LOCUS       NP_446075                670 aa            linear   ROD 05-MAY-2025
DEFINITION  long-chain-fatty-acid--CoA ligase 4 isoform 2 [Rattus norvegicus].
ACCESSION   NP_446075
VERSION     NP_446075.1
DBSOURCE    REFSEQ: accession NM_053623.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Zhou,J., Tang,J., Zhang,C., Li,G., Lin,X., Liao,S., Luo,J., Yu,G.,
            Zheng,F., Guo,Z., Shao,W., Hu,H., Xu,L., Wu,S. and Li,H.
  TITLE     ALKBH5 targets ACSL4 mRNA stability to modulate ferroptosis in
            hyperbilirubinemia-induced brain damage
  JOURNAL   Free Radic Biol Med 220, 271-287 (2024)
   PUBMED   38734267
  REMARK    GeneRIF: ALKBH5 targets ACSL4 mRNA stability to modulate
            ferroptosis in hyperbilirubinemia-induced brain damage.
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Wang,Y., Zhang,G., Gao,Y., Zhang,X. and Qi,H.
  TITLE     METTL3 promotes trophoblast ferroptosis in preeclampsia by
            stabilizing the ACSL4 m6A modification
  JOURNAL   Exp Cell Res 437 (1), 113990 (2024)
   PUBMED   38462207
  REMARK    GeneRIF: METTL3 promotes trophoblast ferroptosis in preeclampsia by
            stabilizing the ACSL4 m[6]A modification.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Qiu,M., Yan,W. and Liu,M.
  TITLE     YAP Facilitates NEDD4L-Mediated Ubiquitination and Degradation of
            ACSL4 to Alleviate Ferroptosis in Myocardial Ischemia-Reperfusion
            Injury
  JOURNAL   Can J Cardiol 39 (11), 1712-1727 (2023)
   PUBMED   37541340
  REMARK    GeneRIF: YAP Facilitates NEDD4L-Mediated Ubiquitination and
            Degradation of ACSL4 to Alleviate Ferroptosis in Myocardial
            Ischemia-Reperfusion Injury.
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Qu,X.F., Liang,T.Y., Wu,D.G., Lai,N.S., Deng,R.M., Ma,C., Li,X.,
            Li,H.Y., Liu,Y.Z., Shen,H.T. and Chen,G.
  TITLE     Acyl-CoA synthetase long chain family member 4 plays detrimental
            role in early brain injury after subarachnoid hemorrhage in rats by
            inducing ferroptosis
  JOURNAL   CNS Neurosci Ther 27 (4), 449-463 (2021)
   PUBMED   33314758
  REMARK    GeneRIF: Acyl-CoA synthetase long chain family member 4 plays
            detrimental role in early brain injury after subarachnoid
            hemorrhage in rats by inducing ferroptosis.
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Dattilo,M.A., Benzo,Y., Herrera,L.M., Prada,J.G., Lopez,P.F.,
            Caruso,C.M., Lasaga,M., Garcia,C.I., Paz,C. and Maloberti,P.M.
  TITLE     Regulation and role of Acyl-CoA synthetase 4 in glial cells
  JOURNAL   J Steroid Biochem Mol Biol 208, 105792 (2021)
   PUBMED   33246155
  REMARK    GeneRIF: Regulation and role of Acyl-CoA synthetase 4 in glial
            cells.
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Lewin,T.M., Kim,J.H., Granger,D.A., Vance,J.E. and Coleman,R.A.
  TITLE     Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different
            subcellular membranes in rat liver and can be inhibited
            independently
  JOURNAL   J Biol Chem 276 (27), 24674-24679 (2001)
   PUBMED   11319232
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Kim,J.H., Lewin,T.M. and Coleman,R.A.
