FUNCTION: Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin (By similarity).
CATALYTIC ACTIVITY: Protein dithiol + NAD(P)⁺ = protein disulfide + NAD(P)H.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the thioredoxin family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

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Cross-references

Sequence databases

EMBL

AE014075; AAN81556.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_754988.1; -.

3D structure databases

HSSP

P23400; 1DBY. [HSSP ENTRY / PDB]

ModBase

P0AGG5.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0015035;	Molecular function: protein disulfide oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0047134;	Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006662;	Biological process: glycerol ether metabolic process (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005746; Thioredoxin.
IPR006662; Thioredoxin-like.
IPR013766; Thioredoxin_dom.
IPR012335; Thioredoxin_fold.
IPR015467; Trx.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR10438; Trx; 1.

Pfam

PF00085; Thioredoxin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00421; THIOREDOXIN.

TIGRFAMs

TIGR01068; thioredoxin; 1.

PROSITE

PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1038821; -.

GenomeReviews

AE014075_GR; c3107.

KEGG

ecc:c3107; -.

Phylogenomic databases

HOGENOM

P0AGG5; -.

Genome annotation databases

CMR

P0AGG5; c3107.

Other

ProtoNet

P0AGG5.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Electron transport; Metal-binding; NAD; Oxidoreductase; Redox-active center; Transport; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 139`	`139`	`Thioredoxin-2.`	`PRO_0000120104`
`DOMAIN`	`26 139`	`114`	`Thioredoxin.`
`ZN_FING`	`5 18`	`14`	`Potential.`
`DISULFID`	`64 67`		`Redox-active (By similarity).`

Sequence information

Length: 139 AA [This is the length of the unprocessed precursor]

Molecular weight: 15555 Da [This is the MW of the unprocessed precursor]

CRC64: 4C973F6FE55C8856 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTVCTHCQA INRIPDDRIE DAAKCGRCGH DLFDGEVINA TGETLDKLLK DDLPVVIDFW 

        70         80         90        100        110        120 
APWCGPCRNF APIFEDVAQE RSGKVRFVKV NTEAERELSS RFGIRSIPTI MIFKNGQVVD 

       130 
MLNGAVPKAP FDSWLNESL

P0AGG5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools