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IOD1_CANLF
ID   IOD1_CANLF              Reviewed;         244 AA.
AC   P49894;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 124.
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; Synonyms=ITDI1, TXDI1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Mongrel; TISSUE=Liver;
RX   PubMed=8051127; DOI=10.1016/s0021-9258(17)31995-6;
RA   Toyoda N., Harney J.W., Berry M.J., Larsen P.R.;
RT   "Identification of critical amino acids for 3,5,3'-triiodothyronine
RT   deiodination by human type 1 deiodinase based on comparative functional-
RT   structural analyses of the human, dog, and rat enzymes.";
RL   J. Biol. Chem. 269:20329-20334(1994).
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   -!- 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; U11762; AAA53207.2; -; mRNA.
DR   RefSeq; NP_001007127.1; NM_001007126.2.
DR   STRING; 9615.ENSCAFP00000053598; -.
DR   Ensembl; ENSCAFT00030006412; ENSCAFP00030005635; ENSCAFG00030003430.
DR   Ensembl; ENSCAFT00040001545; ENSCAFP00040001312; ENSCAFG00040000858.
DR   Ensembl; ENSCAFT00845027993; ENSCAFP00845022033; ENSCAFG00845015704.
DR   GeneID; 403635; -.
DR   KEGG; cfa:403635; -.
DR   CTD; 1733; -.
DR   VEuPathDB; HostDB:ENSCAFG00845015704; -.
DR   GeneTree; ENSGT00940000154482; -.
DR   InParanoid; P49894; -.
DR   OrthoDB; 977776at2759; -.
DR   Proteomes; UP000002254; Chromosome 5.
DR   Bgee; ENSCAFG00000049055; Expressed in metanephros cortex and 26 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central.
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; Reference proteome;
KW   Selenocysteine; Thyroid hormones biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..244
FT                   /note="Type I iodothyronine deiodinase"
FT                   /id="PRO_0000154310"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        121
FT   NON_STD         121
FT                   /note="Selenocysteine"
SQ   SEQUENCE   244 AA;  28424 MW;  E347D761A60618DC CRC64;
     MGLPRPVLWL RRLWVLLQVA VQVAVGKVFL KLFPARVKQH IVAMNGKNPH FSYDNWAPTL
     YSMQYFWFVL KVQWQRLEDR TEPGGLAPNC PVVRLSGQRC NIWDFMQGNR PLVLNFGSCT
     UPSFLFKFDQ FKRLIEDFCS TADFLIIYIE EAHASDGWAF KNNVNIRTHQ TLQDRLQAAR
     LLLDRAPPCP VVVDTMRNQS SQFYAALPER LFVLQEGRIL YKGKPGPWNY HPEEVRAVLE
     KLHS
 
 
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