ID IOD1_RAT Reviewed; 257 AA. AC P24389; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 27-MAR-2024, entry version 142. DE RecName: Full=Type I iodothyronine deiodinase; DE EC=1.21.99.4; DE AltName: Full=5DI; DE AltName: Full=DIOI; DE AltName: Full=Type 1 DI; DE AltName: Full=Type-I 5'-deiodinase; GN Name=Dio1; Synonyms=Itdi1, Txdi1; 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 [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=1825132; DOI=10.1038/349438a0; RA Berry M.J., Banu L., Larsen P.R.; RT "Type I iodothyronine deiodinase is a selenocysteine-containing enzyme."; RL Nature 349:438-440(1991). RN [2] 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 [3] RP MUTAGENESIS OF HIS-158; HIS-174 AND HIS-185. RX PubMed=1517238; DOI=10.1016/s0021-9258(19)37151-0; RA Berry M.J.; RT "Identification of essential histidine residues in rat type I iodothyronine RT deiodinase."; RL J. Biol. Chem. 267:18055-18059(1992). CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'- CC tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 CC (3,3'-diiodothyronine). CC -!- CATALYTIC ACTIVITY: CC Reaction=3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L- CC thyroxine; Xref=Rhea:RHEA:19745, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:58448, ChEBI:CHEBI:533015; EC=1.21.99.4; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10107}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, kidney and thyroid CC gland of adult rats. CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57999; CAA41063.1; -; mRNA. DR EMBL; BC083557; AAH83557.1; -; mRNA. DR PIR; S13642; S13642. DR RefSeq; NP_001311139.1; NM_001324210.1. DR RefSeq; NP_067685.5; NM_021653.4. DR STRING; 10116.ENSRNOP00000070330; -. DR PhosphoSitePlus; P24389; -. DR Ensembl; ENSRNOT00000091521.2; ENSRNOP00000070330.2; ENSRNOG00000061237.2. DR Ensembl; ENSRNOT00055051747; ENSRNOP00055042685; ENSRNOG00055029863. DR Ensembl; ENSRNOT00060046314; ENSRNOP00060038481; ENSRNOG00060026719. DR Ensembl; ENSRNOT00065040050; ENSRNOP00065032554; ENSRNOG00065023419. DR GeneID; 25430; -. DR KEGG; rno:25430; -. DR UCSC; RGD:2504; rat. DR AGR; RGD:2504; -. DR CTD; 1733; -. DR RGD; 2504; Dio1. DR GeneTree; ENSGT00940000154482; -. DR InParanoid; P24389; -. DR OMA; PPFMYKL; -. DR OrthoDB; 5405869at2759; -. DR PhylomeDB; P24389; -. DR BioCyc; MetaCyc:MONOMER-14889; -. DR BRENDA; 1.21.99.4; 5301. DR Reactome; R-RNO-350864; Regulation of thyroid hormone activity. DR SABIO-RK; P24389; -. DR PRO; PR:P24389; -. DR Proteomes; UP000002494; Chromosome 5. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008430; F:selenium binding; ISO:RGD. DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IDA:RGD. DR GO; GO:0006520; P:amino acid metabolic process; ISO:RGD. DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:RGD. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR000643; Iodothyronine_deiodinase. DR InterPro; IPR008261; Iodothyronine_deiodinase_AS. DR InterPro; IPR027252; Iodothyronine_deiodinase_I/III. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11781; IODOTHYRONINE DEIODINASE; 1. DR PANTHER; PTHR11781:SF23; TYPE I IODOTHYRONINE DEIODINASE; 1. DR Pfam; PF00837; T4_deiodinase; 1. DR PIRSF; PIRSF001330; IOD; 1. DR PIRSF; PIRSF500144; IODI_III; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS01205; T4_DEIODINASE; 1. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Membrane; Oxidoreductase; Reference proteome; KW Selenocysteine; Thyroid hormones biosynthesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1..257 FT /note="Type I iodothyronine deiodinase" FT /id="PRO_0000154313" FT TRANSMEM 13..33 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 126 FT NON_STD 126 FT /note="Selenocysteine" FT MUTAGEN 158 FT /note="H->F,Q,N: Loss of enzyme activity." FT /evidence="ECO:0000269|PubMed:1517238" FT MUTAGEN 174 FT /note="H->N: 100-fold increase in KM." FT /evidence="ECO:0000269|PubMed:1517238" FT MUTAGEN 174 FT /note="H->Q: 20-fold increase in KM." FT /evidence="ECO:0000269|PubMed:1517238" FT MUTAGEN 185 FT /note="H->N: No effect on enzyme activity." FT /evidence="ECO:0000269|PubMed:1517238" SQ SEQUENCE 257 AA; 29730 MW; 3142ADB974A3E184 CRC64; MGLSQLWLWL KRLVIFLQVA LEVATGKVLM TLFPERVKQN ILAMGQKTGM TRNPRFAPDN WVPTFFSIQY FWFVLKVRWQ RLEDRAEYGG LAPNCTVVRL SGQKCNVWDF IQGSRPLVLN FGSCTUPSFL LKFDQFKRLV DDFASTADFL IIYIEEAHAT DGWAFKNNVD IRQHRSLQDR LRAAHLLLAR SPQCPVVVDT MQNQSSQLYA ALPERLYVIQ EGRICYKGKP GPWNYNPEEV RAVLEKLCIP PGHMPQF //