Literature summary for 1.21.99.3 extracted from

Luongo, C.; Trivisano, L.; Alfano, F.; Salvatore, D.
Type 3 deiodinase and consumptive hypothyroidism: a common mechanism for a rare disease (2013), Front. Endocrinol. (Lausanne), 4, 115.

Search for more literature for 1.21.99.3

Cloned(Commentary)

Cloned (Comment)	Organism
the enzyme is a selenoenzyme encoded by the DIO3 gene, localized on chromosome 14q32, in humans. The DIO3 genomic structure contains a single exon and, at the 3'-UTR, a specific RNA structure, named SECIS (selenocysteine insertion element), that is crucial for the insertion of the selenocysteine residue and for maximal enzymatic catalytic efficiency. The DIO3 gene is imprinted, with preferential expression of the paternal allele. It belongs to a cluster of imprinted regions, at the DLK1-DIO3 locus	Homo sapiens

Cloned (Comment)

Organism

the enzyme is a selenoenzyme encoded by the DIO3 gene, localized on chromosome 14q32, in humans. The DIO3 genomic structure contains a single exon and, at the 3'-UTR, a specific RNA structure, named SECIS (selenocysteine insertion element), that is crucial for the insertion of the selenocysteine residue and for maximal enzymatic catalytic efficiency. The DIO3 gene is imprinted, with preferential expression of the paternal allele. It belongs to a cluster of imprinted regions, at the DLK1-DIO3 locus

Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	integral membrane protein	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Se2+	the enzyme is a selenoenzyme encoded by the DIO3 gene. The DIO3 genomic structure contains a single exon and, at the 3'-UTR, a specific RNA structure, named SECIS (selenocysteine insertion element), that is crucial for the insertion of the selenocysteine residue and for maximal enzymatic catalytic efficiency. The DIO3 gene is imprinted, with preferential expression of the paternal allele. It belongs to a cluster of imprinted regions, at the DLK1-DIO3 locus	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+	Homo sapiens	-	L-thyroxine + reduced acceptor	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P55073	gene DIO3	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
B-lymphocyte	-	Homo sapiens	-
brain	-	Homo sapiens	-
additional information	the enzyme is prevalently expressed in many fetal tissues, through the adult it is expressed in placenta, brain, and skin, and to a lesser extent in the pregnant uterus and pancreatic B-cells. The enzyme activity increases rapidly during the proliferative phase of hemangioma	Homo sapiens	-
placenta	-	Homo sapiens	-
skin	-	Homo sapiens	-
uterus	pregnant	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+	-	Homo sapiens	L-thyroxine + reduced acceptor	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
type 3 deiodinase	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	type 3 deiodinase is the cause of consumptive hypothyroidism, a clinical entity which often requires close cooperation between clinical endocrinologists, pediatricians, and oncologists, pathology, detailed overview	Homo sapiens
physiological function	the enzyme is active in local deiodination processes, it degrades T4 and T3 into inactive metabolites and is thus the major physiological thyroid hormone inactivator, overview. The enzyme plays a relevant role in pregnancy, the enzyme activity in the maternal-fetal unit locally converts most of the T4 derived from the mother into rT3. The enzyme is involved in consumptive hypothyroidism, overview. Pregnancy can be considered a physiological form of compensated consumptive hypothyroidism, in which the physiologically increased expression of the enzyme increases the inactivation rate of maternal T4 thereby enhancing the need for thyroid hormone	Homo sapiens