P-POD: Princeton Protein Orthology Database: GO3/Nens205

This family has 56 members: 9 Arabidopsis thaliana, 8 Caenorhabditis elegans, 8 Danio rerio, 2 Dictyostelium discoideum, 2 Drosophila melanogaster, 1 Escherichia coli, 5 Gallus gallus, 5 Homo sapiens, 5 Mus musculus, 5 Rattus norvegicus, 4 Saccharomyces cerevisiae, 2 Schizosaccharomyces pombe.

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GO3/Nens205
56 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaTAIR:locus:2014265 (F15H21.7 · F15H21_7 · AT1G64400) · NCBI:NP_176622.1⌘
A. thalianaNCBI:NP_198112.2 · TAIR:locus:2143661 (F15A18.60 · F15A18_60 · LACS7 · AT5G27600)LONG-CHAIN ACYL-COA SYNTHETASE 7⌘
A. thalianaNCBI:NP_566265.1 · TAIR:locus:2083013 (F2O10_7 · AT3G05970 · LACS6 · F2O10.7)long-chain acyl-CoA synthetase 6⌘
A. thalianaNCBI:NP_194116.1 · TAIR:locus:2138141 (T32A16.20 · AT4G23850 · T32A16_20)⌘
A. thalianaNCBI:NP_175368.2 · TAIR:locus:2010177 (F13F21_14 · LACS2 · LRD2 · F13F21.14 · AT1G49430)LONG-CHAIN ACYL-COA SYNTHETASE 2 · LATERAL ROOT DEVELOPMENT 2⌘
A. thalianaNCBI:NP_177882.1 · TAIR:locus:2204765 (LACS9 · T5M16.18 · T5M16_18 · AT1G77590)LONG CHAIN ACYL-COA SYNTHETASE 9⌘
A. thalianaNCBI:NP_178516.1 · TAIR:locus:2058384 (T23O15_3 · T23O15.3 · AT2G04350)⌘
A. thalianaNCBI:NP_182246.1 · TAIR:locus:2065195 (AT2G47240 · T8I13.8)⌘
A. thalianaNCBI:NP_192841.1 · TAIR:locus:2136148 (T22B4.10 · T22B4_10 · AT4G11030)⌘
C. elegansWB:WBGene00019920 · UniProtKB:O16775
C. elegansWB:WBGene00020343 (acs-3 · T08B1.6) · UniProtKB:O44560⌘
C. elegansWB:WBGene00016716 (C46F4.2 · acs-17) · UniProtKB:Q18660⌘
C. elegansWB:WBGene00018152 (F37C12.7 · acs-4) · UniProtKB:Q20121⌘
C. elegansWB:WBGene00011173 · UniProtKB:Q21872
C. elegansWB:WBGene00011174 · UniProtKB:Q21873
C. elegansWB:WBGene00022037 · UniProtKB:Q9N302
C. elegansWB:WBGene00013575 · UniProtKB:Q9XWD1
D. rerioENSEMBL:ENSDARP00000079273
D. rerioENSEMBL:ENSDARP00000046412
D. rerioENSEMBL:ENSDARP00000088720
D. rerioZFIN:ZDB-GENE-050420-181 (si:dkeyp-109h9.2) · UniProtKB:Q1LVA8⌘
D. rerioUniProtKB:Q499A9 · ZFIN:ZDB-GENE-050809-115 (acsl1)acyl-CoA synthetase long-chain family member 1⌘
D. rerioUniProtKB:Q58EE3 · ZFIN:ZDB-GENE-030131-6493 (acsl4l)acyl-CoA synthetase long-chain family member 4, like⌘
D. rerioZFIN:ZDB-GENE-040801-88 (zgc:101071) · UniProtKB:Q6DEJ3⌘
D. rerioUniProtKB:Q6PFP1 · ZFIN:ZDB-GENE-040426-1565 (acsl4a)acyl-CoA synthetase long-chain family member 4a⌘
D. discoideumUniProtKB:Q55DR6 · dictyBase:DDB_G0269242 (fcsA)LC-FACS 1 · fatty acyl-CoA synthetase, long-chain-fatty-acid-CoA ligase⌘
D. discoideumUniProtKB:Q1ZXQ4 · dictyBase:DDB_G0269474 (fcsB)fatty acyl-CoA synthetase, long-chain-fatty-acid-CoA ligase⌘
D. melanogasterUniProtKB:Q8T3L1 · FB:FBgn0010609 (anon-WO0172774.173 · l(2)7447 · l(2)05847 · CG8732 · l(2)k05304 · 7447 · l(2)44DEa)Fatty acyl-CoA synthetase · lethal (2) 44DEa · Fatty acyl CoA synthetase⌘
D. melanogasterFB:FBgn0036821 (CG3961) · UniProtKB:Q9VVT8⌘
E. coliUniProtKB:P31119 · ECOLI:AAS-MONOMER (b2836 · ECK2832 · aas · Aas)2-acylglycerophosphoethanolamine acyltransferase / acyl-ACP synthetase⌘
G. gallusNCBI:XP_422625 · ENTREZ:424810
G. gallusNCBI:XP_414641 · ENTREZ:416324
G. gallusNCBI:XP_420317 · ENTREZ:422345
G. gallusUniProtKB:Q5F420 (Q5F420 · RCJMB04_3m22 · IPI00574629) · ENTREZ:422547⌘
G. gallusUniProtKB:Q5ZIG7 (RCJMB04_26g6 · IPI00651137 · Q5ZIG7) · ENTREZ:423896⌘
H. sapiensENSEMBL:ENSG00000151726 · UniProtKB:P33121 (FACL2 · IPI00012728 · FACL1 · ACSL1 · ACSL1_HUMAN · LACS2 · P33121 · LACS · LACS1 · IPI00401448)Long-chain-fatty-acid--CoA ligase 1⌘
