P10639 (THIO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin
Short name=Trx

Alternative name(s):
ATL-derived factor
Short name=ADF

Gene names

Name:	Txn
Synonyms:	Txn1

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	105 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions By similarity. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity By similarity. ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).
Subunit structure	Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner By similarity. Ref.6
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Secreted By similarity. Note: Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus By similarity.
Post-translational modification	In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins By similarity.
Sequence similarities	Belongs to the thioredoxin family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transcription Transcription regulation Transport
Cellular component	Cytoplasm Nucleus Secreted
Domain	Redox-active center
Molecular function	Activator
PTM	Acetylation Disulfide bond S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antibiotic metabolic process Inferred from electronic annotation. Source: Compara cell redox homeostasis Inferred from direct assay PubMed 18555775. Source: MGI cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara cellular response to hyperoxia Inferred from electronic annotation. Source: Compara electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro negative regulation of protein export from nucleus Inferred from direct assay PubMed 18555775. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 18555775. Source: MGI positive regulation of DNA binding Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein import into nucleus, translocation Inferred from sequence or structural similarity. Source: UniProtKB response to activity Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to dexamethasone stimulus Inferred from electronic annotation. Source: Compara response to radiation Inferred from sequence or structural similarity. Source: UniProtKB response to selenium ion Inferred from electronic annotation. Source: Compara response to thyroxine stimulus Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axon Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 18555775. Source: MGI dendrite Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 11213470PubMed 18555775. Source: MGI
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro peptide disulfide oxidoreductase activity Inferred from direct assay PubMed 18555775. Source: MGI protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 105	104	Thioredoxin		PRO_0000120007
Regions
	Domain	2 – 105	104	Thioredoxin
Sites
	Active site	32	1	Nucleophile By similarity
	Active site	35	1	Nucleophile By similarity
	Site	26	1	Deprotonates C-terminal active site Cys By similarity
	Site	33	1	Contributes to redox potential value By similarity
	Site	34	1	Contributes to redox potential value By similarity
Amino acid modifications
	Modified residue	3	1	N6-acetyllysine By similarity
	Modified residue	39	1	N6-acetyllysine By similarity
	Modified residue	62	1	S-nitrosocysteine By similarity
	Modified residue	69	1	S-nitrosocysteine By similarity
	Modified residue	73	1	S-nitrosocysteine By similarity
	Disulfide bond	32 ↔ 35		Redox-active By similarity
	Disulfide bond	73		Interchain; alternate By similarity
Experimental info
	Sequence conflict	100	1	S → C in BAB25256. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P10639 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3A2B925935F952DA	FASTA	105	11,675
	10 20 30 40 50 60 MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS NVVFLEVDVD 70 80 90 100 DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAS ITEYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction." Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J. EMBO J. 8:757-764(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Erratum Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J. EMBO J. 13:2244-2244(1994) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Structure of the mouse thioredoxin-encoding gene and its processed pseudogene." Matsui M., Taniguchi Y., Hirota K., Taketo M., Yodoi J. Gene 152:165-171(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv. Tissue: Liver.
[4]	"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]. Strain: C57BL/6J. Tissue: Pancreas.
[5]	"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]. Strain: C57BL/6J. Tissue: Colon and Thymus.
[6]	"Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function." Junn E., Han S.H., Im J.Y., Yang Y., Cho E.W., Um H.D., Kim D.K., Lee K.W., Han P.L., Rhee S.G., Choi I. J. Immunol. 164:6287-6295(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TXNIP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X77585 mRNA. Translation: CAA54688.1. D21859 Genomic DNA. Translation: BAA04881.1. AK007537 mRNA. Translation: BAB25096.1. AK007790 mRNA. Translation: BAB25256.1. BC010756 mRNA. Translation: AAH10756.1. BC094415 mRNA. Translation: AAH94415.1.
IPI	IPI00226993.
PIR	S04107. JC4068.
RefSeq	NP_035790.1. NM_011660.3.
UniGene	Mm.260618.
3D structure databases
ProteinModelPortal	P10639.
SMR	P10639. Positions 1-103.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10639. 1 interaction.
PTM databases
PhosphoSite	P10639.
2D gel databases
SWISS-2DPAGE	P10639.
UCD-2DPAGE	P10639.
Proteomic databases
PaxDb	P10639.
PRIDE	P10639.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
GeneID	22166.
KEGG	mmu:22166.
Organism-specific databases
CTD	22166.
MGI	MGI:98874. Txn1.
Phylogenomic databases
eggNOG	COG0526.
GeneTree	ENSGT00530000063008.
HOGENOM	HOG000292977.
HOVERGEN	HBG009243.
InParanoid	P10639.
KO	K03671.
OMA	ITTKESW.
OrthoDB	EOG47PX7J.
Enzyme and pathway databases
Reactome	REACT_107772. Immune System.
Gene expression databases
ArrayExpress	P10639.
Bgee	P10639.
CleanEx	MM_TXN1.
Genevestigator	P10639.
GermOnline	ENSMUSG00000028367. Mus musculus.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
PANTHER	PTHR10438. PTHR10438. 1 hit.
Pfam	PF00085. Thioredoxin. 1 hit. [Graphical view]
PIRSF	PIRSF000077. Thioredoxin. 1 hit.
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302106.
SOURCE	Search...

Entry information

Entry name

THIO_MOUSE

Accession

Primary (citable) accession number: P10639
Secondary accession number(s): Q52KC4, Q9D8R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program