ACSL5: Difference between revisions

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{{Infobox_gene}}
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'''Long-chain-fatty-acid—CoA ligase 5''' is an [[enzyme]] that in [[human]]s is encoded by the ''ACSL5'' [[gene]].<ref name="pmid11127823">{{cite journal | vauthors = Yamashita Y, Kumabe T, Cho YY, Watanabe M, Kawagishi J, Yoshimoto T, Fujino T, Kang MJ, Yamamoto TT | title = Fatty acid induced glioma cell growth is mediated by the acyl-CoA synthetase 5 gene located on chromosome 10q25.1-q25.2, a region frequently deleted in malignant gliomas | journal = Oncogene | volume = 19 | issue = 51 | pages = 5919–25 |date=Dec 2000 | pmid = 11127823 | pmc =  | doi =10.1038/sj.onc.1203981 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACSL5 acyl-CoA synthetase long-chain family member 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51703| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Acyl-CoA synthetase long-chain family member 5
| HGNCid = 16526
| Symbol = ACSL5
| AltSymbols =; ACS2; ACS5; FACL5
| OMIM = 605677
| ECnumber = 
| Homologene = 69208
| MGIid = 1919129
| GeneAtlas_image1 = PBB_GE_ACSL5_218322_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{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:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{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 = 51703
    | Hs_Ensembl = ENSG00000197142
    | Hs_RefseqProtein = NP_057318
    | Hs_RefseqmRNA = NM_016234
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 114123766
    | Hs_GenLoc_end = 114178128
    | Hs_Uniprot = Q9ULC5
    | Mm_EntrezGene = 433256
    | Mm_Ensembl = ENSMUSG00000024981
    | Mm_RefseqmRNA = NM_027976
    | Mm_RefseqProtein = NP_082252
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 55306619
    | Mm_GenLoc_end = 55350970
    | Mm_Uniprot = Q3UC67
  }}
}}
'''Acyl-CoA synthetase long-chain family member 5''', also known as '''ACSL5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACSL5 acyl-CoA synthetase long-chain family member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51703| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 uterus and spleen, and in trace amounts in normal brain, but has markedly increased levels in malignant gliomas. This gene functions in mediating fatty acid-induced glioma cell growth. Three transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ACSL5 acyl-CoA synthetase long-chain family member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51703| accessdate = }}</ref>
| 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 (biology)|tissue]] distribution, all isozymes of this family convert free long-chain fatty acids into fatty [[acyl]]-[[Coenzyme A|CoA]] [[ester]]s, and thereby play a key role in [[lipid]] [[biosynthesis]] and fatty acid degradation. This isozyme is highly expressed in [[uterus]] and [[spleen]], and in trace amounts in normal [[brain]], but has markedly increased levels in [[malignant]] [[gliomas]]. This gene functions in mediating fatty acid-induced glioma [[cell growth]]. Three transcript variants encoding two different [[isoform]]s have been found for this gene.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ACSL5}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Yamashita Y, Kumabe T, Cho YY, ''et al.'' |title=Fatty acid induced glioma cell growth is mediated by the acyl-CoA synthetase 5 gene located on chromosome 10q25.1-q25.2, a region frequently deleted in malignant gliomas. |journal=Oncogene |volume=19 |issue= 51 |pages= 5919-25 |year= 2000 |pmid= 11127823 |doi= }}
*{{cite journal  | vauthors=Lewin TM, Kim JH, Granger DA |title=Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24674–9 |year= 2001 |pmid= 11319232 |doi= 10.1074/jbc.M102036200 |display-authors=etal}}
*{{cite journal  | author=Lewin TM, Kim JH, Granger DA, ''et al.'' |title=Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently. |journal=J. Biol. Chem. |volume=276 |issue= 27 |pages= 24674-9 |year= 2001 |pmid= 11319232 |doi= 10.1074/jbc.M102036200 }}
*{{cite journal  | vauthors=Minekura H, Kang MJ, Inagaki Y |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=10.1016/S0378-1119(01)00714-4  |display-authors=etal}}
*{{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=Lewin TM, Van Horn CG, Krisans SK, Coleman RA |title=Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and mitochondrial-associated membrane |journal=Arch. Biochem. Biophys. |volume=404 |issue= 2 |pages= 263–70 |year= 2002 |pmid= 12147264 |doi=10.1016/S0003-9861(02)00247-3 }}
*{{cite journal  | author=Lewin TM, Van Horn CG, Krisans SK, Coleman RA |title=Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and mitochondrial-associated membrane. |journal=Arch. Biochem. Biophys. |volume=404 |issue= 2 |pages= 263-70 |year= 2002 |pmid= 12147264 |doi= }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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  | pmc=139241 |display-authors=etal}}
*{{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=Clark HF, Gurney AL, Abaya E |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003  | pmc=403697 |display-authors=etal}}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | vauthors=Gassler N, Schneider A, Kopitz J |title=Impaired expression of acyl-CoA-synthetase 5 in epithelial tumors of the small intestine |journal=Hum. Pathol. |volume=34 |issue= 10 |pages= 1048–52 |year= 2003 |pmid= 14608540 |doi=10.1053/S0046-8177(03)00431-3  |display-authors=etal}}
