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Database: UniProt
Entry: A0A0R3P7C5_DROPS
LinkDB: A0A0R3P7C5_DROPS
Original site: A0A0R3P7C5_DROPS 
ID   A0A0R3P7C5_DROPS        Unreviewed;       354 AA.
AC   A0A0R3P7C5; A0A6I8VIW7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Thioredoxin reductase 1, mitochondrial isoform X3 {ECO:0000313|RefSeq:XP_015042311.1};
GN   Name=LOC4814288 {ECO:0000313|RefSeq:XP_015042311.1};
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_015042311.1};
RN   [1] {ECO:0000313|RefSeq:XP_015042311.1}
RP   IDENTIFICATION.
RC   STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_015042311.1};
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_015042311.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR   RefSeq; XP_015042311.1; XM_015186825.2.
DR   AlphaFoldDB; A0A0R3P7C5; -.
DR   SMR; A0A0R3P7C5; -.
DR   EnsemblMetazoa; FBtr0377939; FBpp0338849; FBgn0075294.
DR   GeneID; 4814288; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0075294; Expressed in female reproductive system and 3 other cell types or tissues.
DR   ExpressionAtlas; A0A0R3P7C5; baseline.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001819}.
FT   DOMAIN          6..205
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          225..336
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   354 AA;  38339 MW;  87C3C42A03ECDCF0 CRC64;
     MVAKLKSGDR TITAQTFVIA VGGRPRYPDI PGAVEYGITS DDLFSLDHEP GKTLVVGAGY
     IGLECAGFLK GLGYEPTVMV RSIVLRGFDQ QMAELVASSM DERGIPFLRK TVPLSVTKQD
     NGKLLVKYKN TETGEEGEDT YDTVLWAVGR KGLVEDLNLS NAGVTTFKDK IQVDTKEATN
     VANIFAVGDI IYGKPELTPV AVLAGRLLAR RLYGGSNQRM DYSDVATTVF TPLEYACVGL
     SEEDAVKQHG ADGVEVFHGY YKPTEFFIPQ KSVRYCYLKA VAERTGDQRV YGLHYLGPVA
     GEVIQGFAAA LKSGLTINTL INTVGIHPTT AEEFTRLSIT KRSGLDPTPA SCCS
//
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