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ACRATA: a novel electron transfer domain associated to apoptosis and cancer
BACKGROUND: Recently, several members of a vertebrate protein family containing a six trans-membrane (6TM) domain and involved in apoptosis and cancer (e.g. STEAP, STAMP1, TSAP6), have been identified in Golgi and cytoplasmic membranes. The exact function of these proteins remains unknown. METHODS:...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC546010/ https://www.ncbi.nlm.nih.gov/pubmed/15623366 http://dx.doi.org/10.1186/1471-2407-4-98 |
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author | Sanchez-Pulido, Luis Rojas, Ana M Valencia, Alfonso Martinez-A, Carlos Andrade, Miguel A |
author_facet | Sanchez-Pulido, Luis Rojas, Ana M Valencia, Alfonso Martinez-A, Carlos Andrade, Miguel A |
author_sort | Sanchez-Pulido, Luis |
collection | PubMed |
description | BACKGROUND: Recently, several members of a vertebrate protein family containing a six trans-membrane (6TM) domain and involved in apoptosis and cancer (e.g. STEAP, STAMP1, TSAP6), have been identified in Golgi and cytoplasmic membranes. The exact function of these proteins remains unknown. METHODS: We related this 6TM domain to distant protein families using intermediate sequences and methods of iterative profile sequence similarity search. RESULTS: Here we show for the first time that this 6TM domain is homolog to the 6TM heme binding domain of both the NADPH oxidase (Nox) family and the YedZ family of bacterial oxidoreductases. CONCLUSIONS: This finding gives novel insights about the existence of a previously undetected electron transfer system involved in apoptosis and cancer, and suggests further steps in the experimental characterization of these evolutionarily related families. |
format | Text |
id | pubmed-546010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-5460102005-01-29 ACRATA: a novel electron transfer domain associated to apoptosis and cancer Sanchez-Pulido, Luis Rojas, Ana M Valencia, Alfonso Martinez-A, Carlos Andrade, Miguel A BMC Cancer Research Article BACKGROUND: Recently, several members of a vertebrate protein family containing a six trans-membrane (6TM) domain and involved in apoptosis and cancer (e.g. STEAP, STAMP1, TSAP6), have been identified in Golgi and cytoplasmic membranes. The exact function of these proteins remains unknown. METHODS: We related this 6TM domain to distant protein families using intermediate sequences and methods of iterative profile sequence similarity search. RESULTS: Here we show for the first time that this 6TM domain is homolog to the 6TM heme binding domain of both the NADPH oxidase (Nox) family and the YedZ family of bacterial oxidoreductases. CONCLUSIONS: This finding gives novel insights about the existence of a previously undetected electron transfer system involved in apoptosis and cancer, and suggests further steps in the experimental characterization of these evolutionarily related families. BioMed Central 2004-12-29 /pmc/articles/PMC546010/ /pubmed/15623366 http://dx.doi.org/10.1186/1471-2407-4-98 Text en Copyright © 2004 Sanchez-Pulido et al; licensee BioMed Central Ltd. |
spellingShingle | Research Article Sanchez-Pulido, Luis Rojas, Ana M Valencia, Alfonso Martinez-A, Carlos Andrade, Miguel A ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title | ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title_full | ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title_fullStr | ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title_full_unstemmed | ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title_short | ACRATA: a novel electron transfer domain associated to apoptosis and cancer |
title_sort | acrata: a novel electron transfer domain associated to apoptosis and cancer |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC546010/ https://www.ncbi.nlm.nih.gov/pubmed/15623366 http://dx.doi.org/10.1186/1471-2407-4-98 |
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