H. sapiensENSEMBL:ENSG00000123983 · UniProtKB:O95573 (ACSL3_HUMAN · ACSL3 · ACS3 · LACS3 · FACL3 · IPI00031397 · O95573)Long-chain-fatty-acid--CoA ligase 3⌘
H. sapiensENSEMBL:ENSG00000068366 · UniProtKB:O60488 (IPI00029737 · ACSL4_HUMAN · FACL4 · O60488 · ACSL4 · IPI00219897 · ACS4 · LACS4)Long-chain-fatty-acid--CoA ligase 4⌘
H. sapiensENSEMBL:ENSG00000197142 · UniProtKB:Q9ULC5 (ACSL5 · FACL5 · Q9ULC5 · IPI00008037 · IPI00411387 · ACS5 · UNQ633/PRO1250 · ACSL5_HUMAN)Long-chain-fatty-acid--CoA ligase 5⌘
H. sapiensENSEMBL:ENSG00000164398 · UniProtKB:Q9UKU0 (FACL6 · ACSL6 · Q9UKU0 · IPI00296333 · LACS5 · ACS2 · IPI00657883 · IPI00657816 · KIAA0837 · ACSL6_HUMAN)Long-chain-fatty-acid--CoA ligase 6⌘
M. musculusUniProtKB:P41216 · MGI:MGI:102797 (Acsl1 · Facl2 · Acas1)acyl-CoA synthetase long-chain family member 1⌘
M. musculusUniProtKB:Q9CZW4 · MGI:MGI:1921455 (Facl3 · C85929 · Acsl3)acyl-CoA synthetase long-chain family member 3⌘
M. musculusUniProtKB:Q9QUJ7 · MGI:MGI:1354713 (Acsl4 · Lacs4 · Facl4 · ACS4)acyl-CoA synthetase long-chain family member 4⌘
M. musculusUniProtKB:Q8JZR0 · MGI:MGI:1919129 (Facl5 · Acsl5)acyl-CoA synthetase long-chain family member 5⌘
M. musculusUniProtKB:Q91WC3 · MGI:MGI:894291 (Acsl6 · Lacsl · Facl6)acyl-CoA synthetase long-chain family member 6⌘
R. norvegicusUniProtKB:P18163 · RGD:2015 (Acsl1)acyl-CoA synthetase long-chain family member 1⌘
R. norvegicusUniProtKB:Q63151 (ACSL3_RAT · IPI00760128 · Acs3 · Facl3 · Acsl3 · IPI00205908 · Q63151) · RGD:70552 (Acsl3)Long-chain-fatty-acid--CoA ligase 3 · acyl-CoA synthetase long-chain family member 3⌘⌘
R. norvegicusUniProtKB:O35547 · RGD:69401 (Acsl4)acyl-CoA synthetase long-chain family member 4⌘
R. norvegicusUniProtKB:O88813 · RGD:69402 (Acsl5)acyl-CoA synthetase long-chain family member 5⌘
R. norvegicusRGD:69403 (Acsl6) · UniProtKB:P33124 (Acsl6 · Acs2 · ACSL6_RAT · IPI00324041 · Facl6 · P33124)acyl-CoA synthetase long-chain family member 6 · Long-chain-fatty-acid--CoA ligase 6⌘⌘
S. cerevisiaeUniProtKB:P30624 · SGD:S000005844 (YOR317W · FAA1)Long chain fatty acyl-CoA synthetase with a preference for C12:0-C16:0 fatty acids⌘
S. cerevisiaeUniProtKB:P39518 · SGD:S000000817 (FAA2 · FAM1 · YER015W)Long chain fatty acyl-CoA synthetase⌘
S. cerevisiaeUniProtKB:P39002 · SGD:S000001271 (YIL009W · FAA3)Long chain fatty acyl-CoA synthetase, has a preference for C16 and C18 fatty acids⌘
S. cerevisiaeUniProtKB:P47912 · SGD:S000004860 (YMR246W · FAA4)Long chain fatty acyl-CoA synthetase, regulates protein modification during growth in the presence of ethanol, functions to incorporate palmitic acid into phospholipids and neutral lipids⌘
S. pombeUniProtKB:O60135 · GeneDB_Spombe:SPBC18H10.02 (lcf1 · SPBC18H10.02)long-chain-fatty-acid-CoA ligase Lcf1⌘
S. pombeUniProtKB:Q9P7D7 · GeneDB_Spombe:SPBP4H10.11c (SPBP4H10.11c · lcf2)long-chain-fatty-acid-CoA ligase⌘
ProteinPublicationCurator Notes
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL1 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL1 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G20560.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G20560.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P47912 · SGD:S000004860PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein RLACS complements a homologous mutation in S. cerevisiae. The authors note that the sensitivity of Faa4p and rat liver acyl-CoA synthetase (RLACS), but not Faa1p, to inhibition by triacsin C suggests that RLACS is functionally more similar to Faa4p than to Faa1p.
