Q9Z0J5 (TRXR2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 2, mitochondrial
EC=1.8.1.9

Alternative name(s):
Thioredoxin reductase TR3

Gene names

Name:	Txnrd2
Synonyms:	Trxr2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

Protein attributes

Sequence length	526 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	Maintains mitochondrial thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. Ref.1
Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. Ref.1
Cofactor	FAD. Ref.1
Subunit structure	Homodimer. Ref.1
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Expressed in liver, kidney, adrenal gland and heart. Ref.1
Miscellaneous	The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity. Ref.1
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Mass spectrometry	Isoform 1: Molecular mass is 53037±2 Da from positions 37 - 526. Determined by ESI. Ref.1

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Selenocysteine
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro response to drug Inferred from expression pattern PubMed 18790005. Source: RGD response to hydrogen peroxide Traceable author statement Ref.1. Source: RGD response to hyperoxia Inferred from expression pattern PubMed 20493230. Source: RGD response to oxygen radical Traceable author statement Ref.1. Source: UniProtKB response to selenium ion Inferred from expression pattern PubMed 15792362. Source: RGD
Cellular_component	axon Inferred from direct assay PubMed 20620191. Source: RGD dendrite Inferred from direct assay PubMed 20620191. Source: RGD mitochondrion Inferred from direct assay Ref.1. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 20620191. Source: RGD
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay Ref.1. Source: UniProtKB thioredoxin-disulfide reductase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9Z0J5-1)

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: Q9Z0J5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGG → MEG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 36	36	Mitochondrion Ref.1
	Chain	37 – 526	490	Thioredoxin reductase 2, mitochondrial Ref.1		PRO_0000030290
Regions
	Nucleotide binding	43 – 72	30	FAD By similarity
Sites
	Active site	499	1	Proton acceptor By similarity
Amino acid modifications
	Non-standard residue	525	1	Selenocysteine
	Disulfide bond	88 ↔ 93		Redox-active By similarity UniProtKB P00390
	Cross-link	524 ↔ 525		Cysteinyl-selenocysteine (Cys-Sec) By similarity
Natural variations
	Alternative sequence	1 – 38	38	MAAIV…SAAGG → MEG in isoform 2.		VSP_008307

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 26, 2008. Version 3. Checksum: ADEEBAD54BE6F241	FASTA	526	56,575
	10 20 30 40 50 60 MAAIVAALRG SSGRFRPQTR VLTRGTRGAA GAASAAGGQQ NFDLLVIGGG SGGLACAKEA 70 80 90 100 110 120 AQLGRKVAVA DYVEPSPRGT KWGLGGTCVN VGCIPKKLMH QAALLGGMIR DAQHYGWEVA 130 140 150 160 170 180 QPVQHNWKAM AEAVQNHVKS LNWGHRVQLQ DRKVKYFNIK ASFVNEHTVH GVDKAGKVTQ 190 200 210 220 230 240 LSAKHIVIAT GGRPKYPTQV KGALEHGITS DDIFWLKESP GKTLVVGASY VALECAGFLT 250 260 270 280 290 300 GIGLDTTVMM RSVPLRGFDQ QMASLVTEHM ESHGTRFLKG CVPSLIRKLP TNQLQVTWED 310 320 330 340 350 360 LASGKEDVGT FDTVLWAIGR VPETRNLNLE KAGVNTNPKN QKIIVDAQEA TSVPHIYAIG 370 380 390 400 410 420 DVAEGRPELT PTAIKAGKLL AQRLFGKSST LMNYSNVPTT VFTPLEYGCV GLSEEEAVAL 430 440 450 460 470 480 HGQEHIEVYH AYYKPLEFTV ADRDASQCYI KMVCMREPPQ LVLGLHFLGP NAGEVTQGFA 490 500 510 520 LGIQCGASYA QVMQTVGIHP TCSEEVVKLH ISKRSGLDPT VTGCUG
	Isoform 2 [UniParc]. Checksum: 2700A49416B63831	FASTA	491	53,239
	10 20 30 40 50 60 MEGQQNFDLL VIGGGSGGLA CAKEAAQLGR KVAVADYVEP SPRGTKWGLG GTCVNVGCIP 70 80 90 100 110 120 KKLMHQAALL GGMIRDAQHY GWEVAQPVQH NWKAMAEAVQ NHVKSLNWGH RVQLQDRKVK 130 140 150 160 170 180 YFNIKASFVN EHTVHGVDKA GKVTQLSAKH IVIATGGRPK YPTQVKGALE HGITSDDIFW 190 200 210 220 230 240 LKESPGKTLV VGASYVALEC AGFLTGIGLD TTVMMRSVPL RGFDQQMASL VTEHMESHGT 250 260 270 280 290 300 RFLKGCVPSL IRKLPTNQLQ VTWEDLASGK EDVGTFDTVL WAIGRVPETR NLNLEKAGVN 310 320 330 340 350 360 TNPKNQKIIV DAQEATSVPH IYAIGDVAEG RPELTPTAIK AGKLLAQRLF GKSSTLMNYS 370 380 390 400 410 420 NVPTTVFTPL EYGCVGLSEE EAVALHGQEH IEVYHAYYKP LEFTVADRDA SQCYIKMVCM 430 440 450 460 470 480 REPPQLVLGL HFLGPNAGEV TQGFALGIQC GASYAQVMQT VGIHPTCSEE VVKLHISKRS 490 GLDPTVTGCU G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver." Lee S.-R., Kim J.-R., Kwon K.-S., Yoon H.W., Levine R.L., Ginsburg A., Rhee S.G. J. Biol. Chem. 274:4722-4734(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 37-55; 206-217; 343-362 AND 515-526, SELENOCYSTEINE AT SEC-525, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"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 1). Tissue: Heart.
[3]	"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: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072865 mRNA. Translation: AAD13801.1. BC085734 mRNA. Translation: AAH85734.1.
IPI	IPI00196118. IPI00476563.
RefSeq	NP_072106.1. NM_022584.2.
UniGene	Rn.6300.
3D structure databases
ProteinModelPortal	Q9Z0J5.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000002593.
Proteomic databases
PaxDb	Q9Z0J5.
PRIDE	Q9Z0J5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	50551.
KEGG	rno:50551.
Organism-specific databases
CTD	10587.
RGD	61960. Txnrd2.
Phylogenomic databases
eggNOG	COG1249.
HOGENOM	HOG000276712.
HOVERGEN	HBG004959.
InParanoid	Q9Z0J5.
KO	K00384.
OMA	VMRTVGI.
OrthoDB	EOG408N7T.
Gene expression databases
ArrayExpress	Q9Z0J5.
Genevestigator	Q9Z0J5.
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
BindingDB	Q9Z0J5.
ChEMBL	CHEMBL5086.
NextBio	610344.

Entry information

Entry name

TRXR2_RAT

Accession

Primary (citable) accession number: Q9Z0J5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	February 26, 2008
Last modified:	April 3, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program