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UniProtKB/Swiss-Prot entry Q9JMH6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRXR1_MOUSE
Primary accession number Q9JMH6
Secondary accession numbers Q3UEB7 Q3UK84 Q8CI31 Q99P49 Q9CSV5
Integrated into Swiss-Prot on May 2, 2002
Sequence was last modified on February 26, 2008 (Sequence version 3)
Annotations were last modified on    April 29, 2008 (Entry version 68)
Name and origin of the protein
Protein name Thioredoxin reductase 1, cytoplasmic
Synonyms EC 1.8.1.9
TR
Thioredoxin reductase TR1
Gene name
Name: Txnrd1
Synonyms: Trxr1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
TISSUE=Thymus;
DOI=10.1016/S0378-1119(99)00498-9; PubMed=10721726 [NCBI, ExPASy, EBI, Israel, Japan]
Kawai H., Ota T., Suzuki F., Tatsuka M.;
"Molecular cloning of mouse thioredoxin reductases.";
Gene 242:321-330(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1074/jbc.M004750200; PubMed=11060283 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.;
"Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing.";
J. Biol. Chem. 276:3106-3114(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and DBA/2;
TISSUE=Embryo;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N-3;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
PubMed=11737861 [NCBI, ExPASy, EBI, Israel, Japan]
Osborne S.A., Tonissen K.F.;
"Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes.";
BMC Genomics 2:10-10(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB027565; BAA86985.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF333036; AAK01140.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011902; BAB27905.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146125; BAE26918.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149625; BAE28994.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168356; BAE40292.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037643; AAH37643.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001035978.1; -.
NP_001035979.1; -.
NP_001035988.1; -.
NP_056577.2; -.
UniGene Mm.210155
3D structure databases
HSSP Q94655; 1ONF. [HSSP ENTRY / PDB]
SMR Q9JMH6; 10-493.
ModBase Q9JMH6.
PTM databases
PhosphoSite Q9JMH6; -.
2D gel databases
REPRODUCTION-2DPAGE Q9JMH6; -.
Organism-specific databases
MGI MGI:1354175; Txnrd1.
GeneLynx Txnrd1; Mus musculus.
Gene expression databases
ArrayExpress Q9JMH6; -.
CleanEx MM_TXNRD1; -.
GermOnline ENSMUSG00000020250; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from direct assay from MGI).
GO:0008283; Biological process: cell proliferation (inferred from mutant phenotype from MGI).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF23; Reduct_Se; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01438; TGR; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
BLOCKS Q9JMH6.
Genome annotation databases
Ensembl ENSMUSG00000020250; Mus musculus. [Contig view]
GeneID 50493; -.
KEGG mmu:50493; -.
Other
SOURCE Txnrd1; Mus musculus.
ProtoNet Q9JMH6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; Redox-active center; Selenium; Selenocysteine.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   613  613     Thioredoxin reductase 1, cytoplasmic. PRO_0000067982
NP_BIND   156   173  18     FAD (By similarity). 
COMPBIAS   26    90  65     Pro-rich. 
ACT_SITE   586   586        Proton acceptor (By similarity). 
NON_STD   612   612        Selenocysteine (By similarity). 
MOD_RES   125   125        Phosphotyrosine (By similarity). 
MOD_RES   245   245        Phosphotyrosine (By similarity). 
MOD_RES   536   536        Phosphotyrosine (By similarity). 
DISULFID   173   178        Redox-active (By similarity). 
CROSSLNK   611   612        Cysteinyl-selenocysteine (Cys-Sec) (By similarity). 
VAR_SEQ   1   114        Missing (in isoform 2). VSP_031566
CONFLICT   238   238        K -> E (in Ref. 3; BAE28994). 
CONFLICT   372   372        Q -> R (in Ref. 3; BAE26918). 
CONFLICT   607   607        L -> V (in Ref. 3; BAE26918). 
Sequence information
Length: 613 AA [This is the length of the unprocessed precursor] Molecular weight: 67084 Da [This is the MW of the unprocessed precursor] CRC64: C9FD2E2E8C55118C [This is a checksum on the sequence]
        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 

Q9JMH6 in FASTA format

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