Full text data of ACSL3
ACSL3
(ACS3, FACL3, LACS3)
[Confidence: high (present in two of the MS resources)]
Long-chain-fatty-acid--CoA ligase 3; 6.2.1.3 (Long-chain acyl-CoA synthetase 3; LACS 3)
Long-chain-fatty-acid--CoA ligase 3; 6.2.1.3 (Long-chain acyl-CoA synthetase 3; LACS 3)
hRBCD
IPI00031397
IPI00031397 Long-chain-fatty-acid--CoA ligase 3 Long-chain-fatty-acid--CoA ligase 3 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a 1 n/a n/a Type III membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00031397 Long-chain-fatty-acid--CoA ligase 3 Long-chain-fatty-acid--CoA ligase 3 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a 1 n/a n/a Type III membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O95573
ID ACSL3_HUMAN Reviewed; 720 AA.
AC O95573; Q60I92; Q8IUM9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 3;
DE EC=6.2.1.3;
DE AltName: Full=Long-chain acyl-CoA synthetase 3;
DE Short=LACS 3;
GN Name=ACSL3; Synonyms=ACS3, FACL3, LACS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-551.
RC TISSUE=Placenta;
RX PubMed=9177793; DOI=10.1006/geno.1997.4710;
RA Minekura H., Fujino T., Kang M.-J., Fujita T., Endo Y., Yamamoto T.T.;
RT "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene
RT (ACS3) to chromosome band 2q34-q35.";
RL Genomics 42:180-181(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-551.
RX PubMed=11707336; DOI=10.1016/S0378-1119(01)00714-4;
RA Minekura H., Kang M.-J., Inagaki Y., Suzuki H., Sato H., Fujino T.,
RA Yamamoto T.T.;
RT "Genomic organization and transcription units of the human acyl-CoA
RT synthetase 3 gene.";
RL Gene 278:185-192(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=18003621; DOI=10.1074/jbc.M706160200;
RA Yao H., Ye J.;
RT "Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine
RT synthesis is required for assembly of very low density lipoproteins in
RT human hepatoma Huh7 cells.";
RL J. Biol. Chem. 283:849-854(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty
CC acids for both synthesis of cellular lipids, and degradation via
CC beta-oxidation. ACSL3 mediates hepatic lipogenesis (By
CC similarity). Preferentially uses myristate, laurate, arachidonate
CC and eicosapentaenoate as substrates (By similarity). Has mainly an
CC anabolic role in energy metabolism. Required for the incorporation
CC of fatty acids into phosphatidylcholine, the major phospholipid
CC located on the surface of VLDL (very low density lipoproteins).
CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
CC diphosphate + an acyl-CoA.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC type III membrane protein (By similarity). Peroxisome membrane;
CC Single-pass type III membrane protein (By similarity). Microsome
CC membrane; Single-pass type III membrane protein (By similarity).
CC Endoplasmic reticulum membrane; Single-pass type III membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D89053; BAA37142.1; -; mRNA.
DR EMBL; AB061712; BAB72074.1; -; mRNA.
DR EMBL; AB061436; BAB72139.1; -; Genomic_DNA.
DR EMBL; BC041692; AAH41692.1; -; mRNA.
DR RefSeq; NP_004448.2; NM_004457.3.
DR RefSeq; NP_976251.1; NM_203372.1.
DR UniGene; Hs.655772; -.
DR ProteinModelPortal; O95573; -.
DR SMR; O95573; 122-641.
DR IntAct; O95573; 11.
DR MINT; MINT-4527745; -.
DR STRING; 9606.ENSP00000350012; -.
DR DrugBank; DB00159; Icosapent.
DR PhosphoSite; O95573; -.
DR PaxDb; O95573; -.
DR PeptideAtlas; O95573; -.
DR PRIDE; O95573; -.
DR Ensembl; ENST00000357430; ENSP00000350012; ENSG00000123983.
DR Ensembl; ENST00000392066; ENSP00000375918; ENSG00000123983.
DR GeneID; 2181; -.
DR KEGG; hsa:2181; -.
DR UCSC; uc002vni.3; human.
DR CTD; 2181; -.
DR GeneCards; GC02P223725; -.
DR HGNC; HGNC:3570; ACSL3.
DR HPA; HPA011315; -.
DR MIM; 602371; gene.
DR neXtProt; NX_O95573; -.
