P08628 (THIO_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin
Short name=Trx

Gene names

Name:

TXN

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [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 › Lagomorpha › Leporidae › Oryctolagus

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.
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.
Subcellular location	Nucleus By similarity. Cytoplasm. 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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro oxidation-reduction process Inferred from sequence or structural similarity. Source: UniProtKB 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 regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW response to radiation Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro 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 Ref.1
	Chain	2 – 105	104	Thioredoxin		PRO_0000120010
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

Sequences

	Sequence		Length	Mass (Da)
	P08628 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 9E239D2AD71FB6B6	FASTA	105	11,761
	10 20 30 40 50 60 MVKQIESKSA FQEVLDSAGD KLVVVDFSAT WCGPCKMIKP FFHALSEKFN NVVFIEVDVD 70 80 90 100 DCKDIAAECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELL

References

[1]

"Amino acid sequence of thioredoxin isolated from rabbit bone marrow determined by tandem mass spectrometry." Johnson R.S., Mathews W.R., Biemann K., Hopper S. J. Biol. Chem. 263:9589-9597(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-105, MASS SPECTROMETRY. Tissue: Bone marrow.

Cross-references

Sequence databases
PIR	A28086.
3D structure databases
ProteinModelPortal	P08628.
SMR	P08628. Positions 1-105.
ModBase	Search...
Protein-protein interaction databases
STRING	9986.ENSOCUP00000003102.
Proteomic databases
PRIDE	P08628.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0526.
HOGENOM	HOG000292977.
HOVERGEN	HBG009243.
OrthoDB	EOG47PX7J.
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...

Entry information

Entry name

THIO_RABIT

Accession

Primary (citable) accession number: P08628

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program