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   27-MAR-2024, entry version 112.
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; 9913-ENSBTAP00000002107; -.
DR   Ensembl; ENSBTAT00000002107.8; ENSBTAP00000002107.8; ENSBTAG00000001605.8.
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; KSIWNSF; -.
DR   OrthoDB; 5405869at2759; -.
DR   Reactome; R-BTA-350864; Regulation of thyroid hormone activity.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000001605; Expressed in semen and 57 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000643; Iodothyronine_deiodinase.
DR   InterPro; IPR008261; Iodothyronine_deiodinase_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11781; IODOTHYRONINE DEIODINASE; 1.
DR   PANTHER; PTHR11781:SF20; TYPE II IODOTHYRONINE DEIODINASE; 1.
DR   Pfam; PF00837; T4_deiodinase; 1.
DR   PIRSF; PIRSF001330; IOD; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//