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Fatty acyl-CoA reductase 1 (EC 1.2.1.84)

 FACR1_MOUSE             Reviewed;         515 AA.
Q922J9; Q8BZS2; Q9CXE8; Q9D0Q1; Q9DAU2;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
13-FEB-2019, entry version 135.
RecName: Full=Fatty acyl-CoA reductase 1 {ECO:0000305|PubMed:15220348};
EC=1.2.1.84 {ECO:0000269|PubMed:15220348};
Name=Far1 {ECO:0000312|MGI:MGI:1914670};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Cecum, Embryo, Liver, Placenta, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15220348; DOI=10.1074/jbc.M406225200;
Cheng J.B., Russell D.W.;
"Mammalian wax biosynthesis: I. Identification of two fatty acyl-
coenzyme A reductases with different substrate specificities and
tissue distributions.";
J. Biol. Chem. 279:37789-37797(2004).
[4]
FUNCTION.
PubMed=15220349; DOI=10.1074/jbc.M406226200;
Cheng J.B., Russell D.W.;
"Mammalian wax biosynthesis. II. Expression cloning of wax synthase
cDNAs encoding a member of the acyltransferase enzyme family.";
J. Biol. Chem. 279:37798-37807(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Catalyzes the reduction of saturated and unsaturated C16
or C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348,
PubMed:15220349). It plays an essential role in the production of
ether lipids/plasmalogens which synthesis requires fatty alcohols
(By similarity). In parallel, it is also required for wax
monoesters production since fatty alcohols also constitute a
substrate for their synthesis (PubMed:15220349).
{ECO:0000250|UniProtKB:Q8WVX9, ECO:0000269|PubMed:15220348,
ECO:0000269|PubMed:15220349}.
-!- CATALYTIC ACTIVITY:
Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-
chain primary fatty alcohol + CoA + 2 NADP(+);
Xref=Rhea:RHEA:52716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77396,
ChEBI:CHEBI:83139; EC=1.2.1.84;
Evidence={ECO:0000269|PubMed:15220348};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:15220348};
-!- SUBUNIT: Interacts with PEX19; PEX19 mediates the targeting of
FAR1 to peroxisomes. {ECO:0000250|UniProtKB:Q8WVX9}.
-!- SUBCELLULAR LOCATION: Peroxisome membrane
{ECO:0000269|PubMed:15220348}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8WVX9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q922J9-1; Sequence=Displayed;
Name=2;
IsoId=Q922J9-2; Sequence=VSP_021678, VSP_021679;
Name=3;
IsoId=Q922J9-3; Sequence=VSP_021680;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q922J9-4; Sequence=VSP_021681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues
examined. Highest expression seen in preputial gland. Expressed in
the brain where large quantities of ether lipids are synthesized.
{ECO:0000269|PubMed:15220348}.
-!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AK005531; BAB24102.1; -; mRNA.
EMBL; AK011187; BAB27453.1; -; mRNA.
EMBL; AK014486; BAB29388.1; -; mRNA.
EMBL; AK033674; BAC28423.1; -; mRNA.
EMBL; AK030067; BAC26766.1; -; mRNA.
EMBL; BC007178; AAH07178.1; -; mRNA.
CCDS; CCDS40093.1; -. [Q922J9-1]
CCDS; CCDS72024.1; -. [Q922J9-3]
RefSeq; NP_001272760.1; NM_001285831.1. [Q922J9-3]
RefSeq; NP_081655.2; NM_027379.3. [Q922J9-1]
RefSeq; XP_006508190.1; XM_006508127.3.
RefSeq; XP_006508191.1; XM_006508128.3.
RefSeq; XP_006508192.1; XM_006508129.3. [Q922J9-1]
RefSeq; XP_006508193.1; XM_006508130.3. [Q922J9-1]
RefSeq; XP_006508194.1; XM_006508131.3. [Q922J9-1]
UniGene; Mm.206919; -.
UniGene; Mm.477631; -.
ProteinModelPortal; Q922J9; -.
BioGrid; 212175; 4.
IntAct; Q922J9; 1.
STRING; 10090.ENSMUSP00000033018; -.
SwissLipids; SLP:000000210; -.
iPTMnet; Q922J9; -.
PhosphoSitePlus; Q922J9; -.
SwissPalm; Q922J9; -.
EPD; Q922J9; -.
jPOST; Q922J9; -.
PaxDb; Q922J9; -.
PeptideAtlas; Q922J9; -.
PRIDE; Q922J9; -.
