ID   IOD2_NEOFS              Reviewed;         269 AA.
AC   Q8UVX8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   29-SEP-2021, entry version 71.
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;
OS   Neoceratodus forsteri (Australian lungfish) (Ceratodus forsteri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Ceratodontoidei; Ceratodontidae;
OC   Neoceratodus.
OX   NCBI_TaxID=7892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=12849964; DOI=10.1016/s0016-6480(03)00115-1;
RA   Sutija M., Longhurst T.J., Joss J.M.;
RT   "Deiodinase type II and tissue specific mRNA alternative splicing in the
RT   Australian lungfish, Neoceratodus forsteri.";
RL   Gen. Comp. Endocrinol. 132:409-417(2003).
CC   -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-
CC       tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). {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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC       {ECO:0000305}.
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DR   EMBL; AF327438; AAL56981.2; -; mRNA.
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..269
FT                   /note="Type II iodothyronine deiodinase"
FT                   /id="PRO_0000318643"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        128
FT   NON_STD         128
FT                   /note="Selenocysteine"
FT   NON_STD         261
FT                   /note="Selenocysteine"
SQ   SEQUENCE   269 AA;  30513 MW;  66F17725DF72E62B CRC64;
     MGLLSVDLLI TLQILPWFFS NCLFLALYDS VVLLKHVILL LSCSKSSRGE WRRMLTSEGL
     RTVWNSFLLD AYKQVKLGGD APNSKVVRVT SGCCRRRSFS GKGESECHLL DFASSNRPLV
     VNFGSATUPP FISQLPTFRK LVEEFSDVAD FLLVYIDEAH PADGWAAPGV ATKSFEVKKH
     RSQEERCVAA HKLLEHFSLP PQCQVVADCM DNNTNVAYGV SFERVCIVQR QKIAYLGGKG
     PFFYNLKEVR HWLEQTYRKR UVPTCELIM