Reviewed, UniProtKB/Swiss-Prot Q9JMH6 (TRXR1_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	613 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 Selenium
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cell proliferation Inferred from mutant phenotype. Source: MGI mesoderm formation Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI nucleus Ref.1 Inferred from direct assay. Source: MGI
Molecular function	thioredoxin-disulfide reductase activity Inferred from direct assay. 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
Molecule processing
	Chain	1 – 613	613	Thioredoxin reductase 1, cytoplasmic
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	125	1	Phosphotyrosine By similarity
	Modified residue	245	1	Phosphotyrosine By similarity
	Modified residue	536	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.
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		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: 10721726] [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: 11060283] [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: 16141072] [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: 15489334] [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: 11737861] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_001035978.1. NP_001035979.1. NP_001035988.1. NP_056577.2.
UniGene	Mm.210155 Mm.466268
3D structure databases
HSSP	HSSP built from PDB template 1ONF based on UniProtKB Q94655.
SMR	Q9JMH6. Positions 10-493.
ModBase	Search...
PTM databases
PhosphoSite	Q9JMH6.
2-D gel databases
REPRODUCTION-2DPAGE	Q9JMH6.
Genome annotation databases
Ensembl	ENSMUSG00000020250. Mus musculus. [Contig view]
GeneID	50493.
KEGG	mmu:50493.
Organism-specific databases
MGI	MGI:1354175. Txnrd1.
Phylogenomic databases
HOVERGEN	Q9JMH6.
Gene expression databases
ArrayExpress	Q9JMH6.
CleanEx	MM_TXNRD1.
GermOnline	ENSMUSG00000020250. Mus musculus.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR006338. Reduct_Se. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF23. Reduct_Se. 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. PR00945. HGRDTASE. PR00411. PNDRDTASEI.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01438. TGR. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	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:	July 22, 2008
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)