Ensembl; ENSMUST00000033018; ENSMUSP00000033018; ENSMUSG00000030759. [Q922J9-1]
Ensembl; ENSMUST00000067929; ENSMUSP00000064334; ENSMUSG00000030759. [Q922J9-3]
Ensembl; ENSMUST00000164745; ENSMUSP00000128695; ENSMUSG00000030759. [Q922J9-1]
GeneID; 67420; -.
KEGG; mmu:67420; -.
UCSC; uc009jhn.2; mouse. [Q922J9-2]
UCSC; uc009jho.2; mouse. [Q922J9-1]
UCSC; uc009jhq.2; mouse. [Q922J9-3]
CTD; 84188; -.
MGI; MGI:1914670; Far1.
eggNOG; KOG1221; Eukaryota.
eggNOG; ENOG410XS7R; LUCA.
GeneTree; ENSGT00390000006367; -.
HOGENOM; HOG000261667; -.
HOVERGEN; HBG076152; -.
InParanoid; Q922J9; -.
KO; K13356; -.
OMA; QPYTFYG; -.
OrthoDB; 815047at2759; -.
PhylomeDB; Q922J9; -.
TreeFam; TF313011; -.
BRENDA; 1.2.1.50; 3474.
BRENDA; 1.2.1.84; 3474.
Reactome; R-MMU-8848584; Wax biosynthesis.
ChiTaRS; Far1; mouse.
PRO; PR:Q922J9; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030759; Expressed in 272 organ(s), highest expression level in cardiac ventricle.
ExpressionAtlas; Q922J9; baseline and differential.
Genevisible; Q922J9; MM.
GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:MGI.
GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:MGI.
GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0046474; P:glycerophospholipid biosynthetic process; ISO:MGI.
GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; ISO:MGI.
GO; GO:0010025; P:wax biosynthetic process; IDA:UniProtKB.
CDD; cd09071; FAR_C; 1.
InterPro; IPR026055; FAR.
InterPro; IPR033640; FAR_C.
InterPro; IPR013120; Male_sterile_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR11011; PTHR11011; 1.
Pfam; PF07993; NAD_binding_4; 1.
Pfam; PF03015; Sterile; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Lipid biosynthesis;
Lipid metabolism; Membrane; NADP; Oxidoreductase; Peroxisome;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 515 Fatty acyl-CoA reductase 1.
/FTId=PRO_0000261395.
TOPO_DOM 1 465 Cytoplasmic.
{ECO:0000250|UniProtKB:Q8WVX9}.
TRANSMEM 466 483 Helical. {ECO:0000255}.
TOPO_DOM 484 515 Peroxisomal.
{ECO:0000250|UniProtKB:Q8WVX9}.
REGION 451 507 Necessary and sufficient for PEX19-
mediated localization into peroxisome
membrane. {ECO:0000250|UniProtKB:Q8WVX9}.
VAR_SEQ 242 260 GWIDNFNGPSGLFIAAGKG -> VSSSKLLSSWDSEFQVRT
V (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021678.
VAR_SEQ 261 515 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021679.
VAR_SEQ 319 376 EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKA
PAFLYDIYLRMTGRSPR -> GDYLNHSFKMNPLNQVFRHP
YVKFCSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPW
(in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021680.
VAR_SEQ 515 515 Y -> RRPRI (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_021681.
CONFLICT 35 35 P -> R (in Ref. 1; BAB24102).
{ECO:0000305}.
CONFLICT 364 364 Y -> H (in Ref. 1; BAB24102).
{ECO:0000305}.
