IOD1_RAT
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 03-AUG-2022, entry version 134.
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}.
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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 Ensembl; ENSRNOT00000091521; ENSRNOP00000070330; ENSRNOG00000061237.
DR GeneID; 25430; -.
DR KEGG; rno:25430; -.
DR UCSC; RGD:2504; rat.
DR CTD; 1733; -.
DR RGD; 2504; Dio1.
DR GeneTree; ENSGT00940000154482; -.
DR InParanoid; P24389; -.
DR OrthoDB; 977776at2759; -.
DR PhylomeDB; P24389; -.
DR BioCyc; MetaCyc:MON-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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:cellular 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 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; PTHR11781; 1.
DR Pfam; PF00837; T4_deiodinase; 1.
DR PIRSF; PIRSF001330; IOD; 1.
DR PIRSF; PIRSF500144; IODI_III; 1.
DR SUPFAM; SSF52833; SSF52833; 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
