IOD3_MOUSE
ID IOD3_MOUSE Reviewed; 304 AA.
AC Q91ZI8; G3UY28; Q3UKD2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Thyroxine 5-deiodinase;
DE EC=1.21.99.3;
DE AltName: Full=5DIII;
DE AltName: Full=DIOIII;
DE AltName: Full=Type 3 DI;
DE AltName: Full=Type III iodothyronine deiodinase;
GN Name=Dio3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9886816; DOI=10.1210/endo.140.1.6423;
RA Hernandez A., Lyon G.J., Schneider M.J., St Germain D.L.;
RT "Isolation and characterization of the mouse gene for the type 3
RT iodothyronine deiodinase.";
RL Endocrinology 140:124-130(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-304.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-
CC tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3
CC (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2
CC are inactive metabolites. May play a role in preventing premature
CC exposure of developing fetal tissues to adult levels of thyroid
CC hormones. Can regulate circulating fetal thyroid hormone concentrations
CC throughout gestation. Essential role for regulation of thyroid hormone
CC inactivation during embryological development.
CC {ECO:0000250|UniProtKB:P49897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,3',5'-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-
CC thyroxine; Xref=Rhea:RHEA:18897, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16382, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57261, ChEBI:CHEBI:58448; EC=1.21.99.3;
CC Evidence={ECO:0000250|UniProtKB:P49897};
CC -!- SUBUNIT: Homodimer. May undergo minor heretodimerization with DIO1 and
CC DIO2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-27 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI06848.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI06849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL23960.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE24483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE26869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF426023; AAL23960.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK140797; BAE24483.1; ALT_INIT; mRNA.
DR EMBL; AK146060; BAE26869.1; ALT_INIT; mRNA.
DR EMBL; AL591207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106847; AAI06848.1; ALT_INIT; mRNA.
DR EMBL; BC106848; AAI06849.1; ALT_INIT; mRNA.
DR CCDS; CCDS26171.2; -.
DR RefSeq; NP_742117.2; NM_172119.2.
DR PDB; 4TR3; X-ray; 1.90 A; A=120-304.
DR PDB; 4TR4; X-ray; 1.93 A; A=120-304.
DR PDBsum; 4TR3; -.
DR PDBsum; 4TR4; -.
DR SMR; Q91ZI8; -.
DR STRING; 10090.ENSMUSP00000133920; -.
DR PhosphoSitePlus; Q91ZI8; -.
DR PaxDb; Q91ZI8; -.
DR PRIDE; Q91ZI8; -.
DR Antibodypedia; 56330; 315 antibodies from 26 providers.
DR DNASU; 107585; -.
DR Ensembl; ENSMUST00000173014; ENSMUSP00000133920; ENSMUSG00000075707.
DR GeneID; 107585; -.
DR KEGG; mmu:107585; -.
DR UCSC; uc007pbi.1; mouse.
DR CTD; 1735; -.
DR MGI; MGI:1306782; Dio3.
DR VEuPathDB; HostDB:ENSMUSG00000075707; -.
DR eggNOG; ENOG502S5FA; Eukaryota.
DR GeneTree; ENSGT00940000154482; -.
DR HOGENOM; CLU_089345_0_0_1; -.
DR InParanoid; Q91ZI8; -.
DR OMA; FGSCSXP; -.
DR OrthoDB; 977776at2759; -.
DR PhylomeDB; Q91ZI8; -.
DR TreeFam; TF329721; -.
DR BRENDA; 1.21.99.3; 3474.
DR Reactome; R-MMU-350864; Regulation of thyroid hormone activity.
DR BioGRID-ORCS; 107585; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q91ZI8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q91ZI8; protein.
DR Bgee; ENSMUSG00000075707; Expressed in placenta and 59 other tissues.
DR ExpressionAtlas; Q91ZI8; baseline and differential.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IMP:MGI.
DR GO; GO:0033798; F:thyroxine 5-deiodinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0070342; P:brown fat cell proliferation; IEA:Ensembl.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0097474; P:retinal cone cell apoptotic process; IMP:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0042404; P:thyroid hormone catabolic process; IDA:MGI.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISO:MGI.
DR InterPro; IPR000643; Iodothyronine_deiodinase.
DR InterPro; IPR008261; Iodothyronine_deiodinase_AS.
DR InterPro; IPR027252; Iodothyronine_deiodinase_I/III.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11781; PTHR11781; 1.
DR Pfam; PF00837; T4_deiodinase; 1.
DR PIRSF; PIRSF001330; IOD; 1.
DR PIRSF; PIRSF500144; IODI_III; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS01205; T4_DEIODINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Endosome; Membrane; Oxidoreductase;
KW Reference proteome; Selenocysteine; Signal-anchor;
KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..304
FT /note="Thyroxine 5-deiodinase"
FT /id="PRO_0000154324"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT NON_STD 170
FT /note="Selenocysteine"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4TR3"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:4TR3"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:4TR3"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4TR3"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:4TR3"
SQ SEQUENCE 304 AA; 34111 MW; 877DD709B4104A15 CRC64;
MPRQAASRLV VGEGEGPPGA SGPAATMLRS LLLHSLRLCA QTASCLVLFP RFLGTAFMLW
LLDFLCIRKH FLRRRHPDHP EPEVELNSEG EEMPPDDPPI CVSDDNRLCT LASLKAVWHG
QKLDFFKQAH EGGPAPNSEV VRPDGFQSQR ILDYAQGTRP LVLNFGSCTU PPFMARMSAF
QRLVTKYQRD VDFLIIYIEE AHPSDGWVTT DSPYVIPQHR SLEDRVSAAR VLQQGAPGCA
LVLDTMANSS SSAYGAYFER LYVIQSGTIM YQGGRGPDGY QVSELRTWLE RYDEQLHGTR
PHRF