DR PharmGKB; PA27967; -.
DR eggNOG; COG1022; -.
DR HOGENOM; HOG000159459; -.
DR HOVERGEN; HBG106947; -.
DR InParanoid; O95573; -.
DR KO; K01897; -.
DR OMA; VFMYAKN; -.
DR OrthoDB; EOG7P2XRD; -.
DR PhylomeDB; O95573; -.
DR BioCyc; MetaCyc:HS04703-MONOMER; -.
DR BRENDA; 6.2.1.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ACSL3; -.
DR GenomeRNAi; 2181; -.
DR NextBio; 8805; -.
DR PRO; PR:O95573; -.
DR ArrayExpress; O95573; -.
DR Bgee; O95573; -.
DR CleanEx; HS_ACSL3; -.
DR Genevestigator; O95573; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:UniProtKB.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 720 Long-chain-fatty-acid--CoA ligase 3.
FT /FTId=PRO_0000193107.
FT TRANSMEM 21 41 Helical; Signal-anchor for type III
FT membrane protein; (Potential).
FT TOPO_DOM 42 720 Cytoplasmic (Potential).
FT MOD_RES 683 683 Phosphoserine.
FT VARIANT 551 551 F -> S (in dbSNP:rs1046032).
FT /FTId=VAR_026716.
FT CONFLICT 246 246 E -> D (in Ref. 1; BAA37142 and 2;
FT BAB72074/BAB72139).
SQ SEQUENCE 720 AA; 80420 MW; AAC4B0B4543EC8DD CRC64;
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI
SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
//
ID ACSL3_HUMAN Reviewed; 720 AA.
AC O95573; Q60I92; Q8IUM9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 03-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase 3;
DE EC=6.2.1.3;
DE AltName: Full=Long-chain acyl-CoA synthetase 3;
DE Short=LACS 3;
GN Name=ACSL3; Synonyms=ACS3, FACL3, LACS3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-551.
RC TISSUE=Placenta;
RX PubMed=9177793; DOI=10.1006/geno.1997.4710;
RA Minekura H., Fujino T., Kang M.-J., Fujita T., Endo Y., Yamamoto T.T.;
RT "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene
RT (ACS3) to chromosome band 2q34-q35.";
RL Genomics 42:180-181(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT SER-551.
RX PubMed=11707336; DOI=10.1016/S0378-1119(01)00714-4;
RA Minekura H., Kang M.-J., Inagaki Y., Suzuki H., Sato H., Fujino T.,
RA Yamamoto T.T.;
RT "Genomic organization and transcription units of the human acyl-CoA
RT synthetase 3 gene.";
RL Gene 278:185-192(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=18003621; DOI=10.1074/jbc.M706160200;
RA Yao H., Ye J.;
RT "Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine
RT synthesis is required for assembly of very low density lipoproteins in
RT human hepatoma Huh7 cells.";
RL J. Biol. Chem. 283:849-854(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty
CC acids for both synthesis of cellular lipids, and degradation via
CC beta-oxidation. ACSL3 mediates hepatic lipogenesis (By
CC similarity). Preferentially uses myristate, laurate, arachidonate
CC and eicosapentaenoate as substrates (By similarity). Has mainly an
CC anabolic role in energy metabolism. Required for the incorporation
CC of fatty acids into phosphatidylcholine, the major phospholipid
CC located on the surface of VLDL (very low density lipoproteins).
CC -!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
CC diphosphate + an acyl-CoA.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC type III membrane protein (By similarity). Peroxisome membrane;
CC Single-pass type III membrane protein (By similarity). Microsome
CC membrane; Single-pass type III membrane protein (By similarity).
CC Endoplasmic reticulum membrane; Single-pass type III membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D89053; BAA37142.1; -; mRNA.
DR EMBL; AB061712; BAB72074.1; -; mRNA.
DR EMBL; AB061436; BAB72139.1; -; Genomic_DNA.
DR EMBL; BC041692; AAH41692.1; -; mRNA.
DR RefSeq; NP_004448.2; NM_004457.3.
DR RefSeq; NP_976251.1; NM_203372.1.
DR UniGene; Hs.655772; -.
DR ProteinModelPortal; O95573; -.
DR SMR; O95573; 122-641.
DR IntAct; O95573; 11.
DR MINT; MINT-4527745; -.
DR STRING; 9606.ENSP00000350012; -.
