Entry - *617792 - THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; TXNDC11 - OMIM
 
* 617792

THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; TXNDC11


Alternative titles; symbols

EF-HAND-BINDING PROTEIN 1; EFP1


HGNC Approved Gene Symbol: TXNDC11

Cytogenetic location: 16p13.13     Genomic coordinates (GRCh38): 16:11,679,083-11,742,857 (from NCBI)


TEXT

Description

Thioredoxins are small proteins characterized by an evolutionarily conserved active cysteine site (CGPC) that undergoes reversible oxidation of the 2 cysteines from the dithiol to the disulfide form. TXNDC11 is a thioredoxin that localizes to endoplasmic reticulum (ER) and may function as a protein chaperone (Wang et al., 2005).


Cloning and Expression

By searching an EST database for sequences similar to canine Efp1, Wang et al. (2005) identified human TXNDC11, which they called EFP1. The deduced 958-amino acid human protein has a calculated molecular mass of 107.5 kD. EFP1 has predicted N- and C-terminal thioredoxin domains that have putative catalytic motifs of WCGQS and WCGFC, respectively. Human EFP1 shares about 74% and 83% amino acid identity with canine and mouse Efp1, respectively. Database analysis revealed a putative human EFP1 isoform with a 27-amino acid insertion between the 2 thioredoxin domains. RT-PCR detected variable expression of a 3-kb EFP1 transcript in all 9 human tissues examined, with highest content in thyroid and prostate. RNA dot blot analysis confirmed ubiquitous EFP1 expression. Epitope-tagged EFP1 localized to ER in transfected CHO cells. Western blot analysis detected EFP1 at an apparent molecular mass of 125 kD.


Gene Function

By yeast 2-hybrid analysis, Wang et al. (2005) found that the first intracellular loop of canine or human DUOX1 (606758) interacted with canine Efp1. Coimmunoprecipitation analysis showed that human EFP1 interacted with DUOX1 and DUOX2 (606759) in cotransfected CHO cells in a calcium-independent manner. In primary cultured human thyrocytes, EFP1 also interacted with TPO (606765). Wang et al. (2005) concluded that EFP1 may function as a protein chaperone in ER.


Gene Structure

Wang et al. (2005) determined that the TXNDC11 gene has 13 exons.


Mapping

By genomic sequence analysis, Wang et al. (2005) mapped the TXNDC11 gene to chromosome 16p13.13.


REFERENCES

  1. Wang, D., De Deken, X., Milenkovic, M., Song, Y., Pirson, I., Dumont, J. E., Miot, F. Identification of a novel partner of Duox: EFP1, a thioredoxin-related protein. J. Biol. Chem. 280: 3096-3103, 2005. [PubMed: 15561711, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 11/29/2017
Edit History:
mgross : 11/29/2017

* 617792

THIOREDOXIN DOMAIN-CONTAINING PROTEIN 11; TXNDC11


Alternative titles; symbols

EF-HAND-BINDING PROTEIN 1; EFP1


HGNC Approved Gene Symbol: TXNDC11

Cytogenetic location: 16p13.13     Genomic coordinates (GRCh38): 16:11,679,083-11,742,857 (from NCBI)


TEXT

Description

Thioredoxins are small proteins characterized by an evolutionarily conserved active cysteine site (CGPC) that undergoes reversible oxidation of the 2 cysteines from the dithiol to the disulfide form. TXNDC11 is a thioredoxin that localizes to endoplasmic reticulum (ER) and may function as a protein chaperone (Wang et al., 2005).


Cloning and Expression

By searching an EST database for sequences similar to canine Efp1, Wang et al. (2005) identified human TXNDC11, which they called EFP1. The deduced 958-amino acid human protein has a calculated molecular mass of 107.5 kD. EFP1 has predicted N- and C-terminal thioredoxin domains that have putative catalytic motifs of WCGQS and WCGFC, respectively. Human EFP1 shares about 74% and 83% amino acid identity with canine and mouse Efp1, respectively. Database analysis revealed a putative human EFP1 isoform with a 27-amino acid insertion between the 2 thioredoxin domains. RT-PCR detected variable expression of a 3-kb EFP1 transcript in all 9 human tissues examined, with highest content in thyroid and prostate. RNA dot blot analysis confirmed ubiquitous EFP1 expression. Epitope-tagged EFP1 localized to ER in transfected CHO cells. Western blot analysis detected EFP1 at an apparent molecular mass of 125 kD.


Gene Function

By yeast 2-hybrid analysis, Wang et al. (2005) found that the first intracellular loop of canine or human DUOX1 (606758) interacted with canine Efp1. Coimmunoprecipitation analysis showed that human EFP1 interacted with DUOX1 and DUOX2 (606759) in cotransfected CHO cells in a calcium-independent manner. In primary cultured human thyrocytes, EFP1 also interacted with TPO (606765). Wang et al. (2005) concluded that EFP1 may function as a protein chaperone in ER.


Gene Structure

Wang et al. (2005) determined that the TXNDC11 gene has 13 exons.


Mapping

By genomic sequence analysis, Wang et al. (2005) mapped the TXNDC11 gene to chromosome 16p13.13.


REFERENCES

  1. Wang, D., De Deken, X., Milenkovic, M., Song, Y., Pirson, I., Dumont, J. E., Miot, F. Identification of a novel partner of Duox: EFP1, a thioredoxin-related protein. J. Biol. Chem. 280: 3096-3103, 2005. [PubMed: 15561711] [Full Text: https://doi.org/10.1074/jbc.M407709200]


Creation Date:
Patricia A. Hartz : 11/29/2017

Edit History:
mgross : 11/29/2017