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Reviewed, UniProtKB/Swiss-Prot Q9JMH6 (TRXR1_MOUSE)

Last modified March 2, 2010. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Thioredoxin reductase 1, cytoplasmic
PRO_0000067982

Regions

Nucleotide binding156 – 17318FAD By similarity
Compositional bias26 – 9065Pro-rich

Sites

Active site5861Proton acceptor By similarity

Amino acid modifications

Non-standard residue6121Selenocysteine By similarity
Modified residue1251Phosphotyrosine By similarity
Modified residue2031N6-acetyllysine By similarity
Modified residue2451Phosphotyrosine By similarity
Modified residue3691N6-acetyllysine By similarity
Modified residue5361Phosphotyrosine By similarity
Disulfide bond173 ↔ 178Redox-active By similarity
Cross-link611 ↔ 612Cysteinyl-selenocysteine (Cys-Sec) By similarity

Natural variations

Alternative sequence1 – 114114Missing in isoform 2.
VSP_031566

Experimental info

Sequence conflict2381K → E in BAE28994. Ref.3
Sequence conflict3721Q → R in BAE26918. Ref.3
Sequence conflict6071L → V in BAE26918. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: C9FD2E2E8C55118C

FASTA61367,084
        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

« Hide

Isoform 2.

Checksum: FEBB478D8B22429E
Show »

FASTA49954,544

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References

« Hide '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. expand/collapse author list , 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.

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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.
IPIIPI00469251.
IPI00776252.
RefSeqNP_001035978.1.
NP_001035979.1.
NP_001035988.1.
NP_056577.2.
UniGeneMm.210155
Mm.471159

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JMH6.

PTM databases

PhosphoSiteQ9JMH6.

2-D gel databases

REPRODUCTION-2DPAGEQ9JMH6.

Proteomic databases

PRIDEQ9JMH6.

Genome annotation databases

EnsemblENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250; Mus musculus. [Genome view]
GeneID50493.
KEGGmmu:50493.

Organism-specific databases

CTD50493.
MGIMGI:1354175. Txnrd1.

Phylogenomic databases

eggNOGroNOG05959.
HOGENOMHBG515043.
HOVERGENHBG004959.
InParanoidQ9JMH6.
OMAPTKIEQI.
OrthoDBEOG9DV868.

Enzyme and pathway databases

BRENDA1.8.1.9. 244.

Gene expression databases

ArrayExpressQ9JMH6.
BgeeQ9JMH6.
CleanExMM_TXNRD1.
GenevestigatorQ9JMH6.
GermOnlineENSMUSG00000020250. Mus musculus.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF23. Reduct_Se. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio307476.
SOURCESearch...

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Entry information

Entry nameTRXR1_MOUSE
AccessionPrimary (citable) accession number: Q9JMH6
Secondary accession number(s): Q3UEB7 expand/collapse secondary AC list , Q3UK84, Q8CI31, Q99P49, Q9CSV5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 26, 2008
Last modified: March 2, 2010
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents