ID   IOD2_FUNHE              Reviewed;         266 AA.
AC   P79747; Q8QFX5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   23-FEB-2022, entry version 102.
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   Fundulus heteroclitus (Killifish) (Mummichog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9002998; DOI=10.1210/endo.138.2.4904;
RA   Valverde C., Croteau W., Lafleur G.J. Jr., Orozco A., St Germain D.L.;
RT   "Cloning and expression of a 5'-iodothyronine deiodinase from the liver of
RT   Fundulus heteroclitus.";
RL   Endocrinology 138:642-648(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SEQUENCE REVISION TO 109.
RX   PubMed=12392690; DOI=10.1016/s0016-6480(02)00071-0;
RA   Orozco A., Jeziorski M.C., Linser P.J., Greenberg R.M., Valverde-R C.;
RT   "Cloning of the gene and complete cDNA encoding a type 2 deiodinase from
RT   Fundulus heteroclitus.";
RL   Gen. Comp. Endocrinol. 128:162-167(2002).
CC   -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-
CC       tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for
CC       providing the brain with appropriate levels of T3 during the critical
CC       period of development. {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; U70869; AAB39651.2; -; mRNA.
DR   EMBL; AY065833; AAC79662.2; -; mRNA.
DR   EMBL; AY065834; AAL62449.1; -; Genomic_DNA.
DR   RefSeq; NP_001296885.1; NM_001309956.1.
DR   STRING; 8078.ENSFHEP00000014289; -.
DR   GeneID; 105917782; -.
DR   CTD; 1734; -.
DR   OrthoDB; 977776at2759; -.
DR   Proteomes; UP000265000; Whole Genome Shotgun Assembly.
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..266
FT                   /note="Type II iodothyronine deiodinase"
FT                   /id="PRO_0000154321"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        134
FT   NON_STD         134
FT                   /note="Selenocysteine"
FT   CONFLICT        109
FT                   /note="T -> A (in Ref. 1; AAB39651)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  29678 MW;  99E44E44888B3A6F CRC64;
     MGSASEDLLV TLQILPGFFS NCLFLALYDS VVLVKRVVAL LSRSRSAGCG EWRRMLTSEG
     LRSIWNSFLL DAHKQVKLGC EAPNSKVVKV PDGPRWSSTV VPCGSRIQTG GECRLLDFES
     SDRPLVVNFG SATUPPFISH LPAFRQLVED FSDVADFLLV YIDEAHPSDG WVAPQMGACS
     FSFRKHQNLE ERIGAARKLI EHFSLPPQCQ LVADCMDNNA NVAYGVANER VCIVHQRKIA
     YLGGKGPFFY SLKDVRQWLE LSYGRR