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{{Infobox_gene}}
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'''Very long-chain acyl-CoA synthetase''' is an [[enzyme]] that in humans is encoded by the ''SLC27A2'' [[gene]].<ref name="pmid9730624">{{cite journal | vauthors = Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y | title = Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1 gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in situ hybridization | journal = Cytogenet Cell Genet | volume = 81 | issue = 3-4 | pages = 292–3 |date=Oct 1998 | pmid = 9730624 | pmc =  | doi =10.1159/000015051 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11001| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = Solute carrier family 27 (fatty acid transporter), member 2
| HGNCid = 10996
| Symbol = SLC27A2
| AltSymbols =; ACSVL1; FACVL1; FATP2; HsT17226; VLACS; VLCS; hFACVL1
| OMIM = 603247
| ECnumber = 
| Homologene = 37830
| MGIid = 1347099
| GeneAtlas_image1 = PBB_GE_SLC27A2_205769_at_tn.png
| GeneAtlas_image2 = PBB_GE_SLC27A2_205768_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003824 |text = catalytic 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:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0005782 |text = peroxisomal matrix}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000038 |text = very-long-chain fatty acid metabolic process}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 11001
    | Hs_Ensembl = ENSG00000140284
    | Hs_RefseqProtein = NP_003636
    | Hs_RefseqmRNA = NM_003645
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 48261716
    | Hs_GenLoc_end = 48315873
    | Hs_Uniprot = O14975
    | Mm_EntrezGene = 26458
    | Mm_Ensembl = ENSMUSG00000027359
    | Mm_RefseqmRNA = NM_011978
    | Mm_RefseqProtein = NP_036108
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 126244482
    | Mm_GenLoc_end = 126279682
    | Mm_Uniprot = Q3TN99
  }}
}}
'''Solute carrier family 27 (fatty acid transporter), member 2''', also known as '''SLC27A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11001| 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 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 activates long-chain, branched-chain and very-long-chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy.<ref name="entrez">{{cite web | title = Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11001| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is an isozyme of 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 activates long-chain, branched-chain and [[very long chain fatty acid]]s containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked [[adrenoleukodystrophy]].<ref name="entrez" />
}}
}}


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==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
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{{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=Uchiyama A, Aoyama T, Kamijo K, ''et al.'' |title=Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30360-5 |year= 1997 |pmid= 8939997 |doi=  }}
*{{cite journal   |vauthors=Uchiyama A, Aoyama T, Kamijo K, etal |title=Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30360–5 |year= 1997 |pmid= 8939997 |doi=10.1074/jbc.271.48.30360 }}
*{{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, etal |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 }}
*{{cite journal  | author=Hirsch D, Stahl A, Lodish HF |title=A family of fatty acid transporters conserved from mycobacterium to man. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8625-9 |year= 1998 |pmid= 9671728 |doi= }}
*{{cite journal  | vauthors=Hirsch D, Stahl A, Lodish HF |title=A family of fatty acid transporters conserved from mycobacterium to man. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8625–9 |year= 1998 |pmid= 9671728 |doi=10.1073/pnas.95.15.8625  | pmc=21126 }}
*{{cite journal  | author=Wakui K, Aoyama T, Uchiyama A, ''et al.'' |title=Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1 gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 292-3 |year= 1998 |pmid= 9730624 |doi=  }}
*{{cite journal   |vauthors=Steinberg SJ, Wang SJ, Kim DG, etal |title=Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 2 |pages= 615–21 |year= 1999 |pmid= 10198260 |doi= 10.1006/bbrc.1999.0510 }}
*{{cite journal | author=Steinberg SJ, Wang SJ, Kim DG, ''et al.'' |title=Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 2 |pages= 615-21 |year= 1999 |pmid= 10198260 |doi= 10.1006/bbrc.1999.0510 }}
*{{cite journal  | vauthors=Watkins PA, Pevsner J, Steinberg SJ |title=Human very long-chain acyl-CoA synthetase and two human homologs: initial characterization and relationship to fatty acid transport protein. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=60 |issue= 5-6 |pages= 323–8 |year= 2000 |pmid= 10471116 |doi=10.1016/S0952-3278(99)80007-6 }}
*{{cite journal  | author=Watkins PA, Pevsner J, Steinberg SJ |title=Human very long-chain acyl-CoA synthetase and two human homologs: initial characterization and relationship to fatty acid transport protein. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=60 |issue= 5-6 |pages= 323-8 |year= 2000 |pmid= 10471116 |doi=  }}
*{{cite journal  | vauthors=Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA |title=Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. |journal=Mol. Genet. Metab. |volume=68 |issue= 1 |pages= 32–42 |year= 1999 |pmid= 10479480 |doi= 10.1006/mgme.1999.2883 }}
*{{cite journal  | author=Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA |title=Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein. |journal=Mol. Genet. Metab. |volume=68 |issue= 1 |pages= 32-42 |year= 1999 |pmid= 10479480 |doi= 10.1006/mgme.1999.2883 }}
*{{cite journal   |vauthors=Mihalik SJ, Steinberg SJ, Pei Z, etal |title=Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24771–9 |year= 2002 |pmid= 11980911 |doi= 10.1074/jbc.M203295200 }}
*{{cite journal | author=Mihalik SJ, Steinberg SJ, Pei Z, ''et al.'' |title=Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24771-9 |year= 2002 |pmid= 11980911 |doi= 10.1074/jbc.M203295200 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{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=Ota T, Suzuki Y, Nishikawa T, etal |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 | 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 }}
}}
}}
{{refend}}
{{refend}}


{{membrane-protein-stub}}
{{NLM content}}
{{NLM content}}
{{Membrane transport proteins}}
{{Membrane transport proteins}}
{{Peroxisomal metabolism enzymes}}
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[[Category:Solute carrier family]]
[[Category:Solute carrier family]]
{{WikiDoc Sources}}
 
 
{{membrane-protein-stub}}

Latest revision as of 06:30, 11 September 2017

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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RefSeq (mRNA)

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RefSeq (protein)

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Wikidata
View/Edit Human

Very long-chain acyl-CoA synthetase is an enzyme that in humans is encoded by the SLC27A2 gene.[1][2]

The protein encoded by this gene is an isozyme of 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 activates long-chain, branched-chain and very long chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy.[2]

See also

References

  1. ↑ Wakui K, Aoyama T, Uchiyama A, Hashimoto T, Fukushima Y (Oct 1998). "Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1 gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in situ hybridization". Cytogenet Cell Genet. 81 (3–4): 292–3. doi:10.1159/000015051. PMID 9730624.
  2. ↑ 2.0 2.1 "Entrez Gene: SLC27A2 solute carrier family 27 (fatty acid transporter), member 2".

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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