ID Q3UY43_MOUSE Unreviewed; 581 AA. AC Q3UY43; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 126. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE22370.1}; DE Flags: Fragment; GN Name=Txnrd3 {ECO:0000313|MGI:MGI:2386711}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE22370.1}; RN [1] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE22370.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE22370.1}; RC TISSUE=Olfactory brain {ECO:0000313|EMBL:BAE22370.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). 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 EMBL; AK134987; BAE22370.1; -; mRNA. DR RefSeq; NP_001171530.1; NM_001178059.1. DR RefSeq; NP_001171531.1; NM_001178060.1. DR AlphaFoldDB; Q3UY43; -. DR DNASU; 232223; -. DR GeneID; 232223; -. DR UCSC; uc012eou.1; mouse. DR AGR; MGI:2386711; -. DR CTD; 114112; -. DR MGI; MGI:2386711; Txnrd3. DR OrthoDB; 5473641at2759; -. DR BioGRID-ORCS; 232223; 3 hits in 77 CRISPR screens. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR CDD; cd03419; GRX_GRXh_1_2_like; 1. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. 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; IPR002109; Glutaredoxin. DR InterPro; IPR011899; Glutaredoxin_euk/vir. 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 NCBIfam; TIGR02180; GRX_euk; 1. DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1. DR PANTHER; PTHR42737:SF7; THIOREDOXIN REDUCTASE 3; 1. DR Pfam; PF00462; Glutaredoxin; 1. DR Pfam; PF07992; Pyr_redox_2; 2. 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; PS51354; GLUTAREDOXIN_2; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. DR Genevisible; Q3UY43; MM. PE 2: Evidence at transcript level; 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}. FT DOMAIN 122..184 FT /note="Glutaredoxin" FT /evidence="ECO:0000259|Pfam:PF00462" FT DOMAIN 211..337 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 366..434 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 454..565 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" FT REGION 17..108 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAE22370.1" SQ SEQUENCE 581 AA; 63422 MW; A84850989DF02205 CRC64; SCPVRPRPVR SVLKFSAALP ASSPRRPPAS RFLSRPGSAR SDNKALEKPP SPPPPPRAQT SPGLGKVGVL PNRRLGAVRG GLMSSPPGRR ARLASPGTSR PSSEAREELR RRLRDLIEGN RVMIFSKSYC PHSTRVKELF SSLGVVYNIL ELDQVDDGAS VQEVLTEISN QKTVPNIFVN KVHVGGCDRT FQAHQNGLLQ KLLQDDSAHD YDLIIIGGGS GGLSCAKEAA NLGKKVMVLD FVVPSPQGTT WGLGGTCVNV GCIPKKLMHQ AALLGHALQD AKKYGWEYNQ QVKHNWEAMT EAIQSHIGSL NWGYRVTLRE KGVTYVNSFG EFVDLHKIKV QQLEKGLPGK LKVVAKSTEG PETVEGIYNT VLLAIGRDSC TRKIGLEKIG VKINEKNGKI PVNDVEQTNV PHVYAIGDIL DGKPELTPVA IQAGKLLARR LFGVSLEKCD YINIPTTVFT PLEYGCCGLS EEKAIEMYKK ENLEVYHTLF WPLEWTVAGR DNNTCYAKII CNKFDNERVV GFHLLGPNAG EITQGFAAAM KCGLTKQLLD DTIGIHPTCG EVFTTLEITK SSGLDITQKG C //