DR DrugBank; DB00159; Icosapent.
DR PhosphoSite; O95573; -.
DR PaxDb; O95573; -.
DR PeptideAtlas; O95573; -.
DR PRIDE; O95573; -.
DR Ensembl; ENST00000357430; ENSP00000350012; ENSG00000123983.
DR Ensembl; ENST00000392066; ENSP00000375918; ENSG00000123983.
DR GeneID; 2181; -.
DR KEGG; hsa:2181; -.
DR UCSC; uc002vni.3; human.
DR CTD; 2181; -.
DR GeneCards; GC02P223725; -.
DR HGNC; HGNC:3570; ACSL3.
DR HPA; HPA011315; -.
DR MIM; 602371; gene.
DR neXtProt; NX_O95573; -.
DR PharmGKB; PA27967; -.
DR eggNOG; COG1022; -.
DR HOGENOM; HOG000159459; -.
DR HOVERGEN; HBG106947; -.
DR InParanoid; O95573; -.
DR KO; K01897; -.
DR OMA; VFMYAKN; -.
DR OrthoDB; EOG7P2XRD; -.
DR PhylomeDB; O95573; -.
DR BioCyc; MetaCyc:HS04703-MONOMER; -.
DR BRENDA; 6.2.1.3; 2681.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; ACSL3; -.
DR GenomeRNAi; 2181; -.
DR NextBio; 8805; -.
DR PRO; PR:O95573; -.
DR ArrayExpress; O95573; -.
DR Bgee; O95573; -.
DR CleanEx; HS_ACSL3; -.
DR Genevestigator; O95573; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:UniProtKB.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 720 Long-chain-fatty-acid--CoA ligase 3.
FT /FTId=PRO_0000193107.
FT TRANSMEM 21 41 Helical; Signal-anchor for type III
FT membrane protein; (Potential).
FT TOPO_DOM 42 720 Cytoplasmic (Potential).
FT MOD_RES 683 683 Phosphoserine.
FT VARIANT 551 551 F -> S (in dbSNP:rs1046032).
FT /FTId=VAR_026716.
FT CONFLICT 246 246 E -> D (in Ref. 1; BAA37142 and 2;
FT BAB72074/BAB72139).
SQ SEQUENCE 720 AA; 80420 MW; AAC4B0B4543EC8DD CRC64;
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI
SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
//
MIM
602371
*RECORD*
*FIELD* NO
602371
*FIELD* TI
*602371 ACYL-CoA SYNTHETASE LONG CHAIN FAMILY, MEMBER 3; ACSL3
;;FATTY ACID CoA LIGASE, LONG CHAIN 3; FACL3;;
read moreACYL-CoA SYNTHETASE 3; ACS3
*FIELD* TX
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 ACSL3, which form an activating thioester linkage
between the fatty acid and CoA (Watkins et al., 2007).
CLONING
Fujino et al. (1996) cloned rat Acs3 by PCR of a rat brain cDNA library.
The deduced 720-amino acid rat protein has a calculated molecular mass
of approximately 80 kD. SDS-PAGE of purified Acs3 revealed 2 major
proteins with apparent molecular masses of 79 and 80 kD. Northern blot
analysis of rat tissues showed that Acs3 was predominantly expressed in
brain. Lower expression was detected in lung, adrenal gland, kidney,
small intestine, and adipose tissue, and no expression was detected in
heart and liver.
Minekura et al. (1997) used rat ACS3 cDNA as a probe to isolate a human
ACS3 clone from a placenta cDNA library. The predicted 720-amino acid
human protein is 92% identical to rat Acs3.
By searching databases for sequences containing acyl-CoA synthetase
motifs 1 and 2, Watkins et al. (2007) identified a splice variant of
human ACSL3 with a different 5-prime UTR. Phylogenetic analysis revealed
that ACSL3 belongs to a family of long chain acyl-CoA synthetases.
GENE FUNCTION
Fujino et al. (1996) found that rat Acs3 preferentially used myristate,
laurate, arachidonate, and eicosapentaenoate as substrates.
GENE STRUCTURE
Watkins et al. (2007) determined that the ACSL3 gene contains at least
17 exons.
MAPPING
By somatic cell hybrid analysis and FISH, Minekura et al. (1997) mapped
the ACS3 gene to chromosome 2q34-q35. Watkins et al. (2007) mapped the
ACSL3 gene to the plus strand of chromosome 2q34-q35 by genomic sequence
analysis.
