ID   ACSL6_HUMAN             Reviewed;         697 AA.
AC   Q9UKU0; J3KPG3; O94924; O95829; Q108M9; Q108N0; Q4G191; Q86TN7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 4.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 6 {ECO:0000305};
DE            EC=6.2.1.3 {ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000305};
DE            EC=6.2.1.15 {ECO:0000250|UniProtKB:P33124};
DE   AltName: Full=Long-chain acyl-CoA synthetase 6;
DE            Short=LACS 6;
GN   Name=ACSL6 {ECO:0000312|HGNC:HGNC:16496};
GN   Synonyms=ACS2, FACL6, KIAA0837, LACS5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX   PubMed=10548543; DOI=10.1042/bj3440135;
RA   Malhotra K.T., Malhotra K., Lubin B.H., Kuypers F.A.;
RT   "Identification and molecular characterization of acyl-CoA synthetase in
RT   human red cells and erythroid precursor.";
RL   Biochem. J. 344:135-143(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHROMOSOMAL TRANSLOCATION WITH
RP   ETV6.
RC   TISSUE=Bone marrow;
RX   PubMed=10502316;
RX   DOI=10.1002/(sici)1098-2264(199911)26:3<192::aid-gcc2>3.0.co;2-e;
RA   Yagasaki F., Jinnai I., Yoshida S., Yokoyama Y., Matsuda A., Kusumoto S.,
RA   Kobayashi H., Terasaki H., Ohyashiki K., Asou N., Murohashi I., Bessho M.,
RA   Hirashima K.;
RT   "Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute
RT   myelogenous leukemia with t(5;12)(q31;p13).";
RL   Genes Chromosomes Cancer 26:192-202(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   253-374 (ISOFORM 5), AND ALTERNATIVE SPLICING (ISOFORM 8).
RX   PubMed=16834775; DOI=10.1186/1471-2199-7-21;
RA   Soupene E., Kuypers F.A.;
RT   "Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are
RT   produced by switch of the fatty acid gate domains.";
RL   BMC Mol. Biol. 7:21-21(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:355-364(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORM 8).
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC   TISSUE=Testis;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=22633490; DOI=10.1016/j.molcel.2012.04.033;
RA   Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., Ohno Y.,
RA   Zoeller R.A., Kihara A.;
RT   "The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of
RT   the sphingosine 1-phosphate degradation pathway.";
RL   Mol. Cell 46:461-471(2012).
RN   [9]
RP   CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24269233; DOI=10.1016/j.bbrc.2013.11.036;
RA   Ohkuni A., Ohno Y., Kihara A.;
RT   "Identification of acyl-CoA synthetases involved in the mammalian
RT   sphingosine 1-phosphate metabolic pathway.";
RL   Biochem. Biophys. Res. Commun. 442:195-201(2013).
CC   -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC       active form acyl-CoA for both synthesis of cellular lipids, and
CC       degradation via beta-oxidation (PubMed:22633490, PubMed:24269233).
