ID   Q108N1_HUMAN            Unreviewed;       373 AA.
AC   Q108N1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00026121};
DE            EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE   Flags: Fragment;
GN   Name=ACSL1 {ECO:0000313|EMBL:AAZ30712.1};
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 {ECO:0000313|EMBL:AAZ30712.1};
RN   [1] {ECO:0000313|EMBL:AAZ30712.1}
RP   NUCLEOTIDE SEQUENCE.
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).
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DR   EMBL; DQ083029; AAZ30712.1; -; mRNA.
DR   AlphaFoldDB; Q108N1; -.
DR   PeptideAtlas; Q108N1; -.
DR   ChiTaRS; ACSL1; human.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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   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   2: Evidence at transcript level;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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          116..373
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   NON_TER         373
FT                   /evidence="ECO:0000313|EMBL:AAZ30712.1"
SQ   SEQUENCE   373 AA;  41562 MW;  29B468724F338C76 CRC64;
     MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
     SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
     LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
     LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR
     CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF
     VKATEKALPL SASDTHISYL PLAHIYEQLL KCVMLCHGAK IGFFQGDIRL LMDDLKVLQP
     TVFPVVPRLL NRM
//