Q9JMH6 (TRXR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 1, cytoplasmic
Short name=TR
EC=1.8.1.9

Alternative name(s):
Thioredoxin reductase TR1

Gene names

Name:	Txnrd1
Synonyms:	Trxr1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	613 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Ref.1.
Miscellaneous	The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAH37643.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec. The sequence BAE26918.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec. The sequence BAE40292.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Selenocysteine
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from electronic annotation. Source: Compara benzene-containing compound metabolic process Inferred from electronic annotation. Source: Compara cell proliferation Inferred from mutant phenotype PubMed 15713651. Source: MGI cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to copper ion Inferred from electronic annotation. Source: Compara cellular response to hyperoxia Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from electronic annotation. Source: Compara halogen metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: Compara mesoderm formation Inferred from mutant phenotype PubMed 17697936. Source: MGI methylmercury metabolic process Inferred from electronic annotation. Source: Compara placenta development Inferred from electronic annotation. Source: Compara positive regulation of cell death Inferred from electronic annotation. Source: Compara protein tetramerization Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to selenium ion Inferred from electronic annotation. Source: Compara selenocysteine metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 11259642. Source: MGI mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI neuronal cell body Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.1. Source: MGI
Molecular_function	NAD(P)H oxidase activity Inferred from electronic annotation. Source: Compara NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mercury ion binding Inferred from electronic annotation. Source: Compara selenate reductase activity Inferred from electronic annotation. Source: Compara thioredoxin-disulfide reductase activity Inferred from direct assay PubMed 11259642. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9JMH6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9JMH6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 613	613	Thioredoxin reductase 1, cytoplasmic		PRO_0000067982
Regions
	Nucleotide binding	156 – 173	18	FAD By similarity
	Compositional bias	26 – 90	65	Pro-rich
Sites
	Active site	586	1	Proton acceptor By similarity
Amino acid modifications
	Non-standard residue	612	1	Selenocysteine By similarity
	Modified residue	245	1	Phosphotyrosine By similarity
	Disulfide bond	173 ↔ 178		Redox-active By similarity
	Cross-link	611 ↔ 612		Cysteinyl-selenocysteine (Cys-Sec) By similarity
Natural variations
	Alternative sequence	1 – 114	114	Missing in isoform 2.		VSP_031566
Experimental info
	Sequence conflict	238	1	K → E in BAE28994. Ref.3
	Sequence conflict	372	1	Q → R in BAE26918. Ref.3
	Sequence conflict	607	1	L → V in BAE26918. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: C9FD2E2E8C55118C	FASTA	613	67,084
	10 20 30 40 50 60 MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV LLRGPRGAVL 70 80 90 100 110 120 PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS ELPNKKGQLQ KLPTMNGSKD 130 140 150 160 170 180 PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP 190 200 210 220 230 240 KKLMHQAALL GQALKDSRNY GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV 250 260 270 280 290 300 YENAYGRFIG PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL 310 320 330 340 350 360 PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI GEHMEEHGIK 370 380 390 400 410 420 FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT VLLAVGRDSC TRTIGLETVG 430 440 450 460 470 480 VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EGKLELTPVA IQAGRLLAQR LYGGSNVKCD 490 500 510 520 530 540 YDNVPTTVFT PLEYGCCGLS EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII 550 560 570 580 590 600 CNLKDDERVV GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK 610 RSGGDILQSG CUG
	Isoform 2 [UniParc]. Checksum: FEBB478D8B22429E	FASTA	499	54,544
	10 20 30 40 50 60 MNGSKDPPGS YDFDLIIIGG GSGGLAAAKE AAKFDKKVLV LDFVTPTPLG TRWGLGGTCV 70 80 90 100 110 120 NVGCIPKKLM HQAALLGQAL KDSRNYGWKV EDTVKHDWEK MTESVQSHIG SLNWGYRVAL 130 140 150 160 170 180 REKKVVYENA YGRFIGPHRI VATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS 190 200 210 220 230 240 DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 250 260 270 280 290 300 EEHGIKFIRQ FVPTKIEQIE AGTPGRLRVT AQSTNSEETI EGEFNTVLLA VGRDSCTRTI 310 320 330 340 350 360 GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG 370 380 390 400 410 420 SNVKCDYDNV PTTVFTPLEY GCCGLSEEKA VEKFGEENIE VYHSFFWPLE WTVPSRDNNK 430 440 450 460 470 480 CYAKIICNLK DDERVVGFHV LGPNAGEVTQ GFAAALKCGL TKQQLDSTIG IHPVCAEIFT 490 TLSVTKRSGG DILQSGCUG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of mouse thioredoxin reductases." Kawai H., Ota T., Suzuki F., Tatsuka M. Gene 242:321-330(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION. Tissue: Thymus.
[2]	"Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing." Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N. J. Biol. Chem. 276:3106-3114(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J and DBA/2. Tissue: Embryo.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: FVB/N-3. Tissue: Mammary tumor.
[5]	"Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes." Osborne S.A., Tonissen K.F. BMC Genomics 2:10-10(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB027565 mRNA. Translation: BAA86985.2. AF333036 mRNA. Translation: AAK01140.1. AK011902 mRNA. Translation: BAB27905.1. AK146125 mRNA. Translation: BAE26918.1. Sequence problems. AK149625 mRNA. Translation: BAE28994.1. AK168356 mRNA. Translation: BAE40292.1. Sequence problems. BC037643 mRNA. Translation: AAH37643.1. Sequence problems.
IPI	IPI00469251. IPI00776252.
RefSeq	NP_001035978.1. NM_001042513.1. NP_001035979.1. NM_001042514.1. NP_001035988.1. NM_001042523.1. NP_056577.2. NM_015762.2.
UniGene	Mm.210155.
3D structure databases
ProteinModelPortal	Q9JMH6.
SMR	Q9JMH6. Positions 124-611.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1869051.
PTM databases
PhosphoSite	Q9JMH6.
2D gel databases
REPRODUCTION-2DPAGE	Q9JMH6.
Proteomic databases
PaxDb	Q9JMH6.
PRIDE	Q9JMH6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250.
GeneID	50493.
KEGG	mmu:50493.
UCSC	uc007gjy.1. mouse. uc007gjz.1. mouse.
Organism-specific databases
CTD	7296.
MGI	MGI:1354175. Txnrd1.
Phylogenomic databases
eggNOG	COG1249.
GeneTree	ENSGT00390000007578.
HOGENOM	HOG000276712.
HOVERGEN	HBG004959.
InParanoid	Q9JMH6.
KO	K00384.
OMA	CNIKDNE.
OrthoDB	EOG4H463K.
Enzyme and pathway databases
BRENDA	1.8.1.9. 3474.
Gene expression databases
ArrayExpress	Q9JMH6.
Bgee	Q9JMH6.
CleanEx	MM_TXNRD1.
Genevestigator	Q9JMH6.
GermOnline	ENSMUSG00000020250. Mus musculus.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view]
PANTHER	PTHR22912:SF23. PTHR22912:SF23. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TXNRD1. mouse.
NextBio	307476.
SOURCE	Search...

Entry information

Entry name

TRXR1_MOUSE

Accession

Primary (citable) accession number: Q9JMH6
Secondary accession number(s): Q3UEB7 , Q3UK84, Q8CI31, Q99P49, Q9CSV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	February 26, 2008
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program