Thioredoxin domain-containing protein 17

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Reviewed, UniProtKB/Swiss-Prot Q9BRA2 (TXD17_HUMAN)

Last modified June 16, 2009. Version 64. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Thioredoxin domain-containing protein 17
Alternative name(s):
    Thioredoxin-like protein 5
    14 kDa thioredoxin-related protein
    TRP14
    Protein 42-9-9

Gene names

Name:	TXNDC17
Synonyms:	TXNL5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	123 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide. Ref.3 Ref.4
Subunit structure	Interacts with TRXR1 and DYNLL1/DNCL1. Ref.4
Subcellular location	Cytoplasm. Ref.3
Tissue specificity	Ubiquitously expressed in cell lines. Ref.3
Post-translational modification	The oxidized protein is reduced by TRXR1.
Sequence similarities	Belongs to the thioredoxin family. Contains 1 thioredoxin domain.

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Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	tumor necrosis factor-mediated signaling pathway Ref.3 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosol Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	electron carrier activity Ref.6 Inferred from direct assay. Source: UniProtKB peroxidase activity Ref.3 Inferred from direct assay. Source: UniProtKB protein binding Ref.3 Inferred from physical interaction. Source: UniProtKB protein-disulfide reductase activity Ref.3 Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 123

123

Thioredoxin domain-containing protein 17

PRO_0000120022

Regions

Domain

41 – 123

Thioredoxin

Sites

Active site

Nucleophile

Active site

Nucleophile

Site

Contributes to redox potential value

Site

Contributes to redox potential value

Amino acid modifications

Disulfide bond

43 ↔ 46

Redox-active Ref.6

Experimental info

Mutagenesis

C → S: Loss of peroxidase activity. Ref.3

Mutagenesis

C → S: Loss of peroxidase activity. Ref.3

Secondary structure

123

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9BRA2-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 887ADB4704946B86
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FASTA

123

13,941

        10         20         30         40         50         60 
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI 

        70         80         90        100        110        120 
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF 


SED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Schmidt T. Thesis (2001), University of Goettingen, Germany Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical vein endothelial cell.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[3]	"Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function." Jeong W., Yoon H.W., Lee S.-R., Rhee S.G. J. Biol. Chem. 279:3142-3150(2004) [PubMed: 14607844] [Abstract] Cited for: PROTEIN SEQUENCE OF 41-58, FUNCTION, MUTAGENESIS OF CYS-43 AND CYS-46, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]	"Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways." Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G. J. Biol. Chem. 279:3151-3159(2004) [PubMed: 14607843] [Abstract] Cited for: FUNCTION, INTERACTION WITH DYNLL1.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Structural basis of cellular redox regulation by human TRP14." Woo J.R., Kim S.J., Jeong W., Cho Y.H., Lee S.C., Chung Y.J., Rhee S.G., Ryu S.E. J. Biol. Chem. 279:48120-48125(2004) [PubMed: 15355959] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BOND.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AJ344101 mRNA. Translation: CAC51435.1.
BC006405 mRNA. Translation: AAH06405.1.

IPI

IPI00646689.

RefSeq

NP_116120.1.

UniGene

Hs.408236

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WOU	X-ray	1.80	A	1-123	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BRA2. 3 interactions.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00646689.

Proteomic databases

PRIDE

Q9BRA2.

Genome annotation databases

Ensembl

ENSG00000129235. Homo sapiens. [Contig view]

GeneID

84817.

KEGG

hsa:84817.

Organism-specific databases

GeneCards

GC17P006486.

H-InvDB

HIX0013479.

HGNC

HGNC:28218. TXNDC17.

PharmGKB

PA134861426.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BRA2.

HOVERGEN

Q9BRA2.

OMA

Q9BRA2. YFSGSKD.

Gene expression databases

ArrayExpress

Q9BRA2.

Bgee

Q9BRA2.

CleanEx

HS_TXNDC17.

GermOnline

ENSG00000129235. Homo sapiens.

Family and domain databases

InterPro

IPR010357. DUF953_thioredox.
IPR017937. Thioredoxin_CS.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR12452. DUF953_thioredox. 1 hit.

Pfam

PF06110. DUF953. 1 hit.
[Graphical view]

PROSITE

PS00194. THIOREDOXIN_1. False negative.
PS51352. THIOREDOXIN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

75010.

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Entry information

Entry name

TXD17_HUMAN

Accession

Primary (citable) accession number: Q9BRA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families