ID   IOD2_PIG                Reviewed;         269 AA.
AC   Q6QN12;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   29-SEP-2021, entry version 95.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Landrace X Yorkshire; TISSUE=Pituitary;
RX   PubMed=15192045; DOI=10.1210/en.2004-0356;
RA   Wassen F.W.J.S., Klootwijk W., Kaptein E., Duncker D.J., Visser T.J.,
RA   Kuiper G.G.J.M.;
RT   "Characteristics and thyroid state-dependent regulation of iodothyronine
RT   deiodinases in pigs.";
RL   Endocrinology 145:4251-4263(2004).
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:0000269|PubMed:15192045}.
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   -!- SUBUNIT: Interacts with USP20 and USP33. Interacts with MARCHF6 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: More expressed in pituitary than in brain, low to
CC       undetectable levels in thyroid and skeletal muscle.
CC       {ECO:0000269|PubMed:15192045}.
CC   -!- PTM: Ubiquitinated by MARCHF6, leading to its degradation by the
CC       proteasome. Deubiquitinated by USP20 and USP33 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS48448.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY533207; AAS48448.1; ALT_SEQ; mRNA.
DR   STRING; 9823.ENSSSCP00000025124; -.
DR   PaxDb; Q6QN12; -.
DR   PRIDE; Q6QN12; -.
DR   eggNOG; ENOG502QS2F; Eukaryota.
DR   HOGENOM; CLU_1854524_0_0_1; -.
DR   InParanoid; Q6QN12; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q6QN12; SS.
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; Reference proteome; Selenocysteine;
KW   Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN           1..269
FT                   /note="Type II iodothyronine deiodinase"
FT                   /id="PRO_0000223866"
FT   TRANSMEM        10..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        133
FT   NON_STD         133
FT                   /note="Selenocysteine"
FT   NON_STD         266
FT                   /note="Selenocysteine"
SQ   SEQUENCE   269 AA;  30376 MW;  FF68E3ABABBF06A9 CRC64;
     MGILSVDLLI TLQILPVFFS NCLFLALYDS VILLKHVVLL LSRSKSTRGE WRRMLTSEGM
     RCIWKSFLLD AYKQVKLGED APNSSVVHVS NPEGSNNHGH GTQEKTVDGA ECHLLDFANP
     ERPLVVNFGS ATUPPFTSQL PAFSKLVEEF SSVADFLLVY IDEAHPSDGW AVPGDSSLSF
     EVKKHQNQED RCAAAHQLLE RFSLPPQCRV VADRMDNNAN VAYGVAFERV CIVQRQKIAY
     LGGKGPFYYN LQEVRRWLEK NFSKRUKKT