IOD1_XENLA
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 03-AUG-2022, entry version 79.
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 PRIDE; Q2QEI3; -.
DR GeneID; 733447; -.
DR KEGG; xla:733447; -.
DR CTD; 733447; -.
DR Xenbase; XB-GENE-979948; dio1.L.
DR OrthoDB; 977776at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 733447; Expressed in zone of skin and 17 other tissues.
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:0004800; F:thyroxine 5'-deiodinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000643; Iodothyronine_deiodinase.
DR InterPro; IPR008261; Iodothyronine_deiodinase_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11781; PTHR11781; 1.
DR Pfam; PF00837; T4_deiodinase; 1.
DR PIRSF; PIRSF001330; IOD; 1.
DR SUPFAM; SSF52833; SSF52833; 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