ID B8JK22_DANRE Unreviewed; 697 AA. AC B8JK22; A0A8M2BFN5; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|RuleBase:RU369030}; DE EC=6.2.1.3 {ECO:0000256|RuleBase:RU369030}; GN Name=acsl1a {ECO:0000313|Ensembl:ENSDARP00000039916, GN ECO:0000313|RefSeq:XP_005168406.1, GN ECO:0000313|ZFIN:ZDB-GENE-050809-115}; GN Synonyms=acsl1 {ECO:0000313|RefSeq:XP_005168406.1}, zgc:110081 GN {ECO:0000313|RefSeq:XP_005168406.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000039916}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000105676} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105676}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000039916, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000039916}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [3] {ECO:0000313|Ensembl:ENSDARP00000039916} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000039916}; RG Ensembl; RL Submitted (AUG-2013) to UniProtKB. RN [4] {ECO:0000313|RefSeq:XP_005168406.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005168406.1}; RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; CC Evidence={ECO:0000256|ARBA:ARBA00024548}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; CC Evidence={ECO:0000256|ARBA:ARBA00024565}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; CC Evidence={ECO:0000256|ARBA:ARBA00024495}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; CC Evidence={ECO:0000256|ARBA:ARBA00024532}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; CC Evidence={ECO:0000256|ARBA:ARBA00024469}; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; CC Evidence={ECO:0000256|ARBA:ARBA00024497}; 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 -!- 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; BX537280; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005168406.1; XM_005168349.4. DR STRING; 7955.ENSDARP00000039916; -. DR PaxDb; 7955-ENSDARP00000039916; -. DR Ensembl; ENSDART00000039917.7; ENSDARP00000039916.5; ENSDARG00000030514.8. DR Ensembl; ENSDART00000125125.3; ENSDARP00000105676.1; ENSDARG00000030514.8. DR Ensembl; ENSDART00000188775.1; ENSDARP00000148605.1; ENSDARG00000109220.1. DR GeneID; 555308; -. DR AGR; ZFIN:ZDB-GENE-050809-115; -. DR CTD; 555308; -. DR ZFIN; ZDB-GENE-050809-115; acsl1a. DR eggNOG; KOG1256; Eukaryota. DR HOGENOM; CLU_000022_45_4_1; -. DR OMA; HVYGLMI; -. DR OrthoDB; 443463at2759; -. DR TreeFam; TF313877; -. DR Proteomes; UP000000437; Chromosome 1. DR Bgee; ENSDARG00000030514; Expressed in cardiac ventricle and 24 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central. DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IBA:GO_Central. 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:SF28; LONG-CHAIN-FATTY-ACID--COA LIGASE 1; 1. DR Pfam; PF00501; AMP-binding; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|RuleBase:RU369030}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, KW ECO:0000256|RuleBase:RU369030}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU369030}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU369030}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030}; KW Proteomics identification {ECO:0007829|PeptideAtlas:B8JK22}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21..45 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 117..519 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" SQ SEQUENCE 697 AA; 77439 MW; 688EBD2CC4C96816 CRC64; MQAQDLIRHL RMPELDDLRQ YVRSLPTNTL MGMGAFAAIT TYWLATRPKA LKPPCDLTMQ SVEVPGKEYA RRSILMDNDT HMTYYYKDAL TLYEFFLRGL RVSNNGPCLG SRKAGQPYKW LSYKEVADRA EFAGSALLHR GHSQSGDKYI GIFAQNRPEW TISELACYTY SLVAVPLYDT LGTEAISYVI DKASITTIIC DIADKARLIL DCVSGRKHSV TTIVIMESFD SELTAQAQNC GIDIISLKEL EAIGKANHKT PIPPKPEDLA LICFTSGTTG NPKGAMLTHG NVVSNCSAFI KITEVHCMLN QTDIHISYLP LAHMFERVVE GVLLCHGAKI GYFQGDIRLL MDDLKNLKPT IFPVVPRLLN RMFDKIFGQA NTPLKRWLLD FATSRKEAEL KSGVVRKDSM WDKLIFSKVQ ASLGGRVRLM ITGAAPVSPT VLTFLRAALG CQFYEGYGQT ECTAGCTMSL PGDWTAGHVG APLPCNFVKL VDVAEMNYFA ANGEGEVCVK GPNVFQGYLK DPEQTSGAVD KAGWLHTGDI GKWLPNGTLK IIDRKKHIFK LAQGEYIAPE KIENIYIRSD PVAQVFVHGD SLQACLVGVV VPDPDFLPGW AKNRGIEGSF NDLCKSKEVK NAILEDMIQL GKEAGLKSFE QVRDIALHLE MFSVQNGLLT PTLKAKRTEL KSRFREQIDQ LYAKIKM //