ID Q5ICG6_MOUSE Unreviewed; 722 AA. AC Q5ICG6; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 22-FEB-2023, entry version 75. DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|RuleBase:RU369030}; DE EC=6.2.1.15 {ECO:0000256|RuleBase:RU369030}; DE EC=6.2.1.3 {ECO:0000256|RuleBase:RU369030}; DE AltName: Full=Acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030}; DE AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030}; GN Name=Acsl6 {ECO:0000313|MGI:MGI:894291}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAW33884.1}; RN [1] {ECO:0000313|EMBL:AAW33884.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:AAW33884.1}; RX PubMed=15629433; DOI=10.1016/j.bbrc.2004.11.141; RA Lee E.J., Kim H.C., Cho Y.Y., Byun S.J., Lim J.M., Ryoo Z.Y.; RT "Alternative promotion of the mouse acyl-CoA synthetase 6 (mAcsl6) gene RT mediates the expression of multiple transcripts with 5'-end heterogeneity: RT genetic organization of mAcsl6 variants."; RL Biochem. Biophys. Res. Commun. 327:84-93(2005). CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their CC active form acyl-CoAs for both synthesis of cellular lipids, and CC degradation via beta-oxidation. {ECO:0000256|RuleBase:RU369030}. 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:0000256|ARBA:ARBA00024548, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; CC Evidence={ECO:0000256|ARBA:ARBA00024548, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024565, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; CC Evidence={ECO:0000256|ARBA:ARBA00024565, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024495, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; CC Evidence={ECO:0000256|ARBA:ARBA00024495, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024532, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; CC Evidence={ECO:0000256|ARBA:ARBA00024532, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024469, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; CC Evidence={ECO:0000256|ARBA:ARBA00024469, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024497, CC ECO:0000256|RuleBase:RU369030}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; CC Evidence={ECO:0000256|ARBA:ARBA00024497, CC ECO:0000256|RuleBase:RU369030}; 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:0000256|ARBA:ARBA00024484}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; CC Evidence={ECO:0000256|ARBA:ARBA00024484}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein CC {ECO:0000256|ARBA:ARBA00004643}. Membrane CC {ECO:0000256|ARBA:ARBA00004183}; Single-pass type III membrane protein CC {ECO:0000256|ARBA:ARBA00004183}. Mitochondrion outer membrane CC {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein CC {ECO:0000256|RuleBase:RU369030}. Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein CC {ECO:0000256|RuleBase:RU369030}. Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00025703}; Single-pass type III membrane protein CC {ECO:0000256|ARBA:ARBA00025703}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY786361; AAW33884.1; -; mRNA. DR AlphaFoldDB; Q5ICG6; -. DR PeptideAtlas; Q5ICG6; -. DR AGR; MGI:894291; -. DR MGI; MGI:894291; Acsl6. DR ChiTaRS; Acsl6; mouse. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer 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; IEA:InterPro. DR CDD; cd05927; LC-FACS_euk; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. 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 Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|RuleBase:RU369030}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, KW ECO:0000256|RuleBase:RU369030}; Ligase {ECO:0000256|RuleBase:RU369030}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU369030}; Membrane {ECO:0000256|RuleBase:RU369030}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030}; KW Transmembrane {ECO:0000256|RuleBase:RU369030}; KW Transmembrane helix {ECO:0000256|RuleBase:RU369030}. FT TRANSMEM 47..69 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU369030" FT DOMAIN 141..587 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 597..657 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 722 AA; 80776 MW; B7DD494A0468660B CRC64; MLTFFLVSGG SLWLFAEIAL SLLEKMQTQE ILRILRLPEL SDLGQFFRSL SATTLVSVGA LAAVLAYWLT HRPKALQPPC NLLKQSEEVE DGGGARRSVI GGCTQLLTHY YDDARTMYQV FRRGLSISGN GPCLGFRKPE QPYQWLSYQE VAKRAEFLGS GLLQHDCKVG TEQFVGVFAQ NRPEWIIAEL ACYTYSMVVV PLYDTLGPGS ISYIINTADI CTVIVDKPHK ATLLLEHVER KETPGLKLVI LMEPFEDALR ERGKKCGVDI KSMQAIEDCG RENHHAPVPP RPDDLSIVCF TSGTTGNPKG AMLTHGNVVA DFSGFLKVTE KVIFPRQDDV LISFLPLAHM FERVIQSVVY CHGGRVGFFQ GDIRLLSDDM KALRPTIFSV VPRLLNRMYD KIFHQADTSL KRWLLEFAAK RKQAEVRSGI IRNNSIWDEL FFNKIQASLG GHVRMIVTGA APASPTVLGF LRAALGCQVY EGYGQTECTA GCTFTTPGDW TSGHVGAPLP CNHIKLVDAE ELNYWTCKGE GEICVKGPNV FKGYLKDEDR TKEALDSDGW LHTGDIGKWL PEGTLKIIDR KKHIFKLAQG EYVAPEKIEN IYIRSEPVAQ IYVHGDSLKA FLVGIVVPDP EVMPSWAQKK GIEGTYQELC MKKELKKAIL DDMVMLGKES GLHSFEQVKA IYIHCDMFSV QNGLLTPTLK AKRPELREYF KKQIEELYLV SV //