IOD1_MOUSE
ID IOD1_MOUSE Reviewed; 257 AA.
AC Q61153; Q05CY5; Q5FW63;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 150.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=7476994; DOI=10.1210/mend.9.8.7476994;
RA Maia A.L., Berry M.J., Sabbag R., Harney J.W., Larsen P.R.;
RT "Structural and functional differences in the dio1 gene in mice with
RT inherited type 1 deiodinase deficiency.";
RL Mol. Endocrinol. 9:969-980(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB00228.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; U49861; AAB00228.1; ALT_SEQ; mRNA.
DR EMBL; BC019786; AAH19786.1; -; mRNA.
DR EMBL; BC089608; AAH89608.1; -; mRNA.
DR CCDS; CCDS18436.1; -.
DR RefSeq; NP_031886.3; NM_007860.4.
DR STRING; 10090.ENSMUSP00000081007; -.
DR iPTMnet; Q61153; -.
DR PhosphoSitePlus; Q61153; -.
DR SwissPalm; Q61153; -.
DR MaxQB; Q61153; -.
DR PaxDb; Q61153; -.
DR PRIDE; Q61153; -.
DR ProteomicsDB; 267147; -.
DR DNASU; 13370; -.
DR GeneID; 13370; -.
DR KEGG; mmu:13370; -.
DR UCSC; uc008tzq.1; mouse.
DR CTD; 1733; -.
DR MGI; MGI:94896; Dio1.
DR eggNOG; ENOG502QUGZ; Eukaryota.
DR InParanoid; Q61153; -.
DR OrthoDB; 977776at2759; -.
DR PhylomeDB; Q61153; -.
DR TreeFam; TF329721; -.
DR BioCyc; MetaCyc:MON-16138; -.
DR BRENDA; 1.21.99.4; 3474.
DR Reactome; R-MMU-350864; Regulation of thyroid hormone activity.
DR SABIO-RK; Q61153; -.
DR BioGRID-ORCS; 13370; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dio1; mouse.
DR PRO; PR:Q61153; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61153; protein.
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; IDA:MGI.
DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
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_0000154312"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 126
FT NON_STD 126
FT /note="Selenocysteine"
FT CONFLICT 167
FT /note="N -> K (in Ref. 1; AAB00228)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> V (in Ref. 1; AAB00228)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> M (in Ref. 1; AAB00228 and 2; AAH89608)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="Q -> R (in Ref. 2; AAH19786)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="C -> R (in Ref. 2; AAH19786)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="V -> L (in Ref. 1; AAB00228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29568 MW; DF569BDFF7A4257A CRC64;
MGLPQLWLWL KRLVIFLQVA LEVAVGKVLM TLFPGRVKQS ILAMGQKTGM ARNPRFAPDN
WVPTFFSIQY FWFVLKVRWQ RLEDRAEFGG LAPNCTVVCL SGQKCNIWDF IQGSRPLVLN
FGSCTUPSFL LKFDQFKRLV DDFASTADFL IIYIEEAHAT DGWAFKNNVD IRQHRSLQER
VRAARLLLAR SPQCPVVVDT MQNQSSQLYA ALPERLYVIQ EGRICYKGKA GPWNYNPEEV
RAVLEKLCTP PRHVPQL
