ID IOD1_CHICK Reviewed; 245 AA. AC O42411; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 27-MAR-2024, entry version 123. 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; DE Flags: Fragment; GN Name=DIO1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=HYBRO; TISSUE=Liver; RX PubMed=9389494; DOI=10.1210/endo.138.12.5599; RA van der Geyten S., Sanders J.P., Kaptein E., Darras V.M., Kuehn E.R., RA Leonard J.L., Visser T.J.; RT "Expression of chicken hepatic type I and type III iodothyronine RT deiodinases during embryonic development."; RL Endocrinology 138:5144-5152(1997). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y11110; CAA71996.1; -; mRNA. DR PIR; JC5825; JC5825. DR RefSeq; NP_001091083.1; NM_001097614.1. DR STRING; 9031.ENSGALP00000017451; -. DR PaxDb; 9031-ENSGALP00000017451; -. DR GeneID; 395940; -. DR KEGG; gga:395940; -. DR CTD; 1733; -. DR VEuPathDB; HostDB:geneid_395940; -. DR eggNOG; ENOG502QUGZ; Eukaryota. DR InParanoid; O42411; -. DR PhylomeDB; O42411; -. DR BRENDA; 1.21.99.4; 1306. DR SABIO-RK; O42411; -. DR PRO; PR:O42411; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IBA:GO_Central. DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central. 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..245 FT /note="Type I iodothyronine deiodinase" FT /id="PRO_0000154315" FT TRANSMEM 10..30 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 123 FT NON_STD 123 FT /note="Selenocysteine" FT NON_TER 1 SQ SEQUENCE 245 AA; 28386 MW; B5ED3C480884C3C1 CRC64; LSIRVLLHKL LILLQVTLSV VVGKTMMILF PDTTKRYILK LGEKSRMNQN PKFSYENWGP TFFSFQYLLF VLKVKWRRLE DEAHEGRPAP NTPVVALNGE MQHLFSFMRD NRPLILNFGS CTUPSFMLKF DEFNKLVKDF SSIADFLIIY IEEAHAVDGW AFRNNVVIKN HRSLEDRKTA AQFLQQKNPL CPVVLDTMEN LSSSKYAALP ERLYILQAGN VIYKGGVGPW NYHPQEIRAV LEKLK //