UniProtKB:P30624 · SGD:S000005844PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein RLACS complements a homologous mutation in S. cerevisiae. The authors note that the sensitivity of Faa4p and rat liver acyl-CoA synthetase (RLACS), but not Faa1p, to inhibition by triacsin C suggests that RLACS is functionally more similar to Faa4p than to Faa1p.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP1 (Q60714) complements a yeast faa1 fat1 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL4 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL4 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL5 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL5 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL6 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL6 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21530.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21530.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21540.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21540.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G75960.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G75960.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G77240.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G77240.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT2G17650.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT2G17650.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT3G16910.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT3G16910.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16340.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16340.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16370.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16370.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP2 (O35488) complements a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP3 (O88561) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP6 (Q14C50) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP5 (Q4LDG0) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP4 (Q91VE0) complements a yeast faa1 fat1 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:22633490 Nakahara K, et al. The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell. 2012 May 25;46(4):461-71.The H. sapiens protein ACSL1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:22633490 Nakahara K, et al. The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell. 2012 May 25;46(4):461-71.The H. sapiens protein ACSL1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL3 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL3 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A4 and ACSVL4 complement a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A4 and ACSVL4 complement a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A2 and ACSLV1 complement a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A2 and ACSLV1 complement a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSBG1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSBG1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL6 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL6 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL5 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL5 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein Acsl1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein Acsl1 complements a homologous mutation in S. cerevisiae.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
OMIM (2)
ENSEMBL:ENSG00000068366 · UniProtKB:O60488#300194 AMME COMPLEX;;ALPORT SYNDROME, MENTAL RETARDATION, MIDFACE HYPOPLASIA, AND ELLIPTOCYTOSIS;;ATS-MR
UniProtKB:P39518 · SGD:S000000817#300387 MENTAL RETARDATION, X-LINKED 63; MRX63;;MENTAL RETARDATION, X-LINKED 68; MRX68
SGD Disease Papers (13)
UniProtKB:P39518 · SGD:S000000817PMID:8441467 Mosser J, et al. (1993) Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. Nature 361(6414):726-30
PMID:8209376 Bojes HK and Thurman RG (1994) Peroxisomal proliferators inhibit acyl CoA synthetase and stimulate protein kinase C in vivo. Toxicol Appl Pharmacol 126(2):233-9
PMID:7818538 Kalish JE, et al. (1995) Peroxisomal activation of long- and very long-chain fatty acids in the yeast Pichia pastoris. Biochem Biophys Res Commun 206(1):335-40
PMID:6303275 Sasaki N, et al. (1982) Effect of hypertension on lipid metabolism and beta-oxidation in rat aorta and brain microvessels. Artery 11(2):108-18
PMID:6242313 Carroll JE, et al. (1984) Brominated vegetable oil myopathy: inhibition at multiple sites. Muscle Nerve 7(8):642-6
PMID:6148682 Dang AQ, et al. (1984) Effects of streptozotocin-induced diabetes on microsomal long-chain fatty acyl-CoA synthetase and hydrolase. Lipids 19(8):578-82
PMID:6125278 Berthillier G, et al. (1982) Carnitine metabolism in early stages of Duchenne muscular dystrophy. Clin Chim Acta 122(3):369-75
PMID:6108603 Berge RK, et al. (1980) Intracellular localization of palmitoyl-CoA hydrolase and palmitoyl-CoA synthetase in human blood platelets and liver. Scand J Clin Lab Invest 40(3):271-8
PMID:4074391 Clark DL and Queener SF (1985) Effects of diabetes mellitus on renal fatty acid activation and desaturation. Biochem Pharmacol 34(24):4305-10
PMID:3801501 Harvey BE and Crain RC (1987) Biosynthesis of glycerolipids by hepatoma and liver microsomes. I. Fatty acyl-CoA ligase and acyl-CoA:sn-glycerol-3-phosphate acyltransferase. Biochim Biophys Acta 917(2):247-57
PMID:2932655 Niebroj-Dobosz I, et al. (1985) Lipid storage myopathy in Kearns-Sayre syndrome. Neurology 35(11):1582-6
PMID:2932640 Trevisan CP, et al. (1985) Beta-oxidation enzymes in normal human muscle and in muscle from a patient with an unusual form of myopathic carnitine deficiency. Muscle Nerve 8(8):672-5
PMID:1543733 Shimomura I, et al. (1992) Marked enhancement of acyl-CoA synthetase activity and mRNA, paralleled to lipoprotein lipase mRNA, in adipose tissues of Zucker obese rats (fa/fa). Biochim Biophys Acta 1124(2):112-8
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