CC       Plays an important role in fatty acid metabolism in brain and the acyl-
CC       CoAs produced may be utilized exclusively for the synthesis of the
CC       brain lipid. {ECO:0000269|PubMed:22633490,
CC       ECO:0000269|PubMed:24269233}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000305|PubMed:22633490, ECO:0000305|PubMed:24269233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC         ChEBI:CHEBI:456215; EC=6.2.1.15;
CC         Evidence={ECO:0000250|UniProtKB:P33124};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000250|UniProtKB:P33124};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:24269233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000305|PubMed:24269233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC         ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:22633490, ECO:0000269|PubMed:24269233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000305|PubMed:22633490, ECO:0000305|PubMed:24269233};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-
CC         hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P33124};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC         Evidence={ECO:0000250|UniProtKB:P33124};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-
CC         hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P33124};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC         Evidence={ECO:0000250|UniProtKB:P33124};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-
CC         hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P33124};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC         Evidence={ECO:0000250|UniProtKB:P33124};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- INTERACTION:
CC       Q9UKU0-7; Q9NV79: PCMTD2; NbExp=3; IntAct=EBI-12883224, EBI-6309018;
CC       Q9UKU0-7; Q8N720: ZNF655; NbExp=3; IntAct=EBI-12883224, EBI-625509;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}. Peroxisome
CC       membrane {ECO:0000250}; Single-pass type III membrane protein
CC       {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=4;
CC         IsoId=Q9UKU0-4; Sequence=Displayed;
CC       Name=1; Synonyms=Long, v2;
CC         IsoId=Q9UKU0-1; Sequence=VSP_037819;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q9UKU0-2; Sequence=VSP_021024, VSP_000241;
CC       Name=3;
CC         IsoId=Q9UKU0-3; Sequence=VSP_021024;
CC       Name=5; Synonyms=v4;
CC         IsoId=Q9UKU0-5; Sequence=VSP_037823;
CC       Name=6; Synonyms=v5;
CC         IsoId=Q9UKU0-6; Sequence=VSP_037821;
CC       Name=7; Synonyms=v3;
CC         IsoId=Q9UKU0-7; Sequence=VSP_037820, VSP_037822;
CC       Name=8; Synonyms=v1;
CC         IsoId=Q9UKU0-8; Sequence=VSP_037819, VSP_021024;
CC       Name=9;
CC         IsoId=Q9UKU0-9; Sequence=VSP_046954;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in erythrocyte precursors,
CC       in particular in reticulocytes, fetal blood cells derived from fetal
CC       liver, hemopoietic stem cells from cord blood, bone marrow and brain.
CC       {ECO:0000269|PubMed:10548543}.
CC   -!- DEVELOPMENTAL STAGE: Expression is low at earlier stages of erythroid
CC       development but is very high in reticulocytes.
CC   -!- DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause
CC       of myelodysplastic syndrome with basophilia. Translocation
CC       t(5;12)(q31;p13) with ETV6. {ECO:0000269|PubMed:10502316}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause
CC       of acute myelogenous leukemia with eosinophilia. Translocation
CC       t(5;12)(q31;p13) with ETV6. {ECO:0000269|PubMed:10502316}.
CC   -!- DISEASE: Note=A chromosomal aberration involving ACSL6 may be a cause
CC       of acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13)
CC       with ETV6. {ECO:0000269|PubMed:10502316}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26161.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA74860.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF129166; AAD47199.1; -; mRNA.
DR   EMBL; AF099740; AAD17853.1; -; mRNA.
DR   EMBL; DQ083030; AAZ30713.1; -; mRNA.
DR   EMBL; DQ083031; AAZ30714.1; -; mRNA.
DR   EMBL; AB020644; BAA74860.1; ALT_INIT; mRNA.
DR   EMBL; CR606980; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC025772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC034228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026161; AAH26161.1; ALT_SEQ; mRNA.
DR   EMBL; BC047453; AAH47453.1; -; mRNA.
DR   CCDS; CCDS34228.1; -. [Q9UKU0-8]
DR   CCDS; CCDS34229.1; -. [Q9UKU0-1]
DR   CCDS; CCDS56381.1; -. [Q9UKU0-3]
DR   CCDS; CCDS56382.1; -. [Q9UKU0-7]
DR   CCDS; CCDS56383.1; -. [Q9UKU0-9]
DR   RefSeq; NP_001009185.1; NM_001009185.2. [Q9UKU0-1]
DR   RefSeq; NP_001192176.1; NM_001205247.1.
DR   RefSeq; NP_001192177.1; NM_001205248.1. [Q9UKU0-3]
DR   RefSeq; NP_001192179.1; NM_001205250.1. [Q9UKU0-9]
DR   RefSeq; NP_001192180.1; NM_001205251.1. [Q9UKU0-7]
DR   RefSeq; NP_056071.2; NM_015256.3. [Q9UKU0-8]
DR   AlphaFoldDB; Q9UKU0; -.
DR   SMR; Q9UKU0; -.