*FIELD* RF
1. Fujino, T.; Kang, M.-J.; Suzuki, H.; Iijima, H.; Yamamoto, T.:
Molecular characterization and expression of rat acyl-CoA synthetase
3. J. Biol. Chem. 271: 16748-16752, 1996.
2. Minekura, H.; Fujino, T.; Kang, M.-J.; Fujita, T.; Endo, Y.; Yamamoto,
T. T.: Human acyl-coenzyme A synthetase 3 cDNA and localization of
its gene (ACS3) to chromosome band 2q34-q35. Genomics 42: 180-181,
1997.
3. 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.
*FIELD* CN
Matthew B. Gross - updated: 11/30/2011
Patricia A. Hartz - updated: 10/4/2011
*FIELD* CD
Rebekah S. Rasooly: 2/20/1998
*FIELD* ED
mgross: 12/02/2011
mgross: 11/30/2011
terry: 10/4/2011
terry: 9/19/2008
mgross: 1/6/2004
mgross: 2/22/2001
terry: 4/25/2000
alopez: 10/1/1998
alopez: 2/20/1998
*RECORD*
*FIELD* NO
602371
*FIELD* TI
*602371 ACYL-CoA SYNTHETASE LONG CHAIN FAMILY, MEMBER 3; ACSL3
;;FATTY ACID CoA LIGASE, LONG CHAIN 3; FACL3;;
read moreACYL-CoA SYNTHETASE 3; ACS3
*FIELD* TX
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 ACSL3, which form an activating thioester linkage
between the fatty acid and CoA (Watkins et al., 2007).
CLONING
Fujino et al. (1996) cloned rat Acs3 by PCR of a rat brain cDNA library.
The deduced 720-amino acid rat protein has a calculated molecular mass
of approximately 80 kD. SDS-PAGE of purified Acs3 revealed 2 major
proteins with apparent molecular masses of 79 and 80 kD. Northern blot
analysis of rat tissues showed that Acs3 was predominantly expressed in
brain. Lower expression was detected in lung, adrenal gland, kidney,
small intestine, and adipose tissue, and no expression was detected in
heart and liver.
Minekura et al. (1997) used rat ACS3 cDNA as a probe to isolate a human
ACS3 clone from a placenta cDNA library. The predicted 720-amino acid
human protein is 92% identical to rat Acs3.
By searching databases for sequences containing acyl-CoA synthetase
motifs 1 and 2, Watkins et al. (2007) identified a splice variant of
human ACSL3 with a different 5-prime UTR. Phylogenetic analysis revealed
that ACSL3 belongs to a family of long chain acyl-CoA synthetases.
GENE FUNCTION
Fujino et al. (1996) found that rat Acs3 preferentially used myristate,
laurate, arachidonate, and eicosapentaenoate as substrates.
GENE STRUCTURE
Watkins et al. (2007) determined that the ACSL3 gene contains at least
17 exons.
MAPPING
By somatic cell hybrid analysis and FISH, Minekura et al. (1997) mapped
the ACS3 gene to chromosome 2q34-q35. Watkins et al. (2007) mapped the
ACSL3 gene to the plus strand of chromosome 2q34-q35 by genomic sequence
analysis.
*FIELD* RF
1. Fujino, T.; Kang, M.-J.; Suzuki, H.; Iijima, H.; Yamamoto, T.:
Molecular characterization and expression of rat acyl-CoA synthetase
3. J. Biol. Chem. 271: 16748-16752, 1996.
2. Minekura, H.; Fujino, T.; Kang, M.-J.; Fujita, T.; Endo, Y.; Yamamoto,
T. T.: Human acyl-coenzyme A synthetase 3 cDNA and localization of
its gene (ACS3) to chromosome band 2q34-q35. Genomics 42: 180-181,
1997.
3. 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.
*FIELD* CN
Matthew B. Gross - updated: 11/30/2011
Patricia A. Hartz - updated: 10/4/2011
*FIELD* CD
Rebekah S. Rasooly: 2/20/1998
*FIELD* ED
mgross: 12/02/2011
mgross: 11/30/2011
terry: 10/4/2011
terry: 9/19/2008
mgross: 1/6/2004
mgross: 2/22/2001
terry: 4/25/2000
alopez: 10/1/1998
alopez: 2/20/1998