SEQUENCE 515 AA; 59435 MW; 6A9E9EF9A2F835A4 CRC64;
MVSIPEYYEG KNILLTGATG FLGKVLLEKL LRSCPRVNSV YVLVRQKAGQ TPQERVEEIL
SSKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEI IIDSTNVIFH CAATVRFNEN
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
PGWIDNFNGP SGLFIAAGKG ILRTMRASNN ALADLVPVDV VVNTSLAAAW YSGVNRPRNI
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTDNVNMLM NQLNPEDKKT
FNIDVRQLHW AEYIENYCMG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY


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Pathways :
WP1006: metapathway biotransformation
WP1020: Fatty Acid Biosynthesis
WP105: Fatty Acid Beta Oxidation 2
WP1061: Fatty Acid Beta Oxidation
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1124: metapathway biotransformation
WP1139: Fatty Acid Biosynthesis
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1212: metapathway biotransformation
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1228: Fatty Acid Biosynthesis
WP1237: Fatty Acid Beta Oxidation
WP1251: metapathway biotransformation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1286: metapathway biotransformation
WP1307: Fatty Acid Beta Oxidation
WP133: Fatty Acid Omega Oxidation
WP1352: Fatty Acid Biosynthesis
WP137: Fatty Acid Biosynthesis, Initial Steps
WP1403: AMPK signaling
WP143: Fatty Acid Beta Oxidation
WP1461: Photosynthetic Carbon Reduction
WP148: Fatty Acid Beta Oxidation 2

Related Genes :
[FAS2 YPL231W P1409] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[FAR1 MLSTD2 UNQ2423/PRO4981] Fatty acyl-CoA reductase 1 (EC 1.2.1.84) (Male sterility domain-containing protein 2)
[FAS2 CPAR2_807400] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[hexB DOTSEDRAFT_181128] Fatty acid synthase beta subunit hexB (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39) (Dothistromin biosynthesis protein hexB)]
[Far1] Fatty acyl-CoA reductase 1 (EC 1.2.1.84)
[ACSM1 BUCS1 LAE MACS1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1) (XL-III) (Xenobiotic/medium-chain fatty acid:CoA ligase XL-3) (XM-ligase 3)
[Acsm1 Bucs1 Lae Macs1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1)
[FAR2 MLSTD1] Fatty acyl-CoA reductase 2 (EC 1.2.1.84) (Male sterility domain-containing protein 1)
[atnF ANIA_07880] Fatty acid synthase subunit alpha (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein F) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41)]
[ACSM2B ACSM2 HYST1046] Acyl-coenzyme A synthetase ACSM2B, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 2B) (Butyrate--CoA ligase 2B) (Butyryl-coenzyme A synthetase 2B) (Middle-chain acyl-CoA synthetase 2B) (Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A)
[fadD13 Rv3089] Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL)
[tesA c0615] Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)
[FAA2 FAM1 YER015W] Long-chain-fatty-acid--CoA ligase 2 (EC 6.2.1.3) (Fatty acid activator 2) (Long-chain acyl-CoA synthetase 2)
[tesA apeA pldC b0494 JW0483] Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I)
[ELOVL5 ELOVL2 PRO0530] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[ACSM1 BUCS1 LAE MACS1] Acyl-coenzyme A synthetase ACSM1, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 1) (Butyrate--CoA ligase 1) (Butyryl-coenzyme A synthetase 1) (Lipoate-activating enzyme) (Middle-chain acyl-CoA synthetase 1)
[fadD oldD b1805 JW1794] Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase)
[Acsl3 Acs3 Facl3] Long-chain-fatty-acid--CoA ligase 3 (EC 6.2.1.3) (Brain acyl-CoA synthetase II) (Long-chain acyl-CoA synthetase 3) (LACS 3)
[Dgat1 Dgat] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[DGAT1 AGRP1 DGAT] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (ACAT-related gene product 1) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[FAR2 MS2 At3g11980 MEC18.1 T21B14.18 T21B14_123] Fatty acyl-CoA reductase 2 (EC 1.2.1.84) (Fatty acid reductase 2) (Male sterility protein 2)
[hexA DOTSEDRAFT_66976] Fatty acid synthase alpha subunit hexA (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Dothistromin biosynthesis protein hexA)]
[FAA1 YOR317W O6136] Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Fatty acid activator 1) (Long-chain acyl-CoA synthetase 1)
[ACSBG2 BGR UNQ2443/PRO5005] Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Bubblegum-related protein) (PRTD-NY3)
[Dgat1 Dgat] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[SCS7 FAH1 YMR272C YM8156.14C] Ceramide very long chain fatty acid hydroxylase SCS7 (Ceramide VLCFA hydroxylase SCS7) (4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.6) (Dihydroceramide fatty acyl 2-hydroxylase SCS7) (EC 1.14.18.7) (Sphingolipid alpha-hydroxylase) (Suppressor of calcium sensitivity 7)
[ACSL5 ACS5 FACL5 UNQ633/PRO1250] Long-chain-fatty-acid--CoA ligase 5 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 5) (LACS 5)
[tgs2 Rv3734c MTV025.082c] Probable diacyglycerol O-acyltransferase tgs2 (TGS2) (Diacylglycerol O-acyltransferase) (DGAT) (EC 2.3.1.20) (Long-chain-alcohol O-fatty-acyltransferase) (EC 2.3.1.75) (Probable triacylglycerol synthase tgs2) (Wax ester synthase/acyl-CoA:diacylglycerol acyltransferase) (Wax synthase) (WS)
[ACSL4 ACS4 FACL4 LACS4] Long-chain-fatty-acid--CoA ligase 4 (EC 6.2.1.3) (Long-chain acyl-CoA synthetase 4) (LACS 4)

Bibliography :
[28272479] Plasmalogen biosynthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet of plasma membranes.
[24108123] Topogenesis and homeostasis of fatty acyl-CoA reductase 1.
[20071337] Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis.
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