ID I3L752_PIG Unreviewed; 597 AA.
AC I3L752;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
GN Name=TXNRD3 {ECO:0000313|Ensembl:ENSSSCP00000019856.4,
GN ECO:0000313|VGNC:VGNC:94614};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000019856.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000019856.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000019856.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000019856.4}
RP IDENTIFICATION.
RG Ensembl;
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,
CC ECO:0000256|RuleBase:RU003691}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; I3L752; -.
DR PeptideAtlas; I3L752; -.
DR Ensembl; ENSSSCT00000027349.4; ENSSSCP00000019856.4; ENSSSCG00000023929.4.
DR VGNC; VGNC:94614; TXNRD3.
DR eggNOG; KOG1752; Eukaryota.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000159178; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR TreeFam; TF314782; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000023929; Expressed in testis and 45 other cell types or tissues.
DR ExpressionAtlas; I3L752; 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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF7; THIOREDOXIN REDUCTASE 3; 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.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933}.
FT DOMAIN 112..450
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 470..581
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65211 MW; BE7E85AAC36020F1 CRC64;
LGNVRGVSVP SPPGRRARLS APGTSRSSSA AREELRRRLL GLIEGHRVVI FSKSYCPHST
RVGRQGLLGL LVQDCANIFV NKVHMGGCDR TFQAHQSGLL QKLLQDDPAY DYDLIVIGGG
SGGLACAQEA AILGRKVLVL DFVVPSPQGT SWGLGGTCVN VGCIPKKLMH QAALLGQALT
DSRKFGWEYS QQVKHNWGTM TEAVQNHIGS LNWGYRLSLR EKAVAYINSY GEFEVYFAFF
KATNGKGQET CYTAAKFVIA TGERPRYLGI QGDKEYCITS DDLFSLPYCP GTTLVVGASY
VALECAGFLA GLGLDVTVMV RSVLLRGFDQ EMAERVGSYM EQHGVRFLRK FVPVEVQQLE
KGSPGKLKVM AKSTEGPETI EGVYNTVLLA IGRDSCTKKM GLEKIGVKIN EKSGKIPVND
VEQTNVPYVY AVGDVLEGKP ELTPIAVQAG KLLARRLFGG RLEKCDYVNV PTVVFTPLEY
GCCGYSEERA IEVYQKENLE VYHTLFWPLE WTVACRDNNT CYAKIICNKL DNDRVIGFHV
LGPNAGEIIQ GFAAAMKCGL TKQLLDDTIG IHPTCAEVFT TLQITKASGL DVTQKGC
//