DR   BioGRID; 116897; 10.
DR   IntAct; Q9UKU0; 5.
DR   STRING; 9606.ENSP00000498260; -.
DR   BindingDB; Q9UKU0; -.
DR   ChEMBL; CHEMBL4680042; -.
DR   SwissLipids; SLP:000000203; -.
DR   iPTMnet; Q9UKU0; -.
DR   PhosphoSitePlus; Q9UKU0; -.
DR   BioMuta; ACSL6; -.
DR   DMDM; 146322303; -.
DR   EPD; Q9UKU0; -.
DR   jPOST; Q9UKU0; -.
DR   MassIVE; Q9UKU0; -.
DR   MaxQB; Q9UKU0; -.
DR   PaxDb; 9606-ENSP00000368566; -.
DR   PeptideAtlas; Q9UKU0; -.
DR   ProteomicsDB; 84870; -. [Q9UKU0-4]
DR   ProteomicsDB; 84871; -. [Q9UKU0-1]
DR   ProteomicsDB; 84872; -. [Q9UKU0-2]
DR   ProteomicsDB; 84873; -. [Q9UKU0-3]
DR   ProteomicsDB; 84874; -. [Q9UKU0-5]
DR   ProteomicsDB; 84875; -. [Q9UKU0-6]
DR   ProteomicsDB; 84876; -. [Q9UKU0-7]
DR   ProteomicsDB; 84877; -. [Q9UKU0-8]
DR   Antibodypedia; 25915; 228 antibodies from 29 providers.
DR   DNASU; 23305; -.
DR   Ensembl; ENST00000357096.5; ENSP00000349608.1; ENSG00000164398.15. [Q9UKU0-7]
DR   Ensembl; ENST00000379240.5; ENSP00000368542.1; ENSG00000164398.15. [Q9UKU0-4]
DR   Ensembl; ENST00000379244.5; ENSP00000368546.1; ENSG00000164398.15. [Q9UKU0-3]
DR   Ensembl; ENST00000379246.5; ENSP00000368548.1; ENSG00000164398.15. [Q9UKU0-9]
DR   Ensembl; ENST00000379255.5; ENSP00000368557.1; ENSG00000164398.15. [Q9UKU0-7]
DR   Ensembl; ENST00000543479.5; ENSP00000442124.2; ENSG00000164398.15. [Q9UKU0-6]
DR   Ensembl; ENST00000651356.1; ENSP00000498260.1; ENSG00000164398.15. [Q9UKU0-8]
DR   Ensembl; ENST00000651883.2; ENSP00000499063.2; ENSG00000164398.15. [Q9UKU0-1]
DR   GeneID; 23305; -.
DR   KEGG; hsa:23305; -.
DR   MANE-Select; ENST00000651883.2; ENSP00000499063.2; NM_001009185.3; NP_001009185.1. [Q9UKU0-1]
DR   UCSC; uc003kvv.3; human. [Q9UKU0-4]
DR   AGR; HGNC:16496; -.
DR   CTD; 23305; -.
DR   DisGeNET; 23305; -.
DR   GeneCards; ACSL6; -.
DR   HGNC; HGNC:16496; ACSL6.
DR   HPA; ENSG00000164398; Tissue enhanced (bone marrow, brain, retina).
DR   MIM; 604443; gene.
DR   neXtProt; NX_Q9UKU0; -.
DR   OpenTargets; ENSG00000164398; -.
DR   PharmGKB; PA27970; -.
DR   VEuPathDB; HostDB:ENSG00000164398; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   GeneTree; ENSGT00940000162308; -.
DR   HOGENOM; CLU_000022_45_4_1; -.
DR   InParanoid; Q9UKU0; -.
DR   OMA; PRIWTKF; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; Q9UKU0; -.
DR   TreeFam; TF313877; -.
DR   BioCyc; MetaCyc:HS15193-MONOMER; -.
DR   BRENDA; 6.2.1.3; 2681.
DR   PathwayCommons; Q9UKU0; -.
