ACSL3: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Long-chain-fatty-acid—CoA ligase 3''' is an [[enzyme]] that in [[human]]s is encoded by the ''ACSL3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2181| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Acyl-CoA synthetase long-chain family member 3
| HGNCid = 3570
| Symbol = ACSL3
| AltSymbols =; ACS3; FACL3; PRO2194
| OMIM = 602371
| ECnumber = 
| Homologene = 3278
| MGIid = 1921455
| GeneAtlas_image1 = PBB_GE_ACSL3_201661_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACSL3_201660_at_tn.png
| GeneAtlas_image3 = PBB_GE_ACSL3_201662_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004321 |text = fatty-acyl-CoA synthase activity}} {{GNF_GO|id=GO:0004467 |text = long-chain-fatty-acid-CoA ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2181
    | Hs_Ensembl = ENSG00000123983
    | Hs_RefseqProtein = NP_004448
    | Hs_RefseqmRNA = NM_004457
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 223433976
    | Hs_GenLoc_end = 223516360
    | Hs_Uniprot = O95573
    | Mm_EntrezGene = 74205
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_001033606
    | Mm_RefseqProtein = NP_001028778
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Acyl-CoA synthetase long-chain family member 3''', also known as '''ACSL3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2181| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is an [[isozyme]] of the long-chain [[fatty-acid]]-[[coenzyme]] A [[ligase]] family. Although differing in [[substrate specificity]], [[subcellular]] localization, and [[tissue (biology)|tissue]] distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA [[ester]]s, and thereby play a key role in [[lipid]] [[biosynthesis]] and fatty acid degradation. This isozyme is highly expressed in brain, and preferentially utilizes [[myristate]], [[arachidonate]], and [[eicosapentaenoate]] as substrates. The [[amino acid]] sequence of this isozyme is 92% identical to that of [[rat]] [[homolog]]. Two transcript variants encoding the same protein have been found for this gene.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2181| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ACSL3}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Brueton LA, van Herwerden L, Chotai KA, Winter RM | title = The mapping of a gene for craniosynostosis: evidence for linkage of the Saethre-Chotzen syndrome to distal chromosome 7p | journal = Journal of Medical Genetics | volume = 29 | issue = 10 | pages = 681–685 | date = Oct 1992 | pmid = 1433226 | pmc = 1016122 | doi = 10.1136/jmg.29.10.681 }}
| citations =
* {{cite journal | vauthors = Bakken AM, Farstad M, Holmsen H | title = Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet? | journal = The Biochemical Journal | volume = 274 ( Pt 1) | issue = 1 | pages = 145–52 | date = Feb 1991 | pmid = 1848073 | pmc = 1149932 | doi =  }}
*{{cite journal | author=Brueton LA, van Herwerden L, Chotai KA, Winter RM |title=The mapping of a gene for craniosynostosis: evidence for linkage of the Saethre-Chotzen syndrome to distal chromosome 7p. |journal=J. Med. Genet. |volume=29 |issue= 10 |pages= 681-5 |year= 1992 |pmid= 1433226 |doi= }}
* {{cite journal | vauthors = Bronfman M, Inestrosa NC, Nervi FO, Leighton F | title = Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization | journal = The Biochemical Journal | volume = 224 | issue = 3 | pages = 709–20 | date = Dec 1984 | pmid = 6240978 | pmc = 1144505 | doi =  }}
*{{cite journal | author=Bakken AM, Farstad M, Holmsen H |title=Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet? |journal=Biochem. J. |volume=274 ( Pt 1) |issue= |pages= 145-52 |year= 1991 |pmid= 1848073 |doi=  }}
* {{cite journal | vauthors = Rose CS, King AA, Summers D, Palmer R, Yang S, Wilkie AO, Reardon W, Malcolm S, Winter RM | title = Localization of the genetic locus for Saethre-Chotzen syndrome to a 6 cM region of chromosome 7 using four cases with apparently balanced translocations at 7p21.2 | journal = Human Molecular Genetics | volume = 3 | issue = 8 | pages = 1405–1408 | date = Aug 1994 | pmid = 7987323 | doi = 10.1093/hmg/3.8.1405 }}
*{{cite journal | author=Bronfman M, Inestrosa NC, Nervi FO, Leighton F |title=Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization. |journal=Biochem. J. |volume=224 |issue= 3 |pages= 709-20 |year= 1985 |pmid= 6240978 |doi=  }}
* {{cite journal | vauthors = Fujino T, Kang MJ, Suzuki H, Iijima H, Yamamoto T | title = Molecular characterization and expression of rat acyl-CoA synthetase 3 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 28 | pages = 16748–16752 | date = Jul 1996 | pmid = 8663269 | doi = 10.1074/jbc.271.28.16748 }}
*{{cite journal | author=Rose CS, King AA, Summers D, ''et al.'' |title=Localization of the genetic locus for Saethre-Chotzen syndrome to a 6 cM region of chromosome 7 using four cases with apparently balanced translocations at 7p21.2. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1405-8 |year= 1995 |pmid= 7987323 |doi= }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Fujino T, Kang MJ, Suzuki H, ''et al.'' |title=Molecular characterization and expression of rat acyl-CoA synthetase 3. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16748-52 |year= 1996 |pmid= 8663269 |doi= }}
