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IOD3_SHEEP
ID   IOD3_SHEEP              Reviewed;         292 AA.
AC   Q6DN07;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 3.
DT   25-MAY-2022, entry version 73.
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;
DE   Flags: Fragment;
GN   Name=DIO3;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-245.
RA   Green J., Elsik C., Kiesler D., Prather R., Smith M., Springer G.,
RA   Taylor J.;
RT   "Development of ovine expressed sequence tags for the study of female
RT   reproduction.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-292.
RA   Smit M.A., Davis E.E., Charlier C., Georges M., Cockett N.E.;
RT   "Extending the boundaries of the ovine callipyge imprinted gene cluster.";
RL   Submitted (JUN-2004) 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). RT3 and T2
CC       are inactive metabolites. May play a role in preventing premature
CC       exposure of developing fetal tissues to adult levels of thyroid
CC       hormones. Can regulate circulating fetal thyroid hormone concentrations
CC       throughout gestation. Essential role for regulation of thyroid hormone
CC       inactivation during embryological development.
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; GT879719; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY656759; AAT74923.1; -; Genomic_DNA.
DR   RefSeq; NP_001116122.1; NM_001122650.1.
DR   STRING; 9940.ENSOARP00000014898; -.
DR   GeneID; 100142657; -.
DR   KEGG; oas:100142657; -.
DR   CTD; 1735; -.
DR   eggNOG; ENOG502S5FA; Eukaryota.
DR   OrthoDB; 977776at2759; -.
DR   Proteomes; UP000002356; 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   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   Cell membrane; Endosome; Membrane; Oxidoreductase; Reference proteome;
KW   Selenocysteine; Signal-anchor; Thyroid hormones biosynthesis;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..292
FT                   /note="Thyroxine 5-deiodinase"
FT                   /id="PRO_0000223869"
FT   TOPO_DOM        <1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..50
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        158
FT   NON_STD         158
FT                   /note="Selenocysteine"
FT   NON_TER         1
SQ   SEQUENCE   292 AA;  32772 MW;  3822901891F788FE CRC64;
     VVGEGRGALG GAATMLRSLL LHSLRLCAQT ASCLVLFPRF LGTAFMLWLL DFLCIRKHLL
     GRRRRGQPEI EVELNSDGEE VPPDDPPVCV SDDNRLCTLA SLRAVWHGQK LDFFKQAHEG
     GPAPNSEVVL PDGFQNQHIL DYARGNRPLV LNFGSCTUPP FMARMSAFQR LVTKYQRDVD
     FLIIYIEEAH PSDGWVTTDS PYSIPQHRSL EDRVSAARVL QQGAPECALV LDTMTNSSSS
     AYGAYFERLY IIQSGTIMYQ GGRGPDGYQV SELRTWLERY DEQLHGPQPR RV
 
 
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