UniProt Accession

 GLRX5_MOUSE; Q80Y14; Q3YML1; Q9D6E9 

Genbank Protein ID

 DQ083330; AK013761; AK050883; BC050937; BC058371 

Genbank Nucleotide ID

 AAZ30730.1; BAB28985.1; BAC34443.1; AAH50937.1; AAH58371.1 

Protein Name

 Glutaredoxin-related protein 5, mitochondrial 

Protein Synonyms/Alias

 Monothiol glutaredoxin-5 

Gene Name

 Glrx5 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
49	DALVKKDKVVVFLKG	acetylation	[1]
55	DKVVVFLKGTPEQPQ	acetylation	[2, 3]
55	DKVVVFLKGTPEQPQ	succinylation	[3]
147	RSALVDEKDQDSK**	acetylation	[2, 4]

Reference

 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 

Functional Description

 Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. May protect cells against apoptosis due to reactive oxygen species and oxidative stress. 

Sequence Annotation

 DOMAIN 38 141 Glutaredoxin.
 REGION 93 97 Glutathione binding (By similarity).
 REGION 118 119 Glutathione binding (By similarity).
 METAL 63 63 Iron-sulfur (2Fe-2S); shared with dimeric
 BINDING 55 55 Glutathione (By similarity).
 BINDING 105 105 Glutathione; via amide nitrogen and  

Keyword

 2Fe-2S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Mitochondrion; Redox-active center; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 152 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0030097; P:hemopoiesis; ISS:UniProtKB. 

Interpro

 IPR002109; Glutaredoxin.
 IPR004480; Monothiol_GRX-rel.
 IPR012336; Thioredoxin-like_fold. 

Pfam

 PF00462; Glutaredoxin 

SMART

  

PROSITE

 PS51354; GLUTAREDOXIN_2 

PRINTS