Entry - *614357 - ACYL-CoA SYNTHETASE MEDIUM CHAIN FAMILY, MEMBER 1; ACSM1 - OMIM

 
 
* 614357

ACYL-CoA SYNTHETASE MEDIUM CHAIN FAMILY, MEMBER 1; ACSM1


Alternative titles; symbols

MEDIUM CHAIN ACYL-CoA SYNTHETASE 1; MACS1


HGNC Approved Gene Symbol: ACSM1

Cytogenetic location: 16p12.3     Genomic coordinates (GRCh38): 16:20,623,235-20,697,680 (from NCBI)


TEXT

▼ Description

Fatty acids are incorporated into membranes and signaling molecules and have roles in energy storage and metabolism. These essential functions require activation of the fatty acid by acyl-coenzyme A (CoA) synthetases, such as ACSM1, which form an activating thioester linkage between the fatty acid and CoA (Watkins et al., 2007).


▼ Cloning and Expression

Using mouse Macs1 to search databases, followed by 3-prime and 5-prime RACE of a kidney cDNA library, Fujino et al. (2001) cloned human ACSM1, which they called MACS1. The deduced 577-amino acid protein has an N-terminal mitochondrial localization signal. It has a calculated molecular mass of 65.3 kD. Northern blot analysis of mouse tissues detected a major 2.3-kb Macs1 transcript and a minor 4.4-kb transcript in liver and kidney. No expression was detected in heart, brain, lung, spleen, skeletal muscle, and testis. Subcellular fractionation and extraction of mouse kidney homogenates revealed that Macs1 localized to the mitochondrial matrix.

Watkins et al. (2007) reported that human ACSM1 contains 4 of 5 motifs characteristic of acyl-CoA synthetases. Phylogenetic analysis revealed that ACSM1 belongs to a family of medium chain acyl-CoA synthetases.


▼ Gene Function

Fujino et al. (2001) showed that mouse Macs1 expressed in COS-7 cells preferred octanoate among fatty acids with 4 to 16 carbon atoms. Macs1 required ATP and CoA for activity. Radiolabeled carbon in octanoate was found in CO2, indicating that the fatty acid was degraded by oxidation. Fujino et al. (2001) concluded that the major function of MACS1 is to produce acyl-CoA for oxidation in the mitochondrial matrix.


▼ Gene Structure

Fujino et al. (2001) determined that the ACSM1 gene contains 13 exons.


▼ Mapping

By genomic sequence analysis, Fujino et al. (2001) mapped the ACSM1 gene to chromosome 16p13.1. The ACSM1 and ACSM3 (145505) genes are located within 150 kb of one another and are transcribed in opposite directions.

By genomic sequence analysis, Watkins et al. (2007) mapped the ACSM1 gene to the minus strand of chromosome 16p12.2.


▼ REFERENCES

  1. Fujino, T., Takei, Y. A., Sone, H., Ioka, R. X., Kamataki, A., Magoori, K., Takahashi, S., Sakai, J., Yamamoto, T. T. Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J. Biol. Chem. 276: 35961-35966, 2001. [PubMed: 11470804, related citations] [Full Text]

  2. Watkins, P. A., Maiguel, D., Jia, Z., Pevsner, J. Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J. Lipid Res. 48: 2736-2750, 2007. [PubMed: 17762044, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 11/23/2011
Edit History:
mgross : 12/02/2011
mgross : 11/23/2011

* 614357

ACYL-CoA SYNTHETASE MEDIUM CHAIN FAMILY, MEMBER 1; ACSM1


Alternative titles; symbols

MEDIUM CHAIN ACYL-CoA SYNTHETASE 1; MACS1


HGNC Approved Gene Symbol: ACSM1

Cytogenetic location: 16p12.3     Genomic coordinates (GRCh38): 16:20,623,235-20,697,680 (from NCBI)


TEXT

Description

Fatty acids are incorporated into membranes and signaling molecules and have roles in energy storage and metabolism. These essential functions require activation of the fatty acid by acyl-coenzyme A (CoA) synthetases, such as ACSM1, which form an activating thioester linkage between the fatty acid and CoA (Watkins et al., 2007).


Cloning and Expression

Using mouse Macs1 to search databases, followed by 3-prime and 5-prime RACE of a kidney cDNA library, Fujino et al. (2001) cloned human ACSM1, which they called MACS1. The deduced 577-amino acid protein has an N-terminal mitochondrial localization signal. It has a calculated molecular mass of 65.3 kD. Northern blot analysis of mouse tissues detected a major 2.3-kb Macs1 transcript and a minor 4.4-kb transcript in liver and kidney. No expression was detected in heart, brain, lung, spleen, skeletal muscle, and testis. Subcellular fractionation and extraction of mouse kidney homogenates revealed that Macs1 localized to the mitochondrial matrix.

Watkins et al. (2007) reported that human ACSM1 contains 4 of 5 motifs characteristic of acyl-CoA synthetases. Phylogenetic analysis revealed that ACSM1 belongs to a family of medium chain acyl-CoA synthetases.


Gene Function

Fujino et al. (2001) showed that mouse Macs1 expressed in COS-7 cells preferred octanoate among fatty acids with 4 to 16 carbon atoms. Macs1 required ATP and CoA for activity. Radiolabeled carbon in octanoate was found in CO2, indicating that the fatty acid was degraded by oxidation. Fujino et al. (2001) concluded that the major function of MACS1 is to produce acyl-CoA for oxidation in the mitochondrial matrix.


Gene Structure

Fujino et al. (2001) determined that the ACSM1 gene contains 13 exons.


Mapping

By genomic sequence analysis, Fujino et al. (2001) mapped the ACSM1 gene to chromosome 16p13.1. The ACSM1 and ACSM3 (145505) genes are located within 150 kb of one another and are transcribed in opposite directions.

By genomic sequence analysis, Watkins et al. (2007) mapped the ACSM1 gene to the minus strand of chromosome 16p12.2.


REFERENCES

  1. Fujino, T., Takei, Y. A., Sone, H., Ioka, R. X., Kamataki, A., Magoori, K., Takahashi, S., Sakai, J., Yamamoto, T. T. Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J. Biol. Chem. 276: 35961-35966, 2001. [PubMed: 11470804] [Full Text: https://doi.org/10.1074/jbc.M106651200]

  2. Watkins, P. A., Maiguel, D., Jia, Z., Pevsner, J. Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. J. Lipid Res. 48: 2736-2750, 2007. [PubMed: 17762044] [Full Text: https://doi.org/10.1194/jlr.M700378-JLR200]


Creation Date:
Patricia A. Hartz : 11/23/2011

Edit History:
mgross : 12/02/2011
mgross : 11/23/2011



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: April 19, 2024