IOD3_SPAAU
ID IOD3_SPAAU Reviewed; 267 AA.
AC A7YD35;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 51.
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 Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Campinho M.A., Power D.M., Sweeney G.E.;
RT "Deiodinase expression during sea bream development.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- 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}.
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DR EMBL; DQ888896; ABK20156.1; -; mRNA.
DR Ensembl; ENSSAUT00010063923; ENSSAUP00010060969; ENSSAUG00010024659.
DR GeneTree; ENSGT00940000154482; -.
DR OMA; FGSCSXP; -.
DR Proteomes; UP000472265; Unplaced.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IEA:InterPro.
DR GO; GO:0033798; 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 PANTHER; PTHR11781; PTHR11781; 1.
DR Pfam; PF00837; T4_deiodinase; 1.
DR PIRSF; PIRSF001330; IOD; 1.
DR PIRSF; PIRSF500144; IODI_III; 1.
DR PROSITE; PS01205; T4_DEIODINASE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; Membrane; Oxidoreductase; Reference proteome;
KW Selenocysteine; Signal-anchor; Thyroid hormones biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="Thyroxine 5-deiodinase"
FT /id="PRO_0000318644"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 131
FT NON_STD 131
FT /note="Selenocysteine"
SQ SEQUENCE 267 AA; 30327 MW; 0007513F30B97CBC CRC64;
MHDSGGVQMA RALKHAALCL MLLPRFLLAA VMLWLLDFLC IRKKVLLKMG ERQDGPDDPP
VCVSDSNKMF TLESLRAVWY GQKLDFLKSA HLGRTAPNTE VMLVQERRQV RILDCMKGKR
PLILNFGSCS UPPFMTRLAA FQRVVSQYAD IADFLVVYIE EAHPSDGWVS SDAPYQIPKH
RCLEDRLRAA QLMLAEVPGS NVVVDNMDNS SNAAYGAYFE RLYIVRDERV VYQGGRGPEG
YRISELRNWL EQYRNGLVNS QTAVLHV
