ID   IOD2_LITCT              Reviewed;         264 AA.
AC   P49896;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   29-SEP-2021, entry version 91.
DE   RecName: Full=Type II iodothyronine deiodinase;
DE            EC=1.21.99.4;
DE   AltName: Full=5DII;
DE   AltName: Full=DIOII;
DE   AltName: Full=Type 2 DI;
DE   AltName: Full=Type-II 5'-deiodinase;
GN   Name=dio2; Synonyms=itdi2, txdi2;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7592917; DOI=10.1074/jbc.270.45.26786;
RA   Davey J.C., Becker K.B., Schneider M.J., St Germain D.L., Galton V.A.;
RT   "Cloning of a cDNA for the type II iodothyronine deiodinase.";
RL   J. Biol. Chem. 270:26786-26789(1995).
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). Is responsible for the majority of the
CC       intracellular T3 in tissues such as the pituitary, brain and brown fat
CC       by mediating local deiodination of T4, and is important in regulating
CC       thyroid hormone action in these tissues. Plays a major role in
CC       development.
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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: High levels seen in the metamorphosing tail.
CC   -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC       {ECO:0000305}.
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DR   EMBL; L42815; AAC42231.2; -; Genomic_DNA.
DR   PIR; T10530; T10530.
DR   PRIDE; P49896; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004800; F:thyroxine 5'-deiodinase activity; ISS:UniProtKB.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
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   Membrane; Oxidoreductase; Selenocysteine; Thyroid hormones biosynthesis;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..264
FT                   /note="Type II iodothyronine deiodinase"
FT                   /id="PRO_0000154322"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        124
FT   NON_STD         124
FT                   /note="Selenocysteine"
SQ   SEQUENCE   264 AA;  29342 MW;  DEA60ED11FC03F46 CRC64;
     MGLLSVDLLI TLQILPGFFS NCLFLALYDS VVLVKHVLLQ LNRSKSSHGQ WRRMLTPEGL
     RCVWNSFLLD AYKQVKLGGD APNSNVIHVT DKNSSSGKPG TPCHLLDFAS SERPLVVNFG
     SATUPPFISQ LPAFSKMVEE FSAVADFLLV YIDEAHPSDG WAAPGISSYE VKKHRNQEDR
     CAAANKLLEQ YSLPPQCQVV ADCMDNNTNA AYGVSFERVC IVQRQKIVYL GGKGPFFYNL
     QEVRQWLELT FGKKAESGQT GTEK