  TITLE     Expression and characterization of recombinant rat Acyl-CoA
            synthetases 1, 4, and 5. Selective inhibition by triacsin C and
            thiazolidinediones
  JOURNAL   J Biol Chem 276 (27), 24667-24673 (2001)
   PUBMED   11319222
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Li,Z., Jiang,H., Xie,W., Zhang,Z., Smrcka,A.V. and Wu,D.
  TITLE     Roles of PLC-beta2 and -beta3 and PI3Kgamma in
            chemoattractant-mediated signal transduction
  JOURNAL   Science 287 (5455), 1046-1049 (2000)
   PUBMED   10669417
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Cao,Y., Traer,E., Zimmerman,G.A., McIntyre,T.M. and Prescott,S.M.
  TITLE     Cloning, expression, and chromosomal localization of human
            long-chain fatty acid-CoA ligase 4 (FACL4)
  JOURNAL   Genomics 49 (2), 327-330 (1998)
   PUBMED   9598324
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Kang,M.J., Fujino,T., Sasano,H., Minekura,H., Yabuki,N., Nagura,H.,
            Iijima,H. and Yamamoto,T.T.
  TITLE     A novel arachidonate-preferring acyl-CoA synthetase is present in
            steroidogenic cells of the rat adrenal, ovary, and testis
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 2880-2884 (1997)
   PUBMED   9096315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000021.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D85189.1, SRR26643296.40885.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760400 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="X"
                     /map="Xq33"
     Protein         1..670
                     /product="long-chain-fatty-acid--CoA ligase 4 isoform 2"
                     /EC_number="6.2.1.3"
                     /EC_number="6.2.1.15"
                     /note="long-chain-fatty-acid--CoA ligase 4; LACS 4;
                     long-chain acyl-CoA synthetase 4; fatty acid-Coenzyme A
                     ligase, long chain 4; arachidonate--CoA ligase"
                     /calculated_mol_wt=74196
     Region          80..655
                     /region_name="LC_FACS_euk1"
                     /note="Eukaryotic long-chain fatty acid CoA synthetase
                     (LC-FACS), including fungal proteins; cd17639"
                     /db_xref="CDD:341294"
     Site            order(234,237..242,244..245)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341294"
     Site            order(237,362..363,423..428,514,526,529,541,647)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341294"
     Site            order(237,278..279,333,335..336,339,362..363,423..428,514,
                     526,529,538..541,624)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341294"
     Site            order(278,335..336,339,362,538..540,622,624)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341294"
     CDS             1..670
                     /gene="Acsl4"
                     /gene_synonym="Acs4; Facl4"
                     /coded_by="NM_053623.2:174..2186"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:113976"
                     /db_xref="RGD:69401"
ORIGIN      
        1 makrikakpt sdkpgspyrs vthfdslavi dipgadtldk lfdhavakfg kkdslgtrei
       61 lseenemqpn gkvfkklilg nykwinylev ncrvnnfgsg ltalglkpkn tiaifcetra
      121 ewmiaaqtcf kynfplvtly atlgkeavvh glneseasyl itsvellesk lkaalldinc
      181 vkhiiyvdnk tinraeypeg leihsmqsve elgskpenss ippsrptpsd maivmytsgs
      241 tgrpkgvmmh hsnliagmtg qceripglgp kdtyigylpl ahvleltaei scftygcrig
      301 ysspltlsdq sskikkgskg dctvlkptlm aavpeimdri yknvmskvqe mnyiqktlfk
      361 igydykleqi kkgydaplcn lilfkkvkal lggnvrmmls ggaplspqth rfmnvcfccp
      421 igqgygltes cgagtvtevt dyttgrvgap licceiklkd wqeggytvhd kpnprgeivi
      481 ggqnismgyf kneektaedy svdengqrwf ctgdigefhp dgclqiidrk kdlvklqage
      541 yvslgkveaa lkncplidni cafaksdqsy visfvvpnqk kltllaqqkg vegswvdicn
      601 npameaeilk eireaanamk lerfeipikv rlspepwtpe tglvtdafkl krkelknhyl
      661 kdiermyggk
//
