IOD1_FUNHE
ID IOD1_FUNHE Reviewed; 248 AA.
AC Q804E1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 23-FEB-2022, entry version 75.
DE RecName: Full=Type I iodothyronine deiodinase;
DE EC=1.21.99.4;
DE AltName: Full=5DI;
DE AltName: Full=DIOI;
DE AltName: Full=Type 1 DI;
DE AltName: Full=Type-I 5'-deiodinase;
GN Name=dio1;
OS Fundulus heteroclitus (Killifish) (Mummichog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX NCBI_TaxID=8078;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=12535629; DOI=10.1016/s0016-6480(02)00570-1;
RA Orozco A., Villalobos P., Jeziorski M.C., Valverde-R C.;
RT "The liver of Fundulus heteroclitus expresses deiodinase type 1 mRNA.";
RL Gen. Comp. Endocrinol. 130:84-91(2003).
CC -!- FUNCTION: Responsible for the deiodination of T4 (3,5,3',5'-
CC tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2
CC (3,3'-diiodothyronine). {ECO:0000269|PubMed:12535629}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:12535629}.
CC -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC {ECO:0000305}.
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DR EMBL; AY184803; AAO31952.1; -; mRNA.
DR RefSeq; NP_001296924.1; NM_001309995.1.
DR STRING; 8078.ENSFHEP00000000892; -.
DR GeneID; 105927890; -.
DR CTD; 1733; -.
DR OrthoDB; 977776at2759; -.
DR Proteomes; UP000265000; Whole Genome Shotgun Assembly.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Oxidoreductase; Selenocysteine;
KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..248
FT /note="Type I iodothyronine deiodinase"
FT /id="PRO_0000318634"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 126
FT NON_STD 126
FT /note="Selenocysteine"
SQ SEQUENCE 248 AA; 27849 MW; 73380E5865921BA3 CRC64;
MFLQKLLVYL TAACMFCYIL VLSATLNVLK VLSPNLARKL ILKMGEKVTM TQNPKFSYED
WGLTYGSLAF IKVASQTMWL SLGQEAFVGE DAPDSPVVTV DGERTSICNY LKGNRPLVLS
FGSCTUPPFM FKLGEFKQLV RDFVDVADFL VVYVAEAHST DGWSFGNNFD IRQHRSLEDR
LSAARILVQN DPLCPVVVDE MSNVSAIKYA AQPERLYVLQ AGKVLYKGAM GPWGYNPQEV
RSVLQKMR
