ID   IOD1_XENLA              Reviewed;         252 AA.
AC   Q2QEI3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 84.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16601143; DOI=10.1210/en.2005-0711;
RA   Kuiper G.G., Klootwijk W., Morvan Dubois G., Destree O., Darras V.M.,
RA   Van der Geyten S., Demeneix B., Visser T.J.;
RT   "Characterization of recombinant Xenopus laevis type I iodothyronine
RT   deiodinase: substitution of a proline residue in the catalytic center by
RT   serine (Pro132Ser) restores sensitivity to 6-propyl-2-thiouracil.";
RL   Endocrinology 147:3519-3529(2006).
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:0000250}.
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}.
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DR   EMBL; DQ098656; AAZ43088.1; -; mRNA.
DR   RefSeq; NP_001089136.1; NM_001095667.1.
DR   GeneID; 733447; -.
DR   KEGG; xla:733447; -.
DR   AGR; Xenbase:XB-GENE-979948; -.
DR   CTD; 733447; -.
DR   Xenbase; XB-GENE-979948; dio1.L.
DR   OrthoDB; 5405869at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 733447; Expressed in zone of skin and 17 other cell types or tissues.
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; 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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01205; T4_DEIODINASE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Oxidoreductase; Reference proteome;
KW   Selenocysteine; Thyroid hormones biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..252
FT                   /note="Type I iodothyronine deiodinase"
FT                   /id="PRO_0000318637"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        130
FT   NON_STD         130
FT                   /note="Selenocysteine"
SQ   SEQUENCE   252 AA;  29187 MW;  026288D0E636D131 CRC64;
     MESLLQTIKL MLRYIQKALI LFFLFLYVVV GKVLMFLFPQ TMASVLKSRF EISGVHDPKF
     QYEDWGPTFF TYKFLRSVLE IMWMRLEDEA FVGHSAPNTP VVDLSGELHH IWDYLQGTRP
     LVLSFGSCTU PPFLFRLGEF NKLVNEFNSI ADFLIIYIDE AHAADEWALK NNLHIKKHRS
     LQDRLAAAKR LMEESPSCPV VLDTMSNLCS AKYAALPERL YILQEGKIIY KGKMGPWGYK
     PEEVCSVLEK KK
//