* {{cite journal | vauthors = Minekura H, Fujino T, Kang MJ, Fujita T, Endo Y, Yamamoto TT | title = Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35 | journal = Genomics | volume = 42 | issue = 1 | pages = 180–181 | date = May 1997 | pmid = 9177793 | doi = 10.1006/geno.1997.4710 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT | title = Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene | journal = Gene | volume = 278 | issue = 1-2 | pages = 185–192 | date = Oct 2001 | pmid = 11707336 | doi = 10.1016/S0378-1119(01)00714-4 }}
*{{cite journal | author=Minekura H, Fujino T, Kang MJ, ''et al.'' |title=Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. |journal=Genomics |volume=42 |issue= 1 |pages= 180-1 |year= 1997 |pmid= 9177793 |doi= 10.1006/geno.1997.4710 }}
* {{cite journal | vauthors = Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA | title = Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 26 | pages = 16899–16903 | date = Dec 2002 | pmid = 12477932 | pmc = 139241 | doi = 10.1073/pnas.242603899 }}
*{{cite journal | author=Minekura H, Kang MJ, Inagaki Y, ''et al.'' |title=Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. |journal=Gene |volume=278 |issue= 1-2 |pages= 185-92 |year= 2002 |pmid= 11707336 |doi= }}
* {{cite journal | vauthors = Mashek DG, Bornfeldt KE, Coleman RA, Berger J, Bernlohr DA, Black P, DiRusso CC, Farber SA, Guo W, Hashimoto N, Khodiyar V, Kuypers FA, Maltais LJ, Nebert DW, Renieri A, Schaffer JE, Stahl A, Watkins PA, Vasiliou V, Yamamoto TT | title = Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family | journal = Journal of Lipid Research | volume = 45 | issue = 10 | pages = 1958–1961 | date = Oct 2004 | pmid = 15292367 | doi = 10.1194/jlr.E400002-JLR200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–12135 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{cite journal | vauthors = Qiao S, Tuohimaa P | title = Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in prostate cancer cells | journal = FEBS Letters | volume = 577 | issue = 3 | pages = 451–454 | date = Nov 2004 | pmid = 15556626 | doi = 10.1016/j.febslet.2004.10.044 }}
*{{cite journal  | author=Mashek DG, Bornfeldt KE, Coleman RA, ''et al.'' |title=Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family. |journal=J. Lipid Res. |volume=45 |issue= 10 |pages= 1958-61 |year= 2005 |pmid= 15292367 |doi= 10.1194/jlr.E400002-JLR200 }}
* {{cite journal | vauthors = Rohozinski J, Lamb DJ, Bishop CE | title = UTP14c is a recently acquired retrogene associated with spermatogenesis and fertility in man | journal = Biology of Reproduction | volume = 74 | issue = 4 | pages = 644–651 | date = Apr 2006 | pmid = 16354793 | doi = 10.1095/biolreprod.105.046698 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
* {{cite journal | vauthors = Tu LC, Yan X, Hood L, Lin B | title = Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells | journal = Molecular & Cellular Proteomics | volume = 6 | issue = 4 | pages = 575–588 | date = Apr 2007 | pmid = 17220478 | doi = 10.1074/mcp.M600249-MCP200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Zhou Y, Abidi P, Kim A, Chen W, Huang TT, Kraemer FB, Liu J | title = Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 27 | issue = 10 | pages = 2198–2205 | date = Oct 2007 | pmid = 17761945 | doi = 10.1161/ATVBAHA.107.148429 }}
*{{cite journal  | author=Qiao S, Tuohimaa P |title=Vitamin D3 inhibits fatty acid synthase expression by stimulating the expression of long-chain fatty-acid-CoA ligase 3 in prostate cancer cells. |journal=FEBS Lett. |volume=577 |issue= 3 |pages= 451-4 |year= 2005 |pmid= 15556626 |doi= 10.1016/j.febslet.2004.10.044 }}
*{{cite journal | author=Rohozinski J, Lamb DJ, Bishop CE |title=UTP14c is a recently acquired retrogene associated with spermatogenesis and fertility in man. |journal=Biol. Reprod. |volume=74 |issue= 4 |pages= 644-51 |year= 2006 |pmid= 16354793 |doi= 10.1095/biolreprod.105.046698 }}
*{{cite journal | author=Tu LC, Yan X, Hood L, Lin B |title=Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells. |journal=Mol. Cell Proteomics |volume=6 |issue= 4 |pages= 575-88 |year= 2007 |pmid= 17220478 |doi= 10.1074/mcp.M600249-MCP200 }}
*{{cite journal | author=Zhou Y, Abidi P, Kim A, ''et al.'' |title=Transcriptional activation of hepatic ACSL3 and ACSL5 by oncostatin m reduces hypertriglyceridemia through enhanced beta-oxidation. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=27 |issue= 10 |pages= 2198-205 |year= 2007 |pmid= 17761945 |doi= 10.1161/ATVBAHA.107.148429 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
[[Category:Human proteins]]
{{WikiDoc Sources}}
 
{{gene-2-stub}}

Latest revision as of 17:45, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Long-chain-fatty-acid—CoA ligase 3 is an enzyme that in humans is encoded by the ACSL3 gene.[1]

Function

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3".

External links

Further reading

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