DR   Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   SignaLink; Q9UKU0; -.
DR   BioGRID-ORCS; 23305; 6 hits in 1149 CRISPR screens.
DR   ChiTaRS; ACSL6; human.
DR   GeneWiki; ACSL6; -.
DR   GenomeRNAi; 23305; -.
DR   Pharos; Q9UKU0; Tbio.
DR   PRO; PR:Q9UKU0; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9UKU0; Protein.
DR   Bgee; ENSG00000164398; Expressed in lateral nuclear group of thalamus and 140 other cell types or tissues.
DR   ExpressionAtlas; Q9UKU0; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR   GO; GO:0047676; F:arachidonate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; NAS:UniProtKB.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF54; LONG-CHAIN-FATTY-ACID--COA LIGASE 6; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; Q9UKU0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chromosomal rearrangement;
KW   Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Magnesium; Membrane; Microsome; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..697
FT                   /note="Long-chain-fatty-acid--CoA ligase 6"
FT                   /id="PRO_0000193115"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..697
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MLTFFLVSGGSLWLFVEFVLSLLEKM (in isoform 1 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10048485"
FT                   /id="VSP_037819"
FT   VAR_SEQ         1
FT                   /note="M -> MPEFVLSLLEKM (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046954"
FT   VAR_SEQ         31..65
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037820"
FT   VAR_SEQ         192
FT                   /note="T -> TGLSCQEGASATASTQ (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16834775"
FT                   /id="VSP_037821"
FT   VAR_SEQ         306..345
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_037822"
FT   VAR_SEQ         306..330
FT                   /note="KVIFPRQDDVLISFLPLAHMFERVI -> SQWAPTCADVHISYLPLAHMFER
FT                   MV (in isoform 3, isoform 2 and isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:10502316,
FT                   ECO:0000303|PubMed:10548543"
FT                   /id="VSP_021024"
FT   VAR_SEQ         306..312
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16834775"
FT                   /id="VSP_037823"
FT   VAR_SEQ         653..697
FT                   /note="VKAIHIHSDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYSISM -> DLP
FT                   QCLIQIKVFSKY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10502316"
FT                   /id="VSP_000241"
FT   CONFLICT        19
FT                   /note="G -> E (in Ref. 1; AAD47199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="H -> Q (in Ref. 1; AAD47199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="E -> A (in Ref. 7; AAH47453)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="Q -> L (in Ref. 7; AAH26161)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="K -> R (in Ref. 3; AAZ30714)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696
FT                   /note="S -> P (in Ref. 1; AAD47199 and 3; AAZ30714)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   697 AA;  77752 MW;  AC566177B47D0975 CRC64;
     MQTQEILRIL RLPELGDLGQ FFRSLSATTL VSMGALAAIL AYWFTHRPKA LQPPCNLLMQ
     SEEVEDSGGA RRSVIGSGPQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPKQPYQW
     LSYQEVADRA EFLGSGLLQH NCKACTDQFI GVFAQNRPEW IIVELACYTY SMVVVPLYDT
     LGPGAIRYII NTADISTVIV DKPQKAVLLL EHVERKETPG LKLIILMDPF EEALKERGQK
     CGVVIKSMQA VEDCGQENHQ APVPPQPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF
     LKVTEKVIFP RQDDVLISFL PLAHMFERVI QSVVYCHGGR VGFFQGDIRL LSDDMKALCP
     TIFPVVPRLL NRMYDKIFSQ ANTPLKRWLL EFAAKRKQAE VRSGIIRNDS IWDELFFNKI
     QASLGGCVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV
     GAPLPCNHIK LVDVEELNYW ACKGEGEICV RGPNVFKGYL KDPDRTKEAL DSDGWLHTGD
     IGKWLPAGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS QPVAQIYVHG DSLKAFLVGI
     VVPDPEVMPS WAQKRGIEGT YADLCTNKDL KKAILEDMVR LGKESGLHSF EQVKAIHIHS
     DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM
//