1 Iodothyronine
            Deiodinase Activities: A Functional and Proteomic Study
  JOURNAL   Front Endocrinol (Lausanne) 12, 631176 (2021)
   PUBMED   33746903
  REMARK    GeneRIF: Adaptive Thermogenesis Driving Catch-Up Fat Is Associated
            With Increased Muscle Type 3 and Decreased Hepatic Type 1
            Iodothyronine Deiodinase Activities: A Functional and Proteomic
            Study.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 1862)
  AUTHORS   Schweizer,U., Schlicker,C., Braun,D., Kohrle,J. and Steegborn,C.
  TITLE     Crystal structure of mammalian selenocysteine-dependent
            iodothyronine deiodinase suggests a peroxiredoxin-like catalytic
            mechanism
  JOURNAL   Proc Natl Acad Sci U S A 111 (29), 10526-10531 (2014)
   PUBMED   25002520
REFERENCE   4  (bases 1 to 1862)
  AUTHORS   Tunc-Ozcan,E., Ullmann,T.M., Shukla,P.K. and Redei,E.E.
  TITLE     Low-dose thyroxine attenuates autism-associated adverse effects of
            fetal alcohol in male offspring's social behavior and hippocampal
            gene expression
  JOURNAL   Alcohol Clin Exp Res 37 (11), 1986-1995 (2013)
   PUBMED   23763370
REFERENCE   5  (bases 1 to 1862)
  AUTHORS   Hernandez,A., Garcia,B. and Obregon,M.J.
  TITLE     Gene expression from the imprinted Dio3 locus is associated with
            cell proliferation of cultured brown adipocytes
  JOURNAL   Endocrinology 148 (8), 3968-3976 (2007)
   PUBMED   17510246
  REMARK    GeneRIF: genomic imprinting and gene expression at the Dlk1/Dio3
            imprinted domain may play a role in the regulation of adipocyte
            proliferation and differentiation
REFERENCE   6  (bases 1 to 1862)
  AUTHORS   Hernandez,A., Martinez,M.E., Fiering,S., Galton,V.A. and St
            Germain,D.
  TITLE     Type 3 deiodinase is critical for the maturation and function of
            the thyroid axis
  JOURNAL   J Clin Invest 116 (2), 476-484 (2006)
   PUBMED   16410833
REFERENCE   7  (bases 1 to 1862)
  AUTHORS   Wasco,E.C., Martinez,E., Grant,K.S., St Germain,E.A., St
            Germain,D.L. and Galton,V.A.
  TITLE     Determinants of iodothyronine deiodinase activities in rodent
            uterus
  JOURNAL   Endocrinology 144 (10), 4253-4261 (2003)
   PUBMED   12959985
  REMARK    GeneRIF: Induction of D3 activity begins immediately after
            implantation and increases markedly over next 72 hours. In
            spontaneously cycling female rats, both D2 and D3 were observed to
            be 3- to 8-fold higher in proestrus, compared with diestrus.
REFERENCE   8  (bases 1 to 1862)
  AUTHORS   Friedrichsen,S., Christ,S., Heuer,H., Schafer,M.K., Mansouri,A.,
            Bauer,K. and Visser,T.J.
  TITLE     Regulation of iodothyronine deiodinases in the Pax8-/- mouse model
            of congenital hypothyroidism
  JOURNAL   Endocrinology 144 (3), 777-784 (2003)
   PUBMED   12586753
REFERENCE   9  (bases 1 to 1862)
  AUTHORS   Hernandez,A., Fiering,S., Martinez,E., Galton,V.A. and St
            Germain,D.
  TITLE     The gene locus encoding iodothyronine deiodinase type 3 (Dio3) is
            imprinted in the fetus and expresses antisense transcripts
  JOURNAL   Endocrinology 143 (11), 4483-4486 (2002)
   PUBMED   12399446
REFERENCE   10 (bases 1 to 1862)
  AUTHORS   Croteau,W., Whittemore,S.L., Schneider,M.J. and St Germain,D.L.
  TITLE     Cloning and expression of a cDNA for a mammalian type III
            iodothyronine deiodinase
  JOURNAL   J Biol Chem 270 (28), 16569-16575 (1995)
   PUBMED   7622463
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JAXUCZ010000006.1.
            
            On Jun 24, 2016 this sequence version replaced NM_017210.3.
            
            Summary: This is an intronless, imprinted gene that is
            preferentially expressed from the paternal allele. The encoded
            protein belongs to the iodothyronine deiodinase family, and
            catalyzes the inactivation of thyroid hormone by inner ring
            deiodination of the prohormone thyroxine (T4) and the bioactive
            hormone 3,3',5-triiodothyronine (T3) to inactive metabolites,
            3,3',5' triiodothyronine (RT3) and 3,3'-diiodothyronine (T2),
            respectively. It is highly expressed in placenta, fetal and
            neonatal tissues, and thought to prevent premature exposure of
            developing fetal tissues to adult levels of thyroid hormones. It
            thus plays a critical role in mammalian development by regulating
            circulating fetal thyroid hormone concentration. This protein is a
            selenoprotein, containing the rare selenocysteine (Sec) amino acid
            at its active site. Sec is encoded by the UGA codon, which normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, designated the Sec
            insertion sequence (SECIS) element, that is necessary for the
            recognition of UGA as a Sec codon rather than as a stop signal.
