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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:...

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Detalles Bibliográficos
Autores principales: Sanchez-Pulido, Luis, Rojas, Ana M, Valencia, Alfonso, Martinez-A, Carlos, Andrade, Miguel A
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
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.
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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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