*{{cite journal  | author=Gassler N, Schneider A, Kopitz J, ''et al.'' |title=Impaired expression of acyl-CoA-synthetase 5 in epithelial tumors of the small intestine. |journal=Hum. Pathol. |volume=34 |issue= 10 |pages= 1048-52 |year= 2003 |pmid= 14608540 |doi= }}
*{{cite journal  | vauthors=Deloukas P, Earthrowl ME, Grafham DV |title=The DNA sequence and comparative analysis of human chromosome 10 |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 |display-authors=etal}}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal  | vauthors=Mashek DG, Bornfeldt KE, Coleman RA |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 |display-authors=etal}}
*{{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=Gerhard DS, Wagner L, Feingold EA |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  | pmc=528928 |display-authors=etal}}
*{{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=Gassler N, Obermüller N, Keith M |title=Characterization of metaplastic and heterotopic epithelia in the human gastrointestinal tract by the expression pattern of acyl-CoA synthetase 5 |journal=Histol. Histopathol. |volume=20 |issue= 2 |pages= 409–14 |year= 2005 |pmid= 15736044 |doi= |display-authors=etal}}
*{{cite journal  | author=Gassler N, Obermüller N, Keith M, ''et al.'' |title=Characterization of metaplastic and heterotopic epithelia in the human gastrointestinal tract by the expression pattern of acyl-CoA synthetase 5. |journal=Histol. Histopathol. |volume=20 |issue= 2 |pages= 409-14 |year= 2005 |pmid= 15736044 |doi= }}
*{{cite journal  | vauthors=Obermüller N, Keith M, Kopitz J |title=Coeliac disease is associated with impaired expression of acyl-CoA-synthetase 5 |journal=International journal of colorectal disease |volume=21 |issue= 2 |pages= 130–4 |year= 2006 |pmid= 15809837 |doi= 10.1007/s00384-004-0738-6 |display-authors=etal}}
*{{cite journal  | author=Obermüller N, Keith M, Kopitz J, ''et al.'' |title=Coeliac disease is associated with impaired expression of acyl-CoA-synthetase 5. |journal=International journal of colorectal disease |volume=21 |issue= 2 |pages= 130-4 |year= 2006 |pmid= 15809837 |doi= 10.1007/s00384-004-0738-6 }}
*{{cite journal  | vauthors=Achouri Y, Hegarty BD, Allanic D |title=Long chain fatty acyl-CoA synthetase 5 expression is induced by insulin and glucose: involvement of sterol regulatory element-binding protein-1c |journal=Biochimie |volume=87 |issue= 12 |pages= 1149–55 |year= 2006 |pmid= 16198472 |doi= 10.1016/j.biochi.2005.04.015 |display-authors=etal}}
*{{cite journal  | author=Achouri Y, Hegarty BD, Allanic D, ''et al.'' |title=Long chain fatty acyl-CoA synthetase 5 expression is induced by insulin and glucose: involvement of sterol regulatory element-binding protein-1c. |journal=Biochimie |volume=87 |issue= 12 |pages= 1149-55 |year= 2006 |pmid= 16198472 |doi= 10.1016/j.biochi.2005.04.015 }}
*{{cite journal  | vauthors=Adamo KB, Dent R, Langefeld CD |title=Peroxisome proliferator-activated receptor gamma 2 and acyl-CoA synthetase 5 polymorphisms influence diet response |journal=Obesity (Silver Spring, Md.) |volume=15 |issue= 5 |pages= 1068–75 |year= 2007 |pmid= 17495181 |doi=10.1038/oby.2007.630  |display-authors=etal}}
*{{cite journal  | author=Adamo KB, Dent R, Langefeld CD, ''et al.'' |title=Peroxisome proliferator-activated receptor gamma 2 and acyl-CoA synthetase 5 polymorphisms influence diet response. |journal=Obesity (Silver Spring, Md.) |volume=15 |issue= 5 |pages= 1068-75 |year= 2007 |pmid= 17495181 |doi= }}
*{{cite journal  | vauthors=Gassler N, Roth W, Funke B |title=Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing |journal=Gastroenterology |volume=133 |issue= 2 |pages= 587–98 |year= 2007 |pmid= 17681178 |doi= 10.1053/j.gastro.2007.06.005 |display-authors=etal}}
*{{cite journal  | author=Gassler N, Roth W, Funke B, ''et al.'' |title=Regulation of enterocyte apoptosis by acyl-CoA synthetase 5 splicing. |journal=Gastroenterology |volume=133 |issue= 2 |pages= 587-98 |year= 2007 |pmid= 17681178 |doi= 10.1053/j.gastro.2007.06.005 }}
*{{cite journal  | vauthors=Zhou Y, Abidi P, Kim A |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 |display-authors=etal}}
*{{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}}


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[[Category:Human proteins]]
 
 
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Latest revision as of 17:45, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Long-chain-fatty-acid—CoA ligase 5 is an enzyme that in humans is encoded by the ACSL5 gene.[1][2]

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 uterus and spleen, and in trace amounts in normal brain, but has markedly increased levels in malignant gliomas. This gene functions in mediating fatty acid-induced glioma cell growth. Three transcript variants encoding two different isoforms have been found for this gene.[2]

References

  1. ↑ Yamashita Y, Kumabe T, Cho YY, Watanabe M, Kawagishi J, Yoshimoto T, Fujino T, Kang MJ, Yamamoto TT (Dec 2000). "Fatty acid induced glioma cell growth is mediated by the acyl-CoA synthetase 5 gene located on chromosome 10q25.1-q25.2, a region frequently deleted in malignant gliomas". Oncogene. 19 (51): 5919–25. doi:10.1038/sj.onc.1203981. PMID 11127823.
  2. ↑ 2.0 2.1 "Entrez Gene: ACSL5 acyl-CoA synthetase long-chain family member 5".

External links

Further reading


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