IOD1_RABIT
ID IOD1_RABIT Reviewed; 249 AA.
AC A4GT88;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18466079; DOI=10.1089/thy.2007.0287;
RA Debaveye Y., Ellger B., Mebis L., Darras V.M., Van den Berghe G.;
RT "Regulation of tissue iodothyronine deiodinase activity in a model of
RT prolonged critical illness.";
RL Thyroid 18:551-560(2008).
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; EF428025; ABO21318.1; -; mRNA.
DR RefSeq; NP_001093428.1; NM_001099958.1.
DR STRING; 9986.ENSOCUP00000007619; -.
DR GeneID; 100101570; -.
DR KEGG; ocu:100101570; -.
DR CTD; 1733; -.
DR eggNOG; ENOG502QUGZ; Eukaryota.
DR InParanoid; A4GT88; -.
DR OrthoDB; 977776at2759; -.
DR Proteomes; UP000001811; Unplaced.
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; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Oxidoreductase; Reference proteome;
KW Selenocysteine; Thyroid hormones biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..249
FT /note="Type I iodothyronine deiodinase"
FT /id="PRO_0000318639"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 126
FT NON_STD 126
FT /note="Selenocysteine"
SQ SEQUENCE 249 AA; 28526 MW; 36D30DA30BA72D30 CRC64;
MGLPRPGLWL KRLWVLVQVA VEVAVGKVLM TLFPERVKQN ILAMGQKTGI AQNPNFAQDS
WIPTFFSTQY FWFVLKVRWQ RLEDATEPGG LAPNCSVVRL SGQQCSVWDF MRGNRPLVLN
FGSCTUPSFL SKFDQFKRLI QDFSSIADFL IIYIEEAHAS DGWAFKNNVD IKNHRNLQDR
LRAASLLLAR SPQCPVVVDT MQNQSSQLYA ALPERLYVLR QGRILYKGES GPWNYNPEEV
RAVLEELHS
