IOD2_BOVIN
ID IOD2_BOVIN Reviewed; 269 AA.
AC Q5I3B2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Mammary epithelium;
RX PubMed=15932406; DOI=10.1111/j.1365-2052.2005.01282.x;
RA Connor E.E., Laiakis E.C., Fernandes V.M., Williams J.L., Capuco A.V.;
RT "Molecular cloning, expression and radiation hybrid mapping of the bovine
RT deiodinase type II (DIO2) and deiodinase type III (DIO3) genes.";
RL Anim. Genet. 36:240-243(2005).
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 -!- 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: Highly expressed in thyroid, mammary and pituitary
CC glands, then in hypothalamus. Low levels detected in diaphragm, heart,
CC kidney and lung. {ECO:0000269|PubMed:15932406}.
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}.
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DR EMBL; AY858551; AAW51123.1; -; mRNA.
DR RefSeq; NP_001010992.1; NM_001010992.5.
DR STRING; 9913.ENSBTAP00000002107; -.
DR PaxDb; Q5I3B2; -.
DR Ensembl; ENSBTAT00000002107; ENSBTAP00000002107; ENSBTAG00000001605.
DR GeneID; 494548; -.
DR KEGG; bta:494548; -.
DR CTD; 1734; -.
DR VEuPathDB; HostDB:ENSBTAG00000001605; -.
DR VGNC; VGNC:106710; DIO2.
DR eggNOG; ENOG502QS2F; Eukaryota.
DR GeneTree; ENSGT00940000154482; -.
DR InParanoid; Q5I3B2; -.
DR OMA; TPPFISH; -.
DR OrthoDB; 977776at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000001605; Expressed in semen and 57 other tissues.
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:0033798; F:thyroxine 5-deiodinase activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0042404; P:thyroid hormone catabolic process; IEA:Ensembl.
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_0000223865"
FT TRANSMEM 10..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT NON_STD 133
FT /note="Selenocysteine"
FT NON_STD 266
FT /note="Selenocysteine"
SQ SEQUENCE 269 AA; 30303 MW; 6644027D04BA74EA CRC64;
MGILSVDLLI TLQILPVFFS NCLFLALYDS VILLKHVVLL LSRSKSTRGQ WRRMLTSEGM
RCIWKSFLLD AYKQVKLGED APNSSVVHVS SPEGGDTSGN GAQEKTVDGT ECHLLDFASP
ERPLVVNFGS ATUPPFTNQL PAFSKLVEEF SSVADFLLVY IDEAHPSDGW AVPGDSSLFF
EVKKHRNQED RCAAAHQLLE RFSLPPQCRV VADRMDNNAN VAYGVAFERV CIVQRQKIAY
LGGKGPFFYN LQEVRRWLEK NFSKRUKLD
