IYD1_RAT
ID IYD1_RAT Reviewed; 285 AA.
AC Q5BK17;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Iodotyrosine deiodinase 1 {ECO:0000250|UniProtKB:Q6PHW0};
DE Short=IYD-1 {ECO:0000250|UniProtKB:Q6PHW0};
DE EC=1.21.1.1 {ECO:0000250|UniProtKB:Q6PHW0};
DE AltName: Full=Iodotyrosine dehalogenase 1 {ECO:0000250|UniProtKB:Q6PHW0};
GN Name=Iyd; Synonyms=Dehal1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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: Catalyzes the dehalogenation of halotyrosines such as 3-
CC bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-
CC diiodo-L-tyrosine. During thyroid hormone biosynthesis, facilitates
CC iodide salvage by catalysing the oxidative NADPH-dependent deiodination
CC of the halogenated by-products of thyroid hormone production,
CC monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT). The scavanged
CC iodide can then reenter the hormone-producing pathways. Acts more
CC efficiently on 3-iodo-L-tyrosine than 3,5-diiodo-L-tyrosine.
CC {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine +
CC H(+) + 2 NADPH; Xref=Rhea:RHEA:32479, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.21.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide + L-tyrosine + NADP(+) = 3-iodo-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:27453, ChEBI:CHEBI:16382, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:59898;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27455;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-iodo-L-tyrosine + iodide + NADP(+) = 3,5-diiodo-L-tyrosine +
CC H(+) + NADPH; Xref=Rhea:RHEA:27457, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16382, ChEBI:CHEBI:57506, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:59898;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27459;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + L-tyrosine + NADP(+) = 3-chloro-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:70343, ChEBI:CHEBI:17996, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189422;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70345;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + L-tyrosine + NADP(+) = 3-bromo-L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:70347, ChEBI:CHEBI:15858, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:58349, ChEBI:CHEBI:189423;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70349;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q6PHW0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PHW0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q6PHW0}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; BC091241; AAH91241.1; -; mRNA.
DR RefSeq; NP_001020171.1; NM_001025000.1.
DR AlphaFoldDB; Q5BK17; -.
DR SMR; Q5BK17; -.
DR STRING; 10116.ENSRNOP00000021893; -.
DR iPTMnet; Q5BK17; -.
DR PhosphoSitePlus; Q5BK17; -.
DR PaxDb; Q5BK17; -.
DR PRIDE; Q5BK17; -.
DR Ensembl; ENSRNOT00000021895; ENSRNOP00000021893; ENSRNOG00000016286.
DR GeneID; 308129; -.
DR KEGG; rno:308129; -.
DR UCSC; RGD:1309288; rat.
DR CTD; 389434; -.
DR RGD; 1309288; Iyd.
DR eggNOG; KOG3936; Eukaryota.
DR GeneTree; ENSGT00390000004348; -.
DR HOGENOM; CLU_070764_1_0_1; -.
DR InParanoid; Q5BK17; -.
DR OMA; WVDQDLQ; -.
DR OrthoDB; 1524590at2759; -.
DR PhylomeDB; Q5BK17; -.
DR TreeFam; TF313415; -.
DR Reactome; R-RNO-209968; Thyroxine biosynthesis.
DR PRO; PR:Q5BK17; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016286; Expressed in liver and 6 other tissues.
DR Genevisible; Q5BK17; RN.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0140616; F:iodotyrosine deiodinase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..285
FT /note="Iodotyrosine deiodinase 1"
FT /id="PRO_0000230282"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 96..100
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 124..125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 126
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 126
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 153
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 153
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 157
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 157
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 178
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 178
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 233..235
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 275
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
SQ SEQUENCE 285 AA; 32846 MW; E89714F0630E5E4D CRC64;
MFLLTPVLVA VVCILVIWVF KNADRSLEEK KEEARAQPWV DEDLKDNTEH LQVEEDTEEW
QESEESVEHI LFSHTRYPEQ EMRMRSQEFY ELLSKRRSIR FISSEPVPME VIDNVIKAAG
TAPSGAHTEP WTFVVVKDPD MKHKIREIIE EEEEINYMKR MGKRWVTDLK KLRTNWIKEY
LDTAPVLILI FKQVHGFAVN GKKKVHYYNE ISVSIACGIL LAALQNAGLV TVTTTPLNCG
PRLRVLLGRP SHEKLLVLLP VGYPSRGATV PDLKRKTLDQ IMVTV
