ID   IOD1_SUNMU              Reviewed;         257 AA.
AC   Q95N00;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 82.
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=TXDI1;
OS   Suncus murinus (Asian house shrew) (Musk shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Crocidurinae; Suncus.
OX   NCBI_TaxID=9378;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12161201; DOI=10.1016/s0016-6480(02)00021-7;
RA   Rogatcheva M., Hayashi Y., Oda S., Seo H., Cua K., Refetoff S.,
RA   Murakami M., Mori M., Murata Y.;
RT   "Type 1 iodothyronine deiodinase in the house musk shrew (Suncus murinus,
RT   Insectivora: Soricidae): cloning and characterization of complementary DNA,
RT   unique tissue distribution and regulation by T3.";
RL   Gen. Comp. Endocrinol. 127:48-58(2002).
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). {ECO:0000269|PubMed:12161201}.
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   -!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:12161201}.
CC   -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC       {ECO:0000305}.
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DR   EMBL; AB055517; BAB62750.1; -; mRNA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Oxidoreductase; Selenocysteine;
KW   Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT   CHAIN           1..257
FT                   /note="Type I iodothyronine deiodinase"
FT                   /id="PRO_0000154314"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        126
FT   NON_STD         126
FT                   /note="Selenocysteine"
SQ   SEQUENCE   257 AA;  29454 MW;  74F0965683F8F384 CRC64;
     MGLPGLGLLL KRFGVLVRVA LKVAVGKVLL TLWPSAIRPH LLAMSEKTGM AKNPRFTYED
     WAPTFFSTQY FWFVLKVNWQ QLEDRTKQGD IAPDSPVVHL SGQRARLWDF MQGNRPLVLN
     FGSCSUPSFL FKFDQFKRLV EDFSSVADFL TVYIEEAHAS DGWAFKNNVD IRRHRDLQER
     LQAARLLLDR NPGCPVVVDT MENRSSQLYA ALPERLYVLQ EGRILYKGGP GPWNYHPEEV
     HAVLEQLCRS SAQSPRL
//