            [provided by RefSeq, Jun 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            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 is intronless :: U24282.1, SRR26643429.25078.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene                  :: PMID: 17510246
            protein contains selenocysteine :: PMID: 7622463
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-1862              JAXUCZ010000006.1  135107072-135108933
FEATURES             Location/Qualifiers
     source          1..1862
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q32"
     gene            1..1862
                     /gene="Dio3"
                     /gene_synonym="5DIII; DIOIII"
                     /note="iodothyronine deiodinase 3"
                     /db_xref="GeneID:29475"
                     /db_xref="RGD:68420"
     exon            1..1862
                     /gene="Dio3"
                     /gene_synonym="5DIII; DIOIII"
                     /inference="alignment:Splign:2.1.0"
     CDS             3..917
                     /gene="Dio3"
                     /gene_synonym="5DIII; DIOIII"
                     /EC_number="1.21.99.3"
                     /note="UGA stop codon recoded as selenocysteine; type III
                     iodothyronine deiodinase; type 3 DI; type-III
                     5'-deiodinase; deiodinase, iodothyronine, type 3;
                     deiodinase, iodothyronine, type III"
                     /codon_start=1
                     /transl_except=(pos:510..512,aa:Sec)
                     /product="thyroxine 5-deiodinase"
                     /protein_id="NP_058906.3"
                     /db_xref="GeneID:29475"
                     /db_xref="RGD:68420"
                     /translation="MPRQAASRLVVGEGEGPPGASGPAATMLRSLLLHSLRLCAQTAS
                     CLVLFPRFLGTAFMLWLLDFLCIRKHFLRRRHPDHPEPEVELNSEGEEMPPDDPPICV
                     SDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVRPDGFQSQRILDYAQGTRP
                     LVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYVIPQ
                     HRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRG
                     PDGYQVSELRTWLERYDEQLHGTRPRRL"
     regulatory      1433..1530
                     /regulatory_class="recoding_stimulatory_region"
                     /gene="Dio3"
                     /gene_synonym="5DIII; DIOIII"
                     /note="SECIS_element"
                     /function="essential for recoding UGA to specify
                     selenocysteine"
ORIGIN      
        1 agatgcctcg ccaggccgcc tcgaggttgg tggtcggaga aggtgaaggg cccccggggg
       61 cttcggggcc cgcggccacc atgctgcgct ccctgctgct tcactctctg aggctctgcg
      121 cccagaccgc ctcgtgcctc gtgctgttcc cgcgcttcct aggcacggcc ttcatgctct
      181 ggcttttaga tttcttgtgc atccgcaagc atttcctgcg ccgtcgtcat cctgaccacc
      241 ccgagcccga agtagagctc aacagtgaag gtgaggagat gccccctgac gacccaccca
      301 tctgcgtatc cgacgacaac cggctgtgca ccctggcctc tctgaaggcc gtgtggcatg
      361 gccagaagtt ggatttcttc aagcaggccc atgagggtgg cccagcacct aactcggagg
      421 tcgtccggcc tgatggcttc cagagccagc gcatcctcga ctacgcacaa gggacccgcc
      481 cgttggtgct caattttggc agctgtacct gaccaccgtt catggcgcgg atgagcgcct
      541 tccagcgcct ggtcaccaag taccagcgcg acgttgactt ccttatcatc tacatcgagg
      601 aagcccaccc atccgatggc tgggtcacca cagattcacc ctacgtcatc ccacagcacc
      661 gcagcttgga ggaccgtgtc agcgcagcaa gagtacttca gcaaggcgca cctggctgtg
      721 ctctggttct ggacacgatg gccaactcca gcagttccgc atatggtgcc tattttgagc
      781 gcctctacgt catccagagc ggcaccatca tgtaccaggg aggccgtggc cccgacggtt
      841 accaggtgtc tgagttgcgc acttggttgg agcgctatga cgagcagttg catggtacta
      901 ggccacgtcg actctaaaaa accaagggac aagtgactga attggtgggc tgggtcttct
      961 gggccttcga agctcatgtg cgaatgctcc aaaagaagtc aaggttttca ggggtcccgt
     1021 gacacagatg agcacagcca cagaactcag gctgagtctg gctaacttga gactctgcta
     1081 tagtgactcc cttttggtac tttttggctt gctttctgga gcattgctgt ggctagaact
     1141 ggcaactttg tccctgctga agtttacctg ctggactttc tgacacctgc tccccagcgc
     1201 tatttcagca aagcgcaata agtcgccagc atctcacagc tcgggacttg ttggccacgc
     1261 ccgcgcgccc tgagcgcagc tgggttccag cagcgcctcc ggctctagct agttgcctgg
     1321 cacccacctg tcgagagcag ggagtcctgc tgcttttgtg tttatttctt atccctgggt
     1381 tgggggaggg gctcaagata aagggtgggc agggtaattt ccccgcctag ctttaggtgc
     1441 gctggaaccc tggctgctga tgacgaaccg cctctaactg ggcttgacca cgggtcggct
     1501 ctgaattgca gaggggctcg aaacagcgcc taaagtaaga gggggaaagt gctctgggtt
     1561 ccacggggaa ccgtcaaaaa cagggtgaaa gagggacatg gtaaggggtg ggcttcagga
     1621 ccaaaggaag cggcttgggg cactggcgag gttcgcaggt ccccaagagg gaggctagga
     1681 ctccttggag aagggattaa ttggttcgaa gacaaggaga tggggaagag cctgggagtc
     1741 ctaagcagaa agagcgggtt gtggggtggg gtgaaaacca gtcagtgaat gttgtgttgg
     1801 aaacgttcct tgtgtataaa cttttaagtt acaataataa agacttgaag gaagttgctc
     1861 tg
//
