IYD1_PIG
ID IYD1_PIG Reviewed; 289 AA.
AC Q6TA49;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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:0000269|PubMed:15289438};
DE AltName: Full=Iodotyrosine dehalogenase 1 {ECO:0000303|PubMed:15289438};
GN Name=IYD; Synonyms=DEHAL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Thyroid;
RX PubMed=15289438; DOI=10.1096/fj.04-2023fje;
RA Gnidehou S., Caillou B., Talbot M., Ohayon R., Kaniewski J.,
RA Noel-Hudson M.-S., Morand S., Agnangji D., Sezan A., Courtin F., Virion A.,
RA Dupuy C.;
RT "Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved
RT in the recycling of iodide close to the thyroglobulin iodination site.";
RL FASEB J. 18:1574-1576(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 (By similarity). During thyroid hormone biosynthesis,
CC facilitates iodide salvage by catalysing the oxidative NADPH-dependent
CC deiodination of the halogenated by-products of thyroid hormone
CC production, monoiodotyrosine (L-MIT) and diiodotyrosine (L-DIT)
CC (PubMed:15289438). The scavanged iodide can then reenter the hormone-
CC producing pathways (By similarity). Acts more efficiently on 3-iodo-L-
CC tyrosine than 3,5-diiodo-L-tyrosine (By similarity).
CC {ECO:0000250|UniProtKB:Q6PHW0, ECO:0000269|PubMed:15289438}.
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:0000269|PubMed:15289438};
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:0000269|PubMed:15289438};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q6PHW0}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q6PHW0}.
CC -!- TISSUE SPECIFICITY: Detected in thyroid (at protein level).
CC {ECO:0000269|PubMed:15289438}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; AY426609; AAR83926.1; -; mRNA.
DR RefSeq; NP_999581.1; NM_214416.1.
DR AlphaFoldDB; Q6TA49; -.
DR SMR; Q6TA49; -.
DR STRING; 9823.ENSSSCP00000004423; -.
DR PRIDE; Q6TA49; -.
DR GeneID; 403124; -.
DR KEGG; ssc:403124; -.
DR CTD; 389434; -.
DR eggNOG; KOG3936; Eukaryota.
DR InParanoid; Q6TA49; -.
DR OrthoDB; 1524590at2759; -.
DR BRENDA; 1.21.1.1; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0140616; F:iodotyrosine deiodinase activity; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IDA:UniProtKB.
DR GO; GO:0006570; P:tyrosine metabolic process; IDA: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 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Flavoprotein; FMN; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Iodotyrosine deiodinase 1"
FT /id="PRO_0000230280"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 100..104
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 128..129
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 130
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 130
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 161
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 161
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 182
FT /ligand="3,5-diiodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:57506"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 182
FT /ligand="3-iodo-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:59898"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 237..239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
FT BINDING 279
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9DCX8"
SQ SEQUENCE 289 AA; 33462 MW; 8EEB115DEF431A4E CRC64;
MFLLTPVLVA VVCILMVWIF KNADGATKRR EEEPRARAEA RPWVDEDLKD STDVLQVEED
ADEWQESEEE VEHVPFSHTR YPEKEMVRRS QEFYELLNKR RSVRFISNER VPMEVIDNVI
KAAGTAPSGA HTEPWTFVVV KDPDVKHRIR EIMEEEEKIN YLKRMGPRWV TDLKKLRTNW
IKEYWDTAPV LILIFKQVHG FAANGKKKIH YYNEISVSIA CGIFLAALQN AGLVTVTTTP
FNCGPRLRVF LNRPANEKLL MFLPVGYPSK EATVPDLPRK PLDQIMVTV
