CPLM-005064

Genbank Nucleotide ID

Protein Synonyms/Alias

Thioredoxin I; TR-I; Thioredoxin-2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Position	Peptide	Type	References
42	MIAPMIEKFSEQYPQ	acetylation	[1]
54	YPQADFYKLDVDELG	acetylation	[1]
54	YPQADFYKLDVDELG	ubiquitination	[2, 3]
66	ELGDVAQKNEVSAMP	ubiquitination	[2, 3]
79	MPTLLLFKNGKEVAK	acetylation	[1]
86	KNGKEVAKVVGANPA	acetylation	[1]
86	KNGKEVAKVVGANPA	ubiquitination	[3]
96	GANPAAIKQAIAANA	acetylation	[1]
96	GANPAAIKQAIAANA	ubiquitination	[2, 3]

[1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
[2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
[3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]

Functional Description

Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl- hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER- derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism.

DOMAIN 2 103 Thioredoxin.
ACT_SITE 30 30 Nucleophile.
ACT_SITE 33 33 Nucleophile.
DISULFID 30 33 Redox-active.

3D-structure; Complete proteome; Cytoplasm; Deoxyribonucleotide synthesis; Direct protein sequencing; Disulfide bond; Electron transport; Golgi apparatus; Membrane; Nucleus; Protein transport; Redox-active center; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IDA:SGD.
GO:0000324; C:fungal-type vacuole; IPI:SGD.
GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0015036; F:disulfide oxidoreductase activity; IDA:SGD.
GO:0009055; F:electron carrier activity; IEA:InterPro.
GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO:0045454; P:cell redox homeostasis; TAS:SGD.
GO:0034599; P:cellular response to oxidative stress; ISS:SGD.
GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
GO:0006888; P:ER to Golgi vesicle-mediated transport; IDA:SGD.
GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO:0080058; P:protein deglutathionylation; IDA:SGD.
GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:SGD.
GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
GO:0000011; P:vacuole inheritance; IMP:SGD.

IPR005746; Thioredoxin.
IPR012336; Thioredoxin-like_fold.
IPR017937; Thioredoxin_CS.
IPR013766; Thioredoxin_domain.

PF00085; Thioredoxin

PS00194; THIOREDOXIN_1
PS51352; THIOREDOXIN_2

PR00421; THIOREDOXIN.