ID   IOD1_FELCA              Reviewed;         244 AA.
AC   Q6V915;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 82.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=12960017; DOI=10.1210/en.2003-0728;
RA   Kuiper G.G.J.M., Wassen F., Klootwijk W., van Toor H., Kaptein E.,
RA   Visser T.J.;
RT   "Molecular basis for the substrate selectivity of cat type I iodothyronine
RT   deiodinase.";
RL   Endocrinology 144:5411-5421(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). Plays a role in providing a source of plasma T3
CC       by deiodination of T4 in peripheral tissues such as liver and kidney.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the iodothyronine deiodinase family.
CC       {ECO:0000305}.
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DR   EMBL; AY347714; AAQ92943.1; -; mRNA.
DR   RefSeq; NP_001009267.1; NM_001009267.1.
DR   STRING; 9685.ENSFCAP00000021400; -.
DR   PaxDb; 9685-ENSFCAP00000021400; -.
DR   GeneID; 493798; -.
DR   KEGG; fca:493798; -.
DR   eggNOG; ENOG502QUGZ; Eukaryota.
DR   InParanoid; Q6V915; -.
DR   OrthoDB; 5405869at2759; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004800; F:thyroxine 5'-deiodinase activity; IBA:GO_Central.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IODOTHYRONINE DEIODINASE; 1.
DR   PANTHER; PTHR11781:SF23; TYPE I IODOTHYRONINE DEIODINASE; 1.
DR   Pfam; PF00837; T4_deiodinase; 1.
DR   PIRSF; PIRSF001330; IOD; 1.
DR   PIRSF; PIRSF500144; IODI_III; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS01205; T4_DEIODINASE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Oxidoreductase; Reference proteome;
KW   Selenocysteine; Thyroid hormones biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..244
FT                   /note="Type I iodothyronine deiodinase"
FT                   /id="PRO_0000247810"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10107"
FT   NON_STD         121
FT                   /note="Selenocysteine"
SQ   SEQUENCE   244 AA;  28489 MW;  99615C88CF077288 CRC64;
     MGLSQLGLWL RRLWVLFQVA LQVAVGKVFL ILFPSRVKQH IVAMNRKNPH FSYDNWAPTL
     YSVQYFWFVL KVRWQRLEDR TEPGGLAPNC PVVRLSGQRC SIWDFMKGNR PLVLNFGSCT
     UPSFLFKFDQ FKRLIEDFCS IADFLIIYIE EAHASDGWAF KNNVNIRNHR NLQDRLQAAC
     LLLDRSPRCP VVVDTMKNQS SRLYAALPER LYVLQAGRIL YKGKPGPWNY HPEEVRAVLE
     KLHS
//