Protein Overview: TRR2

General Information:
Name(s) found:	TRR2 / YHR106W [SGD]
Description(s) found: SHOW ONLY BEST	gi\|731695\|sp\|P38816.1\|TRXB2_YEAST RecName: Full=Thioredoxin reductase 2, mitochondrial; Flags: Precursor [NCBI NR] gi\|6321898\|ref\|NP_011974.1\| Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and [NCBI NR] pir\|\|S48948 thioredoxin-disulfide reductase (EC 1.8.1.9) TRR2 - yeast (Saccharomyces cerevisiae) [NCBI NR] gi\|529123\|gb\|AAB68856.1\| Yhr106wp [Saccharomyces cerevisiae] [NCBI NR] gi\|45269655\|gb\|AAS56208.1\| YHR106W [Saccharomyces cerevisiae] [NCBI NR] Thioredoxin reductase 2, mitochondrial OS=Saccharomyces cerevisiae GN=TRR2 PE=1 SV=1 [Swiss-Prot] (P38816) Thioredoxin reductase 2, mitochondrial precursor (EC 1.8.1.9) [Swiss-Prot] TRR2 Thioredoxin reductase [mips] Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD [SGD] TRR2, Chr VIII from 325600-326628 [yeast_orfs2] Chr VIII from 325600-326628 [yeastorf3.fasta] TRR2 SGDID:S0001148, Chr VIII from 325600-326628, Verified ORF [yeastflysequest.fasta] Trr2p [Saccharomyces cerevisiae]gi\|630122\|pir\|\|S48948 thioredoxin-disulfide reductase (EC 1.8.1.9) TRR2 - yeast (Saccharomyces cerevisiae)gi\|45269655\|gb\|AAS56208.1\| YHR106W [Saccharomyces cerevisiae]gi\|529123\|gb\|AAB68856.1\| Yhr106wp [Saccharomyces cer [nrdb_11152004_Chlamydomonas] TRR2 SGDID:S000001148, Chr VIII from 325601-326629, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p, contains active-site motif (CAVC) present in [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta] TRR2 SGDID:S000001148, Chr VIII from 325601-326629, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in [SGD_S-cerevisiae_na_08-19-2008_con_reversed.fasta] YHR106W [Saccharomyces cerevisiae] [nr-271106-contam.fasta] Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p, contains active-site motif (CAVC) present in prokaryotic thioredoxin reductases, binds NADPH and FAD; Trr2p [Sac [nr-271106-contam.fasta] Yhr106wp [Saccharomyces cerevisiae] [nr-271106-contam.fasta] Thioredoxin reductase 2, mitochondrial precursor [nr-271106-contam.fasta] TRR2 SGDID:S000001148, Chr VIII from 325601-326629, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD" [yeast-bovrabprots.fasta] TRR2 SGDID:S000001148, Chr VIII from 325601-326629, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p, contains active-site motif (CAVC) present in prokaryotic thioredoxin reductases, binds NADPH and FAD" [yeast-contam_custom.fasta] [chemostatdb.fasta] Thioredoxin reductase 2, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TRR2 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta] TRR2 SGDID:S000001148, Chr VIII from 325598-326626, Genome Release 64-1-1, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD" [yeast-030211-contam.fasta] TRR2 SGDID:S000001148, Chr VIII from 325598-326626, Genome Release 64-2-1, Verified ORF, "Mitochondrial thioredoxin reductase; involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD; TRR2 has a paralog, TRR1, that arose from the whole genome duplication" [20141208_orf_trans.fasta] YHR106W SGDID:S000001148, Chr VIII from 325598-326626, Genome Release 64-1-1, Verified ORF, "Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
Organism:	Saccharomyces cerevisiae
Length:	342 amino acids
Gene Ontology:
Cellular Component:	mitochondrion [IDA ]
Biological Process:	response to oxidative stress [IMP]
Molecular Function:	thioredoxin-disulfide reductase activity [IDA]

Sequence:

Sequence:
[PDR BLAST]
[ProtParam]

      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MIKHIVSPFR TNFVGISKSV LSRMIHHKVT IIGSGPAAHT AAIYLARAEM KPTLYEGMMA  60
   61 NGIAAGGQLT TTTDIENFPG FPESLSGSEL MERMRKQSAK FGTNIITETV SKVDLSSKPF 120
  121 RLWTEFNEDA EPVTTDAIIL ATGASAKRMH LPGEETYWQQ GISACAVCDG AVPIFRNKPL 180
  181 AVIGGGDSAC EEAEFLTKYA SKVYILVRKD HFRASVIMQR RIEKNPNIIV LFNTVALEAK 240
  241 GDGKLLNMLR IKNTKSNVEN DLEVNGLFYA IGHSPATDIV KGQVDEEETG YIKTVPGSSL 300
  301 TSVPGFFAAG DVQDSRYRQA VTSAGSGCIA ALDAERYLSA QE

Protein Complex Data

	PUBLICATION	TOPOLOGY	COCOMPLEXED PROTEINS
View Details	Riffle et al. (2010) (Unpublished Data)		TRR1 TRR2
View Details	Krogan NJ, et al. (2006)		TRR1 TRR2

Mass Spectrometry Data

The following runs contain data for this protein:

	BAIT	COMMENTS	PUBLICATION
View Run	MLP2	#12 Mitotic Prep1-TiO2 Flowthrough	Keck JM, et al. (2011)
View Run	MLP2	#11 Mitotic Prep1-TiO2 enriched, new search criteria	Keck JM, et al. (2011)

Yeast Two-Hybrid Data

The following interactions contain this protein:

NOT SHOWING SINGLE HITS. [ Show Single Hits ]

[View our yeast two-hybrid interpretation guidelines.]

	BAIT	PREY	HITS	PUBLICATION
View Screen	MDM30	TRR2	2	Uetz P, et al. (2000)

Microscopy / Localization Data

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	PROTEIN(S)	PUBLICATION
View Data	TRR2	Huh WK, et al. (2003)

Protein Structure Data

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[View Top Sequence Alignments] [Show Ginzu Version Information]

Domains predicted:

#		Region(s)	Method	Confidence	Match Description
1	View Details	[1..146] [273..342]	PSI-BLAST	1130.0	Thioredoxin reductase
2	View Details	[147..272]	PSI-BLAST	1130.0	Thioredoxin reductase

Functions predicted (by domain):

Gene Ontology predictions

Term	Confidence	Notes
thioredoxin-disulfide reductase activity	3.42654162439464	bayes_pls_golite062009
antioxidant activity	3.37477730756688	bayes_pls_golite062009
oxidoreductase activity, acting on sulfur group of donors	3.17769237742078	bayes_pls_golite062009
catalytic activity	1.56773888754354	bayes_pls_golite062009
oxidoreductase activity, acting on sulfur group of donors, NAD or NADP as acceptor	1.45104542724719	bayes_pls_golite062009
binding	1.4227698123368	bayes_pls_golite062009
oxidoreductase activity	0.44090433301056	bayes_pls_golite062009
oxygen-dependent protoporphyrinogen oxidase activity	0.1498172520052	bayes_pls_golite062009
dihydrolipoyl dehydrogenase activity	0.130601418359425	bayes_pls_golite062009
protein binding	0.116927178396589	bayes_pls_golite062009
disulfide oxidoreductase activity	0.0160065137614933	bayes_pls_golite062009

No functions predicted.

Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076

Philius Transmembrane Prediction:

Protein predicted to be:	GLOBULAR (No transmembrane regions or signal peptide)
Confidence of classification:	0.81

Source: Reynolds et al. (2008)

TMHMM	2.0c	PSIPRED	v2.61
SignalP	3.0	COILS	1999
DISOPRED	v0.1	NCBI nr	06/2007
PSI-BLAST	2.2.18	FFAS	ffas03
PDB	06/2007	Pfam	22